2.02012-07-30 14:54:45 -06002015-09-13 15:15:31 -0600ECMDB21174M2MDB0015835'-Deoxyadenosine5'-Deoxyadenosine is an abnormal form of deoxyadenosine derived from S-adenosylmethionine. The normal form of deoxyadenosine used in DNA synthesis and repair is 2'-deoxyadenosine where the hydroxyl group (-OH) is at the 2' position of its ribose sugar moiety. 5'-deoxyadenosine has its hydroxyl group at the 5' position of the ribose sugar. 5'-deoxyadenosine is a substrate for 5'-methylthioadenosine phosphorylase. It is also a product of the degradation/conversion of S-adenosyl-methionine by the enzymes: 2-iminoacetate synthase, biotin synthase, lopoyl synthase and pyruvate-formate lyase activating enzyme5'-Deoxy-adenosine5'-DeoxyadenosineCH3AdoCH<sub>3</sub>AdoC10H13N5O3251.2419251.101839307(2R,3R,4S,5R)-2-(6-amino-9H-purin-9-yl)-5-methyloxolane-3,4-diol5'-deoxyadenosine4754-39-6C[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C(N)N=CN=C12InChI=1S/C10H13N5O3/c1-4-6(16)7(17)10(18-4)15-3-14-5-8(11)12-2-13-9(5)15/h2-4,6-7,10,16-17H,1H3,(H2,11,12,13)/t4-,6-,7-,10-/m1/s1XGYIMTFOTBMPFP-KQYNXXCUSA-NSolidCytosollogp-0.52ALOGPSlogs-1.41ALOGPSsolubility9.88e+00 g/lALOGPSmelting_point213.0-214.5 oClogp-1ChemAxonpka_strongest_acidic12.48ChemAxonpka_strongest_basic3.92ChemAxoniupac(2R,3R,4S,5R)-2-(6-amino-9H-purin-9-yl)-5-methyloxolane-3,4-diolChemAxonaverage_mass251.2419ChemAxonmono_mass251.101839307ChemAxonsmilesC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C(N)N=CN=C12ChemAxonformulaC10H13N5O3ChemAxoninchiInChI=1S/C10H13N5O3/c1-4-6(16)7(17)10(18-4)15-3-14-5-8(11)12-2-13-9(5)15/h2-4,6-7,10,16-17H,1H3,(H2,11,12,13)/t4-,6-,7-,10-/m1/s1ChemAxoninchikeyXGYIMTFOTBMPFP-KQYNXXCUSA-NChemAxonpolar_surface_area119.31ChemAxonrefractivity61.65ChemAxonpolarizability24.3ChemAxonrotatable_bond_count1ChemAxonacceptor_count7ChemAxondonor_count3ChemAxonphysiological_charge0ChemAxonformal_charge0ChemAxonPorphyrin and chlorophyll metabolismec00860Biotin metabolismBiotin (vitamin H or vitamin B7) is the essential cofactor of biotin-dependent carboxylases, such as pyruvate carboxylase and acetyl-CoA carboxylase.In E. coli and many organisms, pimelate thioester is derived from malonyl-ACP. The pathway starts with a malonyl-[acp] interacting with S-adenosylmethionine through a biotin synthesis protein BioC resulting in a S-adenosylhomocysteine and a malonyl-[acp] methyl ester. The latter compound is then involved in the synthesis of a 3-ketoglutaryl-[acp] methyl ester through a 3-oxoacyl-[acyl-carrier-protein] synthase. The compound 3-ketoglutaryl-[acp] methyl ester is reduced by a NADPH mediated 3-oxoacyl-[acyl-carrier-protein] reductase resulting in a 3R-hydroxyglutaryl-[acp] methyl ester. This compound is then dehydrated through ad (3R)-hydroxymyristoyl-[acp] dehydratase producing a enoylglutaryl-[acp] methyl ester. This compound is then reduced through a NADPH mediated enoyl-acp-reductase [NADH] resulting in a glutaryl-[acp] methyl ester. This compound interacts with a malonyl-[acp] through a 3-oxoacyl-[acp] synthase 2 resulting in a 3-ketopimeloyl [acp] methyl ester. This compound is then reduced through a NADPH 3-oxoacyl [acp] reductase producing a 3-hydroxypimeloyl-[acp] methyl ester and then dehydrated by (3R)-hydroxymyristoyl-[acp] dehydratase to produce a enoylpimeloyl-[acp] methyl ester. This compound is then reduced by a NADPH dependent enoyl-[acp]reductase resulting in a pimeloyl-[acp] methyl ester. This compound then reacts with water through a carboxylesterase resulting in a pimeloyl-[acp] and a methanol. The pimeloyl-acp reacts with L-alanine through a 8-amino-7-oxononanoate synthase resulting in 8-amino-7-oxononanoate which in turn reacts with S-adenosylmethionine through a 7,8 diaminonanoate transaminase resulting in a S-adenosyl-4-methylthio-2-oxobutanoate and 7,8 diaminononanoate. The latter compound is then dephosphorylated through a dethiobiotin synthetase resulting in a dethiobiotin. This compound interacts with a sulfurated[sulfur carrier), a hydrogen ion and a S-adenosylmethionine through a biotin synthase to produce Biotin and releasing l-methionine and a 5-deoxyadenosine.
Biotin is then metabolized by a bifunctional protein resulting in pyrophosphate and Biotinyl-5-AMP which in turn reacts with the same protein (bifunctional protein birA resulting ina biotin caroxyl carrying protein.This product then enters the fatty acid biosynthesis.
PW000762ec00780MetabolicThiamine metabolismec00730Lipoic acid metabolismLipoic acid metabolism starts with caprylic acid being introduced into the cytoplasm however no transporter has been identified yet.
Once caprylic acid is in the cytoplasm, it can either reacts with a holo-acp, through an ATP driven 2-acylglycerophosphoethanolamine acyltransferase / acyl-ACP synthetase resulting in pyrophosphate, AMP and octanoyl-[acp]. The latter compound can also be obtained from palmitate biosynthesis.
Octanoyl-acp interacts with a lipoyl-carrier protein L-lysine through a Octanoyltransferase resulting in a hydrogen ion, a holo-acyl-acp, and a protein N6-0octanoyl) lysine. The latter compound reacts with an S-adenosylmethionine, a sulfurated[sulfur carrier] and a reduced ferredoxin through a lipoate-protein ligase A, resulting in a 5-deoxyadenosine, a L-methionine, an unsulfurated [sulfur carrier], oxidized ferredoxin, and a Protein N6-(lipoyl) lysine.
Caprylic acid can also interact with ATP and a lipoyl-carrier protein-L-lysine through a lipoate-protein ligase A resulting in a amp, pyrophosphate, hydrogen ion, protein N6-(octanoyl)lysine. The latter compound reacts with an S-adenosylmethionine, a sulfurated[sulfur carrier] and a reduced ferredoxin through a lipoate-protein ligase A, resulting in a 5-deoxyadenosine, a L-methionine, an unsulfurated [sulfur carrier], oxidized ferredoxin, and a Protein N6-(lipoyl) lysine.
R-lipoic acid can be absorbed from the environment, as seen in studies by Morris TW. In this pathway the lipoyl-protein ligase LplA utilizes pre-existing lipoate that has been imported from outside the cell, and thus catalyzes a salvage pathway. Lipoic acid interacts with ATP and hydrogen ion through a lipoyl-protein ligase A, resulting in a pyrophosphate and a Lipoyl-AMP (lipoyl-adenylate). This compound then interacts with a lipoyl-carrier protein-L-lysine through a lipoate-protein ligase A resulting a AMP, a hydrogen ion
and a Protein N6-(lipoyl) lysine.
It has been suggested that the conversion of octanoylated-domains to lipoylated ones described in this pathway may be a type of a repair pathway, activated only if the other lipoate biosynthetic pathways are malfunctioning .
PW000770ec00785MetabolicMetabolic pathwayseco01100Porphyrin metabolismThe metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter .
L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate.
This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane.
Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III.
Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I
Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III.
Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+
uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway.
Uroporphyrinogen III can be processed in anaerobic or aerobic condition.
Anaerobic:
Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX
Aerobic:
Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX.
The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway.
PW000936Metabolictyrosine biosynthesisThe pathways of biosynthesis of phenylalaline and tyrosine are intimately connected. First step of both pathways is the conversion of chorismate to prephenate, the third step of both is the conversion of a ketoacid to the aminoacid through transamination. The two pathways differ only in the second step of their three-step reaction sequences: In the case of phenylalanine biosynthesi a dehydratase converts prephenate to phenylpyruvate(reaction occurs slowly in the absence of enzymic activity); in the case of tyrosine biosynthesis, a dehydrogenase converts prephenate to p-hydroxyphenylpyruvate. Also in both pathways the first two steps are catalyzed by two distinc active sites on a single protein. Thus the first step of each pathway can be catalyzed by two enzyme: those associated with both the phenylalanine specific dehydratase and the tyrosine specific dehydrogenase. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosinePW000806MetabolicThiamin diphosphate biosynthesisPW002028MetabolicThiazole Biosynthesis IThis pathway describes only the synthesis of the thiazole moiety of thiamin. Different variations of this pathway exist, this particular pathway describes the pathway that occurs in Escherichia coli K-12 and Salmonella enterica enterica serovar Typhimurium.
The biosynthesis of the thiazole moiety is complex. In Escherichia coli it involves six proteins, the products of the thiS, thiF, thiG, thiH, thiI, and iscS genes.
The process begins when IscS, a protein that is also involved in the biosynthesis of iron-sulfur clusters, catalyzes the transfer of a sulfur atom from cysteine to a ThiI sulfur-carrier protein, generating a an S-sulfanyl-[ThiI sulfur-carrier protein].
In a parallel route, the ThiF protein activates a ThiS sulfur-carrier protein by adenylation of its carboxy terminus, generating a carboxy-adenylated-[ThiS sulfur-carrier protein]. In a second reaction, which may also be catalyzed by ThiF, the sulfur from an S-sulfanyl-[ThiI sulfur-carrier protein] is transferred to ThiS, generating a thiocarboxy-[ThiS-Protein].
The final reaction of this pathway, which is catalyzed by the ThiG protein, requires three inputs: a thiocarboxy-[ThiS-Protein], 1-deoxy-D-xylulose 5-phosphate and 2-iminoacetate.
2-iminoacetate is formed in Escherichia coli from L-tyrosine by tyrosine lyase (ThiH), which forms a complex with ThiG.
For many years the products of this reaction was assumed to be 4-methyl-5-(β-hydroxyethyl)thiazole (thiazole). However, recent work performed with the thiazole synthase from Bacillus subtilis has shown that the actual product is the thiazole tautomer 2-[(2R,5Z)-(2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate. While in Bacillus a dedicated thiazole tautomerase converts this product into a different tautomer (2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate), most of the proteobacteria lack the tautomerase. (EcoCyc)PW002041MetabolicLipoate Biosynthesis and Incorporation IThe biosynthesis of lipoate is unusual, and shares the same mechanism as the biosynthesis of biotin. The first enzyme in this pathway, lipoyl(octanoyl) transferase, transfers the octanoate moiety from octanoate-ACP molecules to specific lysyl residues in lipoate-dependent enzymes, resulting in octanylated domains, and regenerating the acyl-carrier protein in the process.
The next enzyme in the pathway, lipoyl synthase, catalyzes the conversion of the octanoyl side chain to an active lipoyl, generating a fully active lipoylated domain. The enzyme is an iron-sulfur protein that requires the presence of S-adenosyl-L-methionine. An electron which originates from the [4Fe-4S] cluster of the enzyme serves to split at least two molecules of AdoMet into a 5'-deoxyadenosyl radical and methionine. The radical then abstracts a hydrogen from a C-H bond of the octanoyl side chain, becoming 5'-adenosine in the process. The newly-formed unstable octanoyl radical then reacts directly with the Fe-S center of the enzyme. Two sulfur atoms from the center enter the structure of the octanoyl side chain, producing lipoyl, which dissociates from the enzyme along with excess iron, leaving it with a [2Fe-2S] center. Thus, in this unusual reaction, the iron-sulfur center of the enzyme is not just a catalytic accelerator, but also a substrate, donating the two sulfur atoms. It should be noted that although this process has been well documented in vitro, there is still a possibility that there exists another sulfur donor in vivo, and that the Fe-S center acts as sulfur donor only in the absence of this natural donor.
It has been suggested that the conversion of octanoylated-domains to lipoylated ones described in this pathway may be a type of a repair pathway, activated only if the other lipoate biosynthetic pathways are malfunctioning. (EcoCyc)PW002107Metabolicbiotin biosynthesis from 7-keto-8-aminopelargonatePWY0-1507methylphosphonate degradationPWY0-1533thiazole biosynthesis I (E. coli)PWY-6892lipoate biosynthesis and incorporation IIPWY0-1275preQ<sub>0</sub> biosynthesisPWY-67034-amino-2-methyl-5-diphosphomethylpyrimidine biosynthesisPWY-6890heme biosynthesis from uroporphyrinogen-III IIHEMESYN2-PWYlipoate biosynthesis and incorporation IPWY0-501Specdb::CMs2875Specdb::CMs38211Specdb::CMs136238Specdb::CMs143972Specdb::NmrOneD102918Specdb::NmrOneD102919Specdb::NmrOneD102920Specdb::NmrOneD102921Specdb::NmrOneD102922Specdb::NmrOneD102923Specdb::NmrOneD102924Specdb::NmrOneD102925Specdb::NmrOneD102926Specdb::NmrOneD102927Specdb::NmrOneD102928Specdb::NmrOneD102929Specdb::NmrOneD102930Specdb::NmrOneD102931Specdb::NmrOneD102932Specdb::NmrOneD102933Specdb::NmrOneD102934Specdb::NmrOneD102935Specdb::NmrOneD102936Specdb::NmrOneD102937Specdb::MsMs27500Specdb::MsMs27501Specdb::MsMs27502Specdb::MsMs34058Specdb::MsMs34059Specdb::MsMs34060Specdb::MsMs440104Specdb::MsMs446043Specdb::MsMs446044Specdb::MsMs446045Specdb::MsMs446046Specdb::MsMs446047Specdb::MsMs447224Specdb::MsMs451939Specdb::MsMs2226830Specdb::MsMs2227907Specdb::MsMs2229146Specdb::MsMs2230291Specdb::MsMs2231612Specdb::MsMs2232601Specdb::MsMs2234026Specdb::MsMs2234895Specdb::MsMs2244474Specdb::MsMs2245652Specdb::MsMs2246605HMDB01983439182388325C0519817319CH33ADO5ADKeseler, 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-D590.21097882van 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 370:17-25.17765195Lee SH, Jung BH, Kim SY, Chung BC: A rapid and sensitive method for quantitation of nucleosides in human urine using liquid chromatography/mass spectrometry with direct urine injection. Rapid Commun Mass Spectrom. 2004;18(9):973-7.15116424Lerner, Leon M. An improved preparation of 5'-deoxyadenosine by coupling methods. Carbohydrate Research (1988), 184 250-3.http://hmdb.ca/system/metabolites/msds/000/001/566/original/HMDB01983.pdf?1358462133Pyruvate formate-lyase 1-activating enzymeP0A9N4PFLA_ECOLIpflAhttp://ecmdb.ca/proteins/P0A9N4.xmlAnaerobic ribonucleoside-triphosphate reductase-activating proteinP0A9N8NRDG_ECOLInrdGhttp://ecmdb.ca/proteins/P0A9N8.xml5'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseP0AF12MTNN_ECOLImtnNhttp://ecmdb.ca/proteins/P0AF12.xmlBiotin synthaseP12996BIOB_ECOLIbioBhttp://ecmdb.ca/proteins/P12996.xmlLipoate-protein ligase AP32099LPLA_ECOLIlplAhttp://ecmdb.ca/proteins/P32099.xmlOxygen-independent coproporphyrinogen-III oxidaseP32131HEMN_ECOLIhemNhttp://ecmdb.ca/proteins/P32131.xmlPyruvate formate-lyase 2-activating enzymeP32675PFLC_ECOLIpflChttp://ecmdb.ca/proteins/P32675.xmlOxygen-independent coproporphyrinogen-III oxidase-like protein yggWP52062YGGW_ECOLIyggWhttp://ecmdb.ca/proteins/P52062.xmlLipoyl synthaseP60716LIPA_ECOLIlipAhttp://ecmdb.ca/proteins/P60716.xmlPutative pyruvate formate-lyase 3-activating enzymeP75794PFLE_ECOLIybiYhttp://ecmdb.ca/proteins/P75794.xmlThiazole synthaseP30139THIG_ECOLIthiGhttp://ecmdb.ca/proteins/P30139.xmlDehydroglycine synthaseP30140THIH_ECOLIthiHhttp://ecmdb.ca/proteins/P30140.xmlPhosphomethylpyrimidine synthaseP30136THIC_ECOLIthiChttp://ecmdb.ca/proteins/P30136.xmlRibosomal RNA large subunit methyltransferase NP36979RLMN_ECOLIrlmNhttp://ecmdb.ca/proteins/P36979.xmltRNA-2-methylthio-N(6)-dimethylallyladenosine synthaseP0AEI1MIAB_ECOLImiaBhttp://ecmdb.ca/proteins/P0AEI1.xmlRibosomal protein S12 methylthiotransferase RimOP0AEI4RIMO_ECOLIrimOhttp://ecmdb.ca/proteins/P0AEI4.xml5'-Deoxyadenosine + Water > 5'-Deoxyribose + AdenineRXN0-6550[4Fe-4S] iron-sulfur cluster + 2 S-Adenosylmethionine + Hydrogen ion + NAD + octanoate (protein bound) > [2Fe-2S] iron-sulfur cluster +2 5'-Deoxyadenosine +2 Iron + lipoate (protein bound) +2 L-Methionine + NADH[2Fe-2S] iron-sulfur cluster + S-Adenosylmethionine + Dethiobiotin > [2Fe-1S] desulfurated iron-sulfur cluster + Biotin + 5'-Deoxyadenosine + Hydrogen ion + L-Methionine2 S-Adenosylmethionine + Coproporphyrin III <>2 Carbon dioxide +2 5'-Deoxyadenosine +2 L-Methionine + Protoporphyrinogen IXR06895S-Adenosylmethionine + NADPH + L-Tyrosine > p-Cresol + 5'-Deoxyadenosine + Dehydroglycine + Hydrogen ion + L-Methionine + NADPDethiobiotin + Sulfur donor + 2 S-Adenosylmethionine + 2 e- + 2 Hydrogen ion <> Biotin +2 L-Methionine +2 5'-DeoxyadenosineR01078Protein N6-(octanoyl)lysine + 2 Sulfur donor + 2 S-Adenosylmethionine + Protein N6-(octanoyl)lysine <> Protein N6-(lipoyl)lysine +2 L-Methionine +2 5'-Deoxyadenosine + Protein N6-(lipoyl)lysineR07767Octanoyl-[acp] + 2 Sulfur donor + 2 S-Adenosylmethionine <> Lipoyl-[acp] +2 L-Methionine +2 5'-DeoxyadenosineR07768Hydrogen ion + α-D-ribose-1-methylphosphonate-5-phosphate + S-Adenosylmethionine > α-D-ribose-1,2-cyclic-phosphate-5-phosphate + methane + 5'-Deoxyadenosine + L-MethionineRXN0-6734<i>S</i>-sulfanyl-[acceptor] + Dethiobiotin + S-Adenosylmethionine > an unsulfurated sulfur acceptor + Biotin + 5'-Deoxyadenosine + L-Methionine + Hydrogen ion2.8.1.6-RXNCoproporphyrinogen III + S-Adenosylmethionine > Protoporphyrinogen IX + Carbon dioxide + L-Methionine + 5'-DeoxyadenosineHEMN-RXN5-Aminoimidazole ribonucleotide + S-Adenosylmethionine 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + carbon monoxide + Hydrogen ionPYRIMSYN1-RXNS-Adenosylmethionine + Ribonuc-tri-P-reductases-inactive <> 5'-Deoxyadenosine + L-Methionine + Ribonuc-tri-P-reductases-activeRNTRACTIV-RXNL-Tyrosine + S-Adenosylmethionine + a reduced electron acceptor > Dehydroglycine + p-Cresol + 5'-Deoxyadenosine + L-Methionine + an oxidized electron acceptor + Hydrogen ionRXN-11319N-6-isopentyl adenosine-37 tRNA + S-Adenosylmethionine + <i>S</i>-sulfanyl-[acceptor] 2-methylthio-N-6-isopentyl adenosine-37 tRNA + S-Adenosylhomocysteine + L-Methionine + 5'-Deoxyadenosine + an unsulfurated sulfur acceptor + Hydrogen ionRXN0-50636-Carboxy-5,6,7,8-tetrahydropterin + S-Adenosylmethionine + Hydrogen ion > 7-carboxy-7-deazaguanine + 5'-Deoxyadenosine + L-Methionine + AmmoniaRXN0-6575Dethiobiotin + Hydrogen sulfide + 2 S-adenosyl-L-methionine > Biotin +2 L-Methionine +2 5'-DeoxyadenosineCoproporphyrinogen III + 2 S-adenosyl-L-methionine > Protoporphyrinogen IX +2 Carbon dioxide +2 L-Methionine +2 5'-DeoxyadenosineProtein N(6)-(octanoyl)lysine + 2 Hydrogen sulfide + 2 S-adenosyl-L-methionine > protein N(6)-(lipoyl)lysine +2 L-Methionine +2 5'-DeoxyadenosineS-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine > 5'-Deoxyadenosine + L-Methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA > S-Adenosylhomocysteine + L-Methionine + 5'-Deoxyadenosine + 2-methyladenine(2503) in 23S rRNA5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine > 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + COL-Tyrosine + S-adenosyl-L-methionine + reduced acceptor > 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + acceptor +2 Hydrogen ion2 S-Adenosylmethionine <> S-Adenosylhomocysteine +2 L-Methionine + 5'-DeoxyadenosineR10645 2 S-Adenosylmethionine + Reduced acceptor <> S-Adenosylhomocysteine +2 L-Methionine + 5'-DeoxyadenosineR10652 L-Tyrosine + S-Adenosylmethionine + NADPH <> 2-iminoacetate + p-Cresol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ionR10246 4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <> 5-Aminoimidazole ribonucleotide + 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + COR03472Dethiobiotin + 2 S-adenosyl-L-methionine + 2 Hydrogen ion + a sulfurated [sulfur carrier] > Biotin +2 L-Methionine +2 5'-DeoxyadenosinePW_R002499Octanoyl-[acyl-carrier protein] + 2 a sulfur donor + 2 S-adenosyl-L-methionine > Lipoyl-ACP +2 L-Methionine + 5'-DeoxyadenosinePW_R002519Protein N6-(octanoyl)lysine + 2 a sulfur donor + 2 S-adenosyl-L-methionine > Protein N6-(lipoyl)lysine +2 L-Methionine +2 5'-DeoxyadenosinePW_R002522Protein N6-(octanoyl)lysine + 2 Reduced ferredoxin + 2 a sulfurated [sulfur carrier] + 2 S-adenosyl-L-methionine >2 L-Methionine +2 5'-Deoxyadenosine + Oxidized ferredoxin + Protein N6-(lipoyl)lysine + an unsulfurated [sulfur carrier]PW_R003564S-adenosyl-L-methionine + Coproporphyrinogen III > 5'-Deoxyadenosine + L-Methionine + Carbon dioxide + Protoporphyrinogen IXPW_R003483L-Tyrosine + NADPH + S-adenosyl-L-methionine + L-Tyrosine + NADPH > Hydrogen ion + NADP + L-Methionine + 5'-Deoxyadenosine + p-Cresol + 2-iminoacetatePW_R0051745-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine >3 Hydrogen ion + CO + Formic acid + L-Methionine + 5'-Deoxyadenosine + 4-amino-2-methyl-5-phosphomethylpyrimidinePW_R005931L-Tyrosine + S-adenosyl-L-methionine + NADPH > Dehydroglycine + 4-Methylcatechol + 5'-Deoxyadenosine + L-Methionine + NADP + Hydrogen ionPW_R005962a [lipoyl-carrier protein] N6-octanoyl-L-lysine + 2 S-adenosyl-L-methionine + 2 a sulfurated [sulfur carrier] + 2 Reduced ferredoxin > Protein N6-(lipoyl)lysine +2 5'-Deoxyadenosine +2 L-Methionine +2 an unsulfurated [sulfur carrier] +2 Oxidized ferredoxinPW_R0061382 S-Adenosylmethionine + Coproporphyrin III <>2 Carbon dioxide +2 5'-Deoxyadenosine +2 L-Methionine + Protoporphyrinogen IXDethiobiotin + Sulfur donor + 2 S-Adenosylmethionine + 2 e- + 2 Hydrogen ion <> Biotin +2 L-Methionine +2 5'-Deoxyadenosine2 S-Adenosylmethionine + Reduced acceptor <> S-Adenosylhomocysteine +2 L-Methionine +5 5'-Deoxyadenosine2 S-Adenosylmethionine <> S-Adenosylhomocysteine +2 L-Methionine +5 5'-Deoxyadenosine4 4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <>5 5-Aminoimidazole ribonucleotide +4 4-Amino-2-methyl-5-phosphomethylpyrimidine +5 5'-Deoxyadenosine + L-Methionine + Formic acid + CO2 S-Adenosylmethionine + Coproporphyrin III <>2 Carbon dioxide +2 5'-Deoxyadenosine +2 L-Methionine + Protoporphyrinogen IXDethiobiotin + Sulfur donor + 2 S-Adenosylmethionine + 2 e- + 2 Hydrogen ion <> Biotin +2 L-Methionine +2 5'-Deoxyadenosine2 S-Adenosylmethionine + Reduced acceptor <> S-Adenosylhomocysteine +2 L-Methionine +5 5'-Deoxyadenosine2 S-Adenosylmethionine + Coproporphyrin III <>2 Carbon dioxide +2 5'-Deoxyadenosine +2 L-Methionine + Protoporphyrinogen IXProtein N6-(octanoyl)lysine + 2 Sulfur donor + 2 S-Adenosylmethionine <> Protein N6-(lipoyl)lysine +2 L-Methionine +2 5'-Deoxyadenosine4 4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <>5 5-Aminoimidazole ribonucleotide +4 4-Amino-2-methyl-5-phosphomethylpyrimidine +5 5'-Deoxyadenosine + L-Methionine + Formic acid + CO