2.0 2012-05-31 13:57:31 -0600 2015-06-03 15:54:19 -0600 ECMDB03011 M2MDB000473 O-Acetylserine O-Acetylserine is an intermediate in the biosynthesis of the common amino acid cysteine in bacteria and plants. O-Acetylserine is biosynthesized by acetylation of the serine by the enzyme serine transacetylase. The enzyme O-acetylserine (thiol)-lyase, using sulfide sources, converts this ester into cysteine, releaseing acetate. <i>O</i>-acetylserine Acetylserine AcSer O(3)-acetyl-L-serine O-Acetyl-L-serine O-Acetyl-Serine O3-Acetyl-L-serine O³-acetyl-L-serine C5H9NO4 147.1293 147.053157781 (2S)-3-(acetyloxy)-2-aminopropanoic acid O-acetyl-L-serine 5147-00-2 CC(=O)OC[C@H](N)C(O)=O InChI=1S/C5H9NO4/c1-3(7)10-2-4(6)5(8)9/h4H,2,6H2,1H3,(H,8,9)/t4-/m0/s1 VZXPDPZARILFQX-BYPYZUCNSA-N Solid Cytosol Extra-organism Periplasm logp -2.85 ALOGPS logs 0.07 ALOGPS solubility 1.74e+02 g/l ALOGPS logp -3.4 ChemAxon pka_strongest_acidic 1.86 ChemAxon pka_strongest_basic 8.6 ChemAxon iupac (2S)-3-(acetyloxy)-2-aminopropanoic acid ChemAxon average_mass 147.1293 ChemAxon mono_mass 147.053157781 ChemAxon smiles CC(=O)OC[C@H](N)C(O)=O ChemAxon formula C5H9NO4 ChemAxon inchi InChI=1S/C5H9NO4/c1-3(7)10-2-4(6)5(8)9/h4H,2,6H2,1H3,(H,8,9)/t4-/m0/s1 ChemAxon inchikey VZXPDPZARILFQX-BYPYZUCNSA-N ChemAxon polar_surface_area 89.62 ChemAxon refractivity 31.19 ChemAxon polarizability 13.44 ChemAxon rotatable_bond_count 4 ChemAxon acceptor_count 4 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Cysteine and methionine metabolism ec00270 Selenoamino acid metabolism ec00450 Sulfur metabolism 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 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. PW000922 ec00920 Metabolic Microbial metabolism in diverse environments ec01120 Metabolic pathways eco01100 Secondary Metabolites: cysteine biosynthesis from serine The 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-cysteine PW000977 Metabolic cysteine biosynthesis The 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. PW000800 Metabolic sulfur 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. PW000923 Metabolic sulfur 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. PW000925 Metabolic sulfur 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. PW000926 Metabolic sulfur 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. PW000927 Metabolic sulfur 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. PW000924 Metabolic cysteine biosynthesis I CYSTSYN-PWY Specdb::CMs 888 Specdb::CMs 889 Specdb::CMs 890 Specdb::CMs 1103 Specdb::CMs 2337 Specdb::CMs 30391 Specdb::CMs 30392 Specdb::CMs 30837 Specdb::CMs 31437 Specdb::CMs 38510 Specdb::CMs 150112 Specdb::NmrOneD 4928 Specdb::NmrOneD 129158 Specdb::NmrOneD 129159 Specdb::NmrOneD 129160 Specdb::NmrOneD 129161 Specdb::NmrOneD 129162 Specdb::NmrOneD 129163 Specdb::NmrOneD 129164 Specdb::NmrOneD 129165 Specdb::NmrOneD 129166 Specdb::NmrOneD 129167 Specdb::NmrOneD 129168 Specdb::NmrOneD 129169 Specdb::NmrOneD 129170 Specdb::NmrOneD 129171 Specdb::NmrOneD 129172 Specdb::NmrOneD 129173 Specdb::NmrOneD 129174 Specdb::NmrOneD 129175 Specdb::NmrOneD 129176 Specdb::NmrOneD 129177 Specdb::MsMs 6499 Specdb::MsMs 177954 Specdb::MsMs 177955 Specdb::MsMs 177956 Specdb::MsMs 180267 Specdb::MsMs 180268 Specdb::MsMs 180269 Specdb::MsMs 448112 Specdb::MsMs 1471189 Specdb::MsMs 2235801 Specdb::MsMs 2235862 Specdb::MsMs 2236103 Specdb::MsMs 2237259 Specdb::MsMs 2237498 Specdb::MsMs 2237553 Specdb::MsMs 2238271 Specdb::MsMs 2239328 Specdb::MsMs 2239949 Specdb::MsMs 2240261 Specdb::MsMs 2241428 Specdb::MsMs 2241742 Specdb::MsMs 2242072 Specdb::MsMs 2242322 Specdb::MsMs 2243559 Specdb::MsMs 2243817 HMDB03011 189 89874 C00979 17981 ACETYLSERINE OAS O-Acetylserine Keseler, 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. 21097882 Kanehisa, 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. 22080510 van 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. 17765195 Winder, 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. 18331064 Sreekumar 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. 19212411 Sugahara K, Zhang J, Kodama H: Liquid chromatographic-mass spectrometric analysis of N-acetylamino acids in human urine. J Chromatogr B Biomed Appl. 1994 Jul 1;657(1):15-21. 7952062 Cystathionine gamma-synthase P00935 METB_ECOLI metB http://ecmdb.ca/proteins/P00935.xml Serine acetyltransferase P0A9D4 CYSE_ECOLI cysE http://ecmdb.ca/proteins/P0A9D4.xml Cysteine synthase A P0ABK5 CYSK_ECOLI cysK http://ecmdb.ca/proteins/P0ABK5.xml Cysteine synthase B P16703 CYSM_ECOLI cysM http://ecmdb.ca/proteins/P16703.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Probable amino-acid metabolite efflux pump P31125 EAMA_ECOLI eamA http://ecmdb.ca/proteins/P31125.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Cysteine/O-acetylserine efflux protein P38101 EAMB_ECOLI eamB http://ecmdb.ca/proteins/P38101.xml O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ion R00897 ACSERLY-RXN Acetyl-CoA + L-Serine <> O-Acetylserine + Coenzyme A R00586 SERINE-O-ACETTRAN-RXN O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid R00897 O-Acetylserine + Thiosulfate <> Cysteine-S-sulfate + Acetic acid R03132 O-Acetylserine + Hydrogen selenide <> Selenocysteine + Acetic acid R03601 O-Acetylserine + Thiosulfate + Thioredoxin + Hydrogen ion <> L-Cysteine + Sulfite + Thioredoxin disulfide + Acetic acid R04859 Acetyl-CoA + L-Serine > CoA + O-Acetylserine O-Acetylserine + Hydrogen sulfide > L-Cysteine + Acetic acid L-Serine + Acetyl-CoA + L-Serine > Coenzyme A + O-Acetylserine PW_R002846 O-Acetylserine > Hydrogen ion + Acetic acid + L-Cysteine PW_R002847 O-Acetylserine + Hydrogen sulfide > Hydrogen ion + Acetic acid + L-Cysteine PW_R002848 O-Acetylserine + Thiosulfate + Thiosulfate > Cysteine-S-sulfate + Acetic acid PW_R005147 O-Acetylserine + Hydrogen sulfide <> Acetic acid + L-Cysteine + Hydrogen ion O-Acetylserine + Hydrogen sulfide <> L-Cysteine + Acetic acid Acetyl-CoA + L-Serine <> O-Acetylserine + Coenzyme A