2.02012-05-31 10:27:32 -06002015-09-13 12:56:08 -0600ECMDB00574M2MDB000152L-CysteineCysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible: as reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. Oxidation of cysteine can produce a disulfide bond with another thiol, or further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead and cadmium tightly.Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is important in energy metabolism. (http://www.dcnutrition.com/AminoAcids/)(+)-2-Amino-3-mercaptopropionate(+)-2-Amino-3-mercaptopropionic acid(2R)-2-amino-3-mercaptopropanoate(2R)-2-amino-3-mercaptopropanoic acid(2R)-2-amino-3-sulfanylpropanoate(2R)-2-amino-3-sulfanylpropanoic acid(2R)-2-amino-3-sulphanylpropanoate(2R)-2-amino-3-sulphanylpropanoic acid(R)-(+)-cysteine(R)-2-amino-3-mercapto-Propanoate(R)-2-amino-3-mercapto-Propanoic acid(R)-2-Amino-3-mercaptopropanoate(R)-2-Amino-3-mercaptopropanoic acid(R)-cysteine2-Amino-3-mercaptopropanoate2-Amino-3-mercaptopropanoic acid2-Amino-3-mercaptopropionate2-Amino-3-mercaptopropionic acid3-Mercapto-L-Alaninea-amino-b-Thiolpropionatea-amino-b-Thiolpropionic acidAcetylcysteineAlpha-Amino-beta-thiolpropionateAlpha-Amino-beta-thiolpropionic acidB-MercaptoalanineBeta-MercaptoalanineCCarbocysteineCisteinaCisteinumCysCysteinCysteineCysteinumFree cysteineHalf-cystineL CysteineL-(+)-CysteineL-2-Amino-3-mercaptopropanoateL-2-Amino-3-mercaptopropanoic acidL-2-Amino-3-mercaptopropionateL-2-Amino-3-mercaptopropionic acidL-CysteinL-CysteinePolycysteineThioserineα-amino-β-Thiolpropionateα-amino-β-Thiolpropionic acidβ-MercaptoalanineC3H7NO2S121.158121.019749163(2R)-2-amino-3-sulfanylpropanoic acidL-cysteine52-90-4N[C@@H](CS)C(O)=OInChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1XUJNEKJLAYXESH-REOHCLBHSA-NSolidCytosolExtra-organismPeriplasmlogp-2.57logs-0.72solubility2.31e+01 g/lmelting_point220 oClogp-2.8pka_strongest_acidic2.35pka_strongest_basic9.05iupac(2R)-2-amino-3-sulfanylpropanoic acidaverage_mass121.158mono_mass121.019749163smilesN[C@@H](CS)C(O)=OformulaC3H7NO2SinchiInChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1inchikeyXUJNEKJLAYXESH-REOHCLBHSA-Npolar_surface_area63.32refractivity28.22polarizability11.41rotatable_bond_count2acceptor_count3donor_count3physiological_charge0formal_charge0Glutathione metabolismThe biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione.
PW000833ec00480MetabolicCysteine and methionine metabolismec00270Glycine, serine and threonine metabolismec00260Pantothenate and CoA biosynthesisThe CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate.
The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate.
On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine.
Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid.
Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine.
The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA.
Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A.
. The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III.
The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth.
The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06].PW000828ec00770MetabolicSelenoamino acid metabolismec00450Sulfur metabolismThe sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion.
The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described.
The third variant of sulfur metabolism starts with the import of an alkyl sulfate into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. The alkyl sulfate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000922ec00920MetabolicAminoacyl-tRNA biosynthesisec00970Taurine and hypotaurine metabolismec00430Thiamine metabolismec00730Microbial metabolism in diverse environmentsec01120Sulfur relay systemec04122Metabolic pathwayseco01100L-alanine metabolismL-alanine is an essential component of proteins and peptidoglycan. The latter also contains about three molecules of D-alanine for every L-alanine. Only about 10 percent of the total alanine synthesized flows into peptidoglycan.
There are at least 3 ways to begin the biosynthesis of alanine.
The first method for alanine biosynthesis begins with L-cysteine produced from L-cysteine biosynthesis pathway. L-cysteine reacts with an [L-cysteine desulfurase] L-cysteine persulfide through a cysteine desulfurase resulting in a release of [L-cysteine desulfurase] l-cysteine persulfide and L-alanine.
The second method starts with pyruvic acid reacting with L-glutamic acid through a glutamate-pyruvate aminotransferase resulting in a oxoglutaric acid and L-alanine.
The third method starts with L-glutamic acid interacting with Alpha-ketoisovaleric acid through a valine transaminase resulting in an oxoglutaric acid and L-valine. L-valine reacts with pyruvic acid through a valine-pyruvate aminotransferase resulting Alpha-ketoisovaleric acid and L-alanine.
This first step of the pathway, which can be catalyzed by either of two racemases( biosynthetic or catabolic), also serves an essential role in biosynthesis because its product, D-alanine, is an essential component of cell wall peptidoglycan (murein). D-alanine is metabolized by an ATP driven D-alanine ligase A and B resulting in D-alanyl-D-alanine. This product is incorporated into the peptidoglycan biosynthesis.
L-alanine is metabolized with alanine racemase, either catabolic or metabolic resulting in a D-alanine. This compound reacts with water and a quinone through a
D-amino acid dehydrogenase resulting in Pyruvic acid, hydroquinone and ammonium, thus entering the central metabolism and thereby can serve as a total source of carbon and energy. This pathway is unique among those through which L-amino acids are degraded, in that the L form must first be converted to the D form.
D-alanine, is an essential component of cell wall peptidoglycan (murein). The role of the alr racemase is predominately biosynthetic: it is produced constitutively in small amounts. The role of the dadX racemase is degradative: it is induced to high levels by alanine and is subject to catabolite repression.
PW000788MetabolicSecondary Metabolites: cysteine biosynthesis from serineThe pathway starts with a 3-phosphoglyceric acid interacting with an NAD driven D-3-phosphoglycerate dehydrogenase / α-ketoglutarate reductase resulting in an NADH, a hydrogen ion and a phosphohydroxypyruvic acid. This compound then interacts with an L-glutamic acid through a 3-phosphoserine aminotransferase / phosphohydroxythreonine aminotransferase resulting in a oxoglutaric acid and a DL-D-phosphoserine. The latter compound then interacts with a water molecule through a phosphoserine phosphatase resulting in a phosphate and an L-serine. The L-serine interacts with an acetyl-coa through a serine acetyltransferase resulting in a release of a Coenzyme A and a O-Acetylserine. The O-acetylserine then interacts with a hydrogen sulfide through a O-acetylserine sulfhydrylase A resulting in an acetic acid, a hydrogen ion and an L-cysteinePW000977Metaboliccysteine biosynthesisThe pathway of cysteine biosynthesis is a two-step conversion starting from L-serine and yielding L-cysteine. L-serine biosynthesis is shown for context.
L-cysteine can also be synthesized from sulfate derivatives.
The process through L-serine involves a serine acetyltransferase that produces a O-acetylserine which reacts together with hydrogen sulfide through a cysteine synthase complex in order to produce L-cysteine and acetic acid.
Hydrogen sulfide is produced from a sulfate. Sulfate reacts with sulfate adenylyltransferase to produce adenosine phosphosulfate. This compound in turn is phosphorylated through a adenylyl-sulfate kinase into a phosphoadenosine phosphosulfate which in turn reacts with a phosphoadenosine phosphosulfate reductase to produce a sulfite. The sulfite reacts with a sulfite reductase to produce the hydrogen sulfide.
This pathway is regulated at the genetic level in its second step, wtih both cysteine synthase isozymes being under the positive control of the cysteine-responsive transcription factor CysB. It is also subject to very strong feedback inhibition of its first step by the final pathway product, cysteine.
Although two cysteine synthase isozymes exist, only cysteine synthase A (CysK) forms a complex with serine acetyltransferase. CysK is also the only one of the two cysteine synthases that is required for cell viability on cysteine-free medium.
Both steps in this pathway are reversible. Based on genetic and proteomic data, it appears that the cysteine synthases may actually act as a sulfur scavenging system during sulfur starvation, stripping sulfur off of L-cysteine, generating any number of variant amino acids in the process.PW000800Metabolicmethionine biosynthesisThe de novo biosynthesis of methionine is an energy-costly process involving inputs from several other pathways. The carbon skeleton of methionine is derived from aspartate. The sulfur is derived from cysteine which derives its sulfur from sulfate assimilation. The methyl group is derived from serine via one-carbon metabolism. Methionine is also converted to S-adenosyl-L-methionine, a methyl group donor, by the product of gene metK .
The synthesis starts with a product of the lysine biosynthesis pathway, L-aspartate-semialdehyde. This compound is dehydrogenated by a NADPH
aspartate kinase / homoserine dehydrogenase resulting in NADP and L-homoserine. Homoserine is activated by O-succinylation in a reaction catalyzed by MetA. The product O-succinyl-L-homoserine combines with cysteine to form cystathionine in a reaction catalyzed by MetB. Lyase cleavage of cystathionine by MetC forms homocysteine. This β-cystathionase activity can also be supplied by MalY as demonstrated in vivo by the ability of constitutive MalY expression to complement metC mutants auxotrophic for methionine . Homocysteine is subsequently methylated by either MetH or MetE to produce methionine. In E. coli MetH can function only in the presence of exogenously supplied vitamin B12 (cobalamin), which represses MetE expression. B12 is likely to be available in the gut. In the absence of exogenously supplied B12, MetE catalyzes this final step of de novo methionine biosynthesis.
L-methionine is then transferred into the periplasmic space through a leucine efflux transporter.
Under stressful conditions there is further regulation of the pathway enzymes. Under heat-shock conditions growth is slowed due to the thermal instability of MetA. Oxidative stress affects MetE which contains an oxidation-sensitive cysteine residue at position 645 near the active site. Oxidation of methionone itself can also occur although the cell contains methionine sufloxide reductases MsrA and MsrB to combat this. Weak organic acids also generate oxidative stress, with more complex effects. Sulfur limitation depletes homocysteine which serves as a coactivator for MetR activation of MetE expression.
Due to the absence of this pathway in mammals, some of the bacterial biosynthetic enzymes are potential drug targets. In addition, although methionine is used as a food additive and a medication, its industrial scale production in microorganisms has not yet been achieved due to the complexity and strong regulation of its biosynthetic pathway.PW000814Metabolicsulfur metabolism (butanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000923Metabolicsulfur metabolism (butanesulfonate/phenylacetaldehyde)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW001012Metabolicsulfur metabolism (ethanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case ethanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Ethanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000925Metabolicsulfur metabolism (isethionate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case isethionate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Isethionate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000926Metabolicsulfur metabolism (methanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case methanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Methanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000927Metabolicsulfur metabolism (propanesulfonate)The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 3-(N-morpholino)propanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 3-(N-morpholino)propanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.PW000924MetabolictRNA Charging 2This pathway groups together all E. coli tRNA charging reactions.PW000803MetabolictRNA chargingThis pathway groups together all E. coli tRNA charging reactions.PW000799Metabolicglutathione metabolism IIThe biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione.
Glutathione can then be degraded into various different glutathione containg compounds by reacting with a napthalene through a glutathione S-transferase
PW001927Metabolicglutathione metabolism IIIThe biosynthesis of glutathione starts with the introduction of L-glutamic acid through either a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a
glutamate / aspartate ABC transporter. Once in the cytoplasm, L-glutamice acid reacts with L-cysteine through an ATP glutamate-cysteine ligase resulting in gamma-glutamylcysteine. This compound reacts which Glycine through an ATP driven glutathione synthetase thus catabolizing Glutathione.
This compound is metabolized through a spontaneous reaction with an oxidized glutaredoxin resulting in a reduced glutaredoxin and an oxidized glutathione. This compound is reduced by a NADPH glutathione reductase resulting in a glutathione.
PW002018MetabolicHydrogen Sulfide Biosynthesis IIt has long been known that many bacteria are able to produce hydrogen sulfide [Barrett87]. However, the physiological role of H2S in nonsulfur bacteria was unknown. A recent report has now shown that production of H2S serves to defend cells from antibiotics by mitigating oxidative stress.
This pathway is one of two pathways for hydrogen sulfide biosynthesis. Neither of the two activities have been shown biochemically for the E. coli enzymes. The function of AspC as a cysteine transaminase is hypothesized based on sequence similarity to mammalian enzymes. The function of SseA was determined based on the phenotype of an sseA null mutant, which does not produce hydrogen sulfide.PW002066MetabolicL-cysteine degradationThe degradation of cysteine starts with L-cysteine reacting with l-cysteine desulfhydrase resulting in the release of a hydrogen sulfide, a hydrogen ion and a a 2-aminoprop-2-enoate. The latter compound in turn reacts spontaneously to form a 2-iminopropanoate. This compound in turn reacts spontaneously with water and a hydrogen ion resulting in the release of ammonium and pyruvate.PW002110Metaboliccysteine biosynthesis ICYSTSYN-PWYthiazole biosynthesis I (E. coli)PWY-6892molybdenum cofactor biosynthesisPWY-6823tRNA chargingTRNA-CHARGING-PWYmethionine biosynthesis IHOMOSER-METSYN-PWYL-cysteine degradation IILCYSDEG-PWYcoenzyme A biosynthesisCOA-PWYglutathione biosynthesisGLUTATHIONESYN-PWYhydrogen sulfide biosynthesisPWY0-1534alanine biosynthesis IIIPWY0-1021Specdb::CMs572Specdb::CMs573Specdb::CMs574Specdb::CMs575Specdb::CMs576Specdb::CMs3282Specdb::CMs30101Specdb::CMs30201Specdb::CMs30306Specdb::CMs30307Specdb::CMs30592Specdb::CMs30734Specdb::CMs30756Specdb::CMs31774Specdb::CMs37632Specdb::CMs146278Specdb::CMs1066885Specdb::CMs1066887Specdb::CMs1066889Specdb::CMs1066890Specdb::CMs1066892Specdb::NmrOneD1241Specdb::NmrOneD1426Specdb::NmrOneD4743Specdb::NmrOneD144450Specdb::NmrOneD144451Specdb::NmrOneD144452Specdb::NmrOneD144453Specdb::NmrOneD144454Specdb::NmrOneD144455Specdb::NmrOneD144456Specdb::NmrOneD144457Specdb::NmrOneD144458Specdb::NmrOneD144459Specdb::NmrOneD144460Specdb::NmrOneD144461Specdb::NmrOneD144462Specdb::NmrOneD144463Specdb::NmrOneD144464Specdb::NmrOneD144465Specdb::NmrOneD144466Specdb::NmrOneD144467Specdb::NmrOneD144468Specdb::NmrOneD144469Specdb::NmrOneD166443Specdb::MsMs800Specdb::MsMs801Specdb::MsMs802Specdb::MsMs4204Specdb::MsMs4205Specdb::MsMs4206Specdb::MsMs4207Specdb::MsMs4208Specdb::MsMs4209Specdb::MsMs4210Specdb::MsMs4211Specdb::MsMs4217Specdb::MsMs179826Specdb::MsMs179827Specdb::MsMs179828Specdb::MsMs182160Specdb::MsMs182161Specdb::MsMs182162Specdb::MsMs447649Specdb::MsMs447738Specdb::MsMs1471148Specdb::MsMs2226479Specdb::MsMs2228252Specdb::MsMs2228881Specdb::MsMs2230541Specdb::NmrTwoD1024Specdb::NmrTwoD1371HMDB0057458625653C0009717561CYSFCYL-CysteineKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72.18402659van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4.19212411Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75.6696735Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6.12297216Kersemans V, Cornelissen B, Kersemans K, Bauwens M, Achten E, Dierckx RA, Mertens J, Slegers G: In vivo characterization of 123/125I-2-iodo-L-phenylalanine in an R1M rhabdomyosarcoma athymic mouse model as a potential tumor tracer for SPECT. J Nucl Med. 2005 Mar;46(3):532-9.15750170Yu FH, Westenbroek RE, Silos-Santiago I, McCormick KA, Lawson D, Ge P, Ferriera H, Lilly J, DiStefano PS, Catterall WA, Scheuer T, Curtis R: Sodium channel beta4, a new disulfide-linked auxiliary subunit with similarity to beta2. J Neurosci. 2003 Aug 20;23(20):7577-85.12930796Sandmann J, Schwedhelm KS, Tsikas D: Specific transport of S-nitrosocysteine in human red blood cells: Implications for formation of S-nitrosothiols and transport of NO bioactivity within the vasculature. FEBS Lett. 2005 Aug 1;579(19):4119-24.16023102Paivalainen S, Suokas M, Lahti O, Heape AM: Degraded myelin-associated glycoprotein (dMAG) formation from pure human brain myelin-associated glycoprotein (MAG) is not mediated by calpain or cathepsin L-like activities. J Neurochem. 2003 Feb;84(3):533-45.12558973Iyer S, Leonidas DD, Swaminathan GJ, Maglione D, Battisti M, Tucci M, Persico MG, Acharya KR: The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution. J Biol Chem. 2001 Apr 13;276(15):12153-61. Epub 2000 Nov 7.11069911Nishiya Y, Yoshida Y, Yoshimura M, Fukamachi H, Nakano Y: Homogeneous enzymatic assay for L-cysteine with betaC-S lyase. Biosci Biotechnol Biochem. 2005 Nov;69(11):2244-6.16306712Santamaria I, Velasco G, Cazorla M, Fueyo A, Campo E, Lopez-Otin C: Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. 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Agricultural and Biological Chemistry (1977), 41(10), 2071-5.http://hmdb.ca/system/metabolites/msds/000/000/493/original/HMDB00574.pdf?1358894667Aspartate aminotransferaseP00509AAT_ECOLIaspChttp://ecmdb.ca/proteins/P00509.xmlCystathionine gamma-synthaseP00935METB_ECOLImetBhttp://ecmdb.ca/proteins/P00935.xmlAminopeptidase NP04825AMPN_ECOLIpepNhttp://ecmdb.ca/proteins/P04825.xmlCystathionine beta-lyase metCP06721METC_ECOLImetChttp://ecmdb.ca/proteins/P06721.xmlCysteine desulfuraseP0A6B7ISCS_ECOLIiscShttp://ecmdb.ca/proteins/P0A6B7.xmlGlutamate--cysteine ligaseP0A6W9GSH1_ECOLIgshAhttp://ecmdb.ca/proteins/P0A6W9.xmlTryptophanaseP0A853TNAA_ECOLItnaAhttp://ecmdb.ca/proteins/P0A853.xmlCysteine synthase AP0ABK5CYSK_ECOLIcysKhttp://ecmdb.ca/proteins/P0ABK5.xmlCoenzyme A biosynthesis bifunctional protein coaBCP0ABQ0COABC_ECOLIcoaBChttp://ecmdb.ca/proteins/P0ABQ0.xmlAminoacyl-histidine dipeptidaseP15288PEPD_ECOLIpepDhttp://ecmdb.ca/proteins/P15288.xmlCysteine synthase BP16703CYSM_ECOLIcysMhttp://ecmdb.ca/proteins/P16703.xmlCysteinyl-tRNA synthetaseP21888SYC_ECOLIcysShttp://ecmdb.ca/proteins/P21888.xmlProtein malYP23256MALY_ECOLImalYhttp://ecmdb.ca/proteins/P23256.xmlPeptidase BP37095PEPB_ECOLIpepBhttp://ecmdb.ca/proteins/P37095.xmlCytosol aminopeptidaseP68767AMPA_ECOLIpepAhttp://ecmdb.ca/proteins/P68767.xmlCysteine desulfurase_P77444SUFS_ECOLIsufShttp://ecmdb.ca/proteins/P77444.xmlATP-binding/permease protein cydCP23886CYDC_ECOLIcydChttp://ecmdb.ca/proteins/P23886.xmlATP-binding/permease protein cydDP29018CYDD_ECOLIcydDhttp://ecmdb.ca/proteins/P29018.xmltRNA sulfurtransferaseP77718THII_ECOLIthiIhttp://ecmdb.ca/proteins/P77718.xmlCysteine desulfuration protein sufEP76194SUFE_ECOLIsufEhttp://ecmdb.ca/proteins/P76194.xmlAminopeptidase NP04825AMPN_ECOLIpepNhttp://ecmdb.ca/proteins/P04825.xmlUncharacterized amino-acid ABC transporter ATP-binding protein yecCP37774YECC_ECOLIyecChttp://ecmdb.ca/proteins/P37774.xmlInner membrane amino-acid ABC transporter permease protein yecSP0AFT2YECS_ECOLIyecShttp://ecmdb.ca/proteins/P0AFT2.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlProbable amino-acid metabolite efflux pumpP31125EAMA_ECOLIeamAhttp://ecmdb.ca/proteins/P31125.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlCysteine/O-acetylserine efflux proteinP38101EAMB_ECOLIeamBhttp://ecmdb.ca/proteins/P38101.xmlCystine-binding periplasmic proteinP0AEM9FLIY_ECOLIfliYhttp://ecmdb.ca/proteins/P0AEM9.xmlCysteinylglycine + Water > L-Cysteine + GlycineR00899RXN-6622Adenosine triphosphate + L-Cysteine + Water > ADP + Hydrogen ion + Phosphate + L-CysteineRXN0-3Adenosine triphosphate + L-Cysteine + Water > ADP + Hydrogen ion + Phosphate + L-CysteineRXN0-3L-Cysteine + SufSE sulfur acceptor complex > L-Alanine + SufSE with bound sulfurO-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ionR00897ACSERLY-RXNL-Cysteine + Water > Hydrogen sulfide + Ammonium + Pyruvic acidAdenosine triphosphate + L-Cysteine + tRNA(Cys) + tRNA(Cys) <> Adenosine monophosphate + L-Cysteinyl-tRNA(Cys) + Pyrophosphate + L-Cysteinyl-tRNA(Cys)R03650L-Cysteine + IscS sulfur acceptor protein > L-Alanine + IscS with bound sulfurAdenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + PhosphateR00894GLUTCYSLIG-RXND-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine > 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + PyrophosphateR04231P-PANTOCYSLIG-RXNL-Cysteine + O-Succinyl-L-homoserine <> L-Cystathionine + Hydrogen ion + Succinic acidR03260O-SUCCHOMOSERLYASE-RXNL-Cysteine + Water <> Hydrogen sulfide + Pyruvic acid + AmmoniaR00782LCYSDESULF-RXNAdenosine triphosphate + L-Glutamate + L-Cysteine <> ADP + Phosphate + gamma-GlutamylcysteineR00894L-Cysteine + alpha-Ketoglutarate <> 3-Mercaptopyruvic acid + DL-Glutamic acidR00896O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acidR00897Cysteinylglycine + Water <> L-Cysteine + GlycineR00899Cystathionine + Succinic acid <> O-Succinyl-L-homoserine + L-CysteineR02508o-acetyl-l-homoserine + L-Cysteine <> L-Cystathionine + Acetic acidR03217O-Succinyl-L-homoserine + L-Cysteine <> L-Cystathionine + Succinic acidR03260Adenosine triphosphate + L-Cysteine + tRNA(Cys) <> Adenosine monophosphate + Pyrophosphate + L-Cysteinyl-tRNA(Cys)R03650Adenosine triphosphate + D-4'-Phosphopantothenate + L-Cysteine <> Adenosine monophosphate + Pyrophosphate + 4-PhosphopantothenoylcysteineR04230Cytidine triphosphate + D-4'-Phosphopantothenate + L-Cysteine <> Cytidine monophosphate + Pyrophosphate + 4-PhosphopantothenoylcysteineR04231O-Acetylserine + Thiosulfate + Thioredoxin + Hydrogen ion <> L-Cysteine + Sulfite + Thioredoxin disulfide + Acetic acidR04859[Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-AlanineR07460Oxoglutaric acid + L-Cysteine > L-Glutamate + 3-Mercaptopyruvic acidCYSTEINE-AMINOTRANSFERASE-RXNL-Cysteine + L-Glutamate + Adenosine triphosphate > Hydrogen ion + gamma-Glutamylcysteine + Phosphate + ADPGLUTCYSLIG-RXNL-Cysteine + Water > Pyruvic acid + Ammonia + Hydrogen sulfide + Hydrogen ionLCYSDESULF-RXNL-Cysteine + O-Succinyl-L-homoserine > Hydrogen ion + Succinic acid + L-CystathionineO-SUCCHOMOSERLYASE-RXNL-Cysteine + a sulfur acceptor + Hydrogen ion L-Alanine + <i>S</i>-sulfanyl-[acceptor]RXN-12588L-Cysteine + Adenosine triphosphate + Water > L-Cysteine + ADP + Phosphate + Hydrogen ionRXN0-3L-Cysteine + Adenosine triphosphate + Water > L-Cysteine + ADP + Phosphate + Hydrogen ionRXN0-3L-Cysteine + L-Cysteine-Desulfurases > L-Alanine + Persulfurated-L-cysteine-desulfurasesRXN0-308Cytidine triphosphate + (R)-4'-phosphopantothenate + L-Cysteine > Cytidine monophosphate + Pyrophosphate + 4-PhosphopantothenoylcysteineO-Acetylserine + Hydrogen sulfide > L-Cysteine + Acetic acidAdenosine triphosphate + L-Glutamate + L-Cysteine > ADP + Inorganic phosphate + gamma-GlutamylcysteineL-Cysteine + acceptor > L-Alanine + S-sulfanyl-acceptorO-Succinyl-L-homoserine + L-Cysteine > L-Cystathionine + Succinic acidAdenosine triphosphate + L-Cysteine + tRNA(Cys) > Adenosine monophosphate + Pyrophosphate + L-cysteinyl-tRNA(Cys)L-Cysteine + 'activated' tRNA > L-Serine + tRNA containing a thionucleotideL-Cysteine + 'Activated' tRNA <> L-Serine + tRNA containing a thionucleotideR03923 L-Cysteine + an [L-cysteine desulfurase] L-cysteine persulfide > an [L-cysteine desulfurase] L-cysteine persulfide + L-Alanine + L-AlaninePW_R002661L-Cysteine + tRNA(Cys) + Adenosine triphosphate + Hydrogen ion > Pyrophosphate + Adenosine monophosphate + L-cysteinyl-tRNA(Cys)PW_R002824O-Acetylserine > Hydrogen ion + Acetic acid + L-CysteinePW_R002847O-Acetylserine + Hydrogen sulfide > Hydrogen ion + Acetic acid + L-CysteinePW_R002848L-Cysteine > Hydrogen ion + Hydrogen sulfide + 2-Aminoacrylic acidPW_R003466Cytidine triphosphate + D-4'-Phosphopantothenate + L-Cysteine + D-4'-Phosphopantothenate > Cytidine monophosphate + Pyrophosphate + 4-Phosphopantothenoylcysteine + Cytidine monophosphatePW_R002991D-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine + D-4'-Phosphopantothenate > Cytidine monophosphate + Pyrophosphate + Hydrogen ion + 4-Phosphopantothenoylcysteine + Cytidine monophosphatePW_R003003L-Glutamic acid + Adenosine triphosphate + L-Cysteine + L-Glutamate > Adenosine diphosphate + Phosphate + Hydrogen ion + gamma-Glutamylcysteine + ADPPW_R003052L-Cysteine + Adenosine triphosphate + Water > ADP + Phosphate + Hydrogen ionPW_RCT000186L-Cysteine > Hydrogen sulfide + Hydrogen ion + 2-aminoprop-2-enoatePW_R006145O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ionAdenosine triphosphate + L-Cysteine + tRNA(Cys) <> Adenosine monophosphate + L-Cysteinyl-tRNA(Cys) + PyrophosphateO-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid[Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-AlanineCysteinylglycine + Water > L-Cysteine + GlycineAdenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + PhosphateD-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine >4 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + Pyrophosphate[Enzyme]-cysteine + L-Cysteine <> [Enzyme]-S-sulfanylcysteine + L-AlanineAdenosine triphosphate + L-Cysteine + L-Glutamate <> ADP + gamma-Glutamylcysteine + Hydrogen ion + PhosphateD-4'-Phosphopantothenate + Cytidine triphosphate + L-Cysteine >4 4-Phosphopantothenoylcysteine + Cytidine monophosphate + Hydrogen ion + PyrophosphateLuria-Bertani (LB) mediaShake flask204.0uMtrue45.037 oCBL21 DE3Stationary phase cultures (overnight culture)816000180000Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911