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Escherichia coli K-12 substr. MG1655 Compound: coenzyme A

Synonyms: CoA, co-A-SH, co-enzyme-A, co-A, HS-CoA

Superclasses: a cofactor a prosthetic group

Summary from MetaCyc:
Coenzyme A (CoA) is a ubiquitous cofactor found in bacteria, plants, and animals. CoA participates in a large number of enzymatic reactions central to intermediary metabolism, including the oxidation of fatty acids, carbohydrates, and amino acids. Coenzyme A is the common acyl carrier in prokaryotic and eukaryotic cells, and is required for a multitude of reactions for both biosynthetic and degradative pathways [Rubio06].

Chemical Formula: C21H32N7O16P3S

Molecular Weight: 763.5 Daltons

Monoisotopic Molecular Weight: 767.1152083656 Daltons

SMILES: CC(C)(C(O)C(=O)NCCC(=O)NCCS)COP(=O)(OP(=O)(OCC1(OC(C(C1OP([O-])(=O)[O-])O)N3(C2(=C(C(N)=NC=N2)N=C3))))[O-])[O-]

InChI: InChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/p-4/t11-,14-,15-,16+,20-/m1/s1

InChIKey: InChIKey=RGJOEKWQDUBAIZ-IBOSZNHHSA-J

Unification Links: CAS:85-61-0 , ChEBI:57287 , HMDB:HMDB01423 , IAF1260:33502 , KEGG:C00010 , KNApSAcK:C00007258 , MetaboLights:MTBLC57287 , PubChem:25113190 , Wikipedia:Coenzyme_a

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -817.249

Reactions known to consume the compound:

1,4-dihydroxy-2-naphthoate biosynthesis I :
ATP + 2-succinylbenzoate + coenzyme A → AMP + 4-(2'-carboxyphenyl)-4-oxobutyryl-CoA + diphosphate

2-methylcitrate cycle I :
propanoate + ATP + coenzyme A → propanoyl-CoA + AMP + diphosphate

acetate conversion to acetyl-CoA :
acetate + ATP + coenzyme A → acetyl-CoA + AMP + diphosphate

acyl carrier protein metabolism I :
an apo-[acp] + coenzyme A → adenosine 3',5'-bisphosphate + a holo-[acyl-carrier protein]

fatty acid β-oxidation I :
a 2,3,4-saturated fatty acyl CoA + acetyl-CoA ↔ a 3-oxoacyl-CoA + coenzyme A
a 2,3,4-saturated fatty acid + ATP + coenzyme A → a 2,3,4-saturated fatty acyl CoA + AMP + diphosphate

L-carnitine degradation I :
L-carnitine + ATP + coenzyme A → L-carnitinyl-CoA + AMP + diphosphate

mixed acid fermentation :
formate + acetyl-CoA ← pyruvate + coenzyme A

phenylacetate degradation I (aerobic) :
succinyl-CoA + acetyl-CoA ← 3-oxoadipyl-CoA + coenzyme A
2,3-didehydroadipyl-CoA + acetyl-CoA ← 3-oxo-5,6-didehydrosuberyl-CoA + coenzyme A
phenylacetate + ATP + coenzyme A → phenylacetyl-CoA + AMP + diphosphate

pyruvate decarboxylation to acetyl CoA :
acetyl-CoA + a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine ← a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + coenzyme A

superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass :
pyruvate + coenzyme A + NAD+ → acetyl-CoA + CO2 + NADH

TCA cycle I (prokaryotic) :
2-oxoglutarate + coenzyme A + NAD+ → succinyl-CoA + CO2 + NADH

threonine degradation I :
2-oxobutanoate + coenzyme A → propanoyl-CoA + formate

Not in pathways:
isochorismatase / aryl-carrier protein + coenzyme A → EntB isochorismatase / aryl-carrier protein + adenosine 3',5'-bisphosphate
apo-serine activating enzyme + coenzyme A → adenosine 3',5'-bisphosphate + aryl carrier protein / L-seryl-AMP synthase

Reactions known to produce the compound:

1,4-dihydroxy-2-naphthoate biosynthesis I :
1,4-dihydroxy-2-naphthoyl-CoA + H2O → 1,4-dihydroxy-2-naphthoate + coenzyme A + H+

2-methylcitrate cycle I :
oxaloacetate + propanoyl-CoA + H2O → (2S,3S)-2-methylcitrate + coenzyme A + H+

anhydromuropeptides recycling , UDP-N-acetyl-D-glucosamine biosynthesis I :
D-glucosamine 1-phosphate + acetyl-CoA → N-acetyl-α-D-glucosamine 1-phosphate + coenzyme A + H+

arginine degradation II (AST pathway) :
L-arginine + succinyl-CoA → N2-succinyl-L-arginine + coenzyme A + H+

CDP-diacylglycerol biosynthesis I :
a long-chain acyl-CoA + sn-glycerol 3-phosphate → a 1-acyl-sn-glycerol 3-phosphate + coenzyme A
a long-chain acyl-CoA + a 1-acyl-sn-glycerol 3-phosphate → a 1,2-diacyl-sn-glycerol 3-phosphate + coenzyme A

coenzyme A biosynthesis I :
3'-dephospho-CoA + ATP → ADP + coenzyme A + H+

cysteine biosynthesis I :
L-serine + acetyl-CoA ↔ O-acetyl-L-serine + coenzyme A

dTDP-N-acetylthomosamine biosynthesis :
dTDP-thomosamine + acetyl-CoA → dTDP-N-acetylthomosamine + coenzyme A + H+

fatty acid biosynthesis initiation I :
acetyl-CoA + a malonyl-[acp] + H+ → an acetoacetyl-[acp] + CO2 + coenzyme A

glycolate and glyoxylate degradation II :
acetyl-CoA + glyoxylate + H2O → (S)-malate + coenzyme A + H+

glyoxylate cycle :
acetyl-CoA + glyoxylate + H2O → (S)-malate + coenzyme A + H+
oxaloacetate + acetyl-CoA + H2O → citrate + coenzyme A + H+

leucine biosynthesis :
3-methyl-2-oxobutanoate + acetyl-CoA + H2O → (2S)-2-isopropylmalate + coenzyme A + H+

lysine biosynthesis I :
(S)-2,3,4,5-tetrahydrodipicolinate + succinyl-CoA + H2O → N-succinyl-2-amino-6-ketopimelate + coenzyme A

methionine biosynthesis I :
L-homoserine + succinyl-CoA → O-succinyl-L-homoserine + coenzyme A

mixed acid fermentation , TCA cycle I (prokaryotic) :
oxaloacetate + acetyl-CoA + H2O → citrate + coenzyme A + H+

oleate β-oxidation :
3-trans,5-cis-tetradecadienoyl-CoA + H2O → (3E,5Z)-tetradecadienoate + coenzyme A + H+

threonine degradation I :
propanoyl-CoA + phosphate → propanoyl phosphate + coenzyme A

Not in pathways:
a ribosomal protein-L-alanine + acetyl-CoA → a ribosomal protein-N-acetyl-L-alanine + coenzyme A
acetyl-CoA + spermidine → N1-acetylspermidine + coenzyme A + H+
50S ribosomal subunit protein L12 + acetyl-CoA → 50S ribosomal subunit protein L7 + coenzyme A
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+
a 2,3,4-saturated fatty acyl CoA[periplasmic space] + H2O[periplasmic space] → a 2,3,4-saturated fatty acid[periplasmic space] + coenzyme A[periplasmic space] + H+[periplasmic space]
L-alanine + pimeloyl-CoA + H+ → CO2 + 8-amino-7-oxononanoate + coenzyme A
3-hydroxybenzoyl-CoA + H2O → 3-hydroxybenzoate + coenzyme A + H+
a cytidine34 in tRNAmet + ATP + acetyl-CoA + H2O → [elongator tRNAmet]-N4-acetylcytidine34 + ADP + coenzyme A + phosphate + H+
(R)-3-hydroxybutanoyl-CoA + H2O → (R)-3-hydroxybutanoate + coenzyme A + H+
(S)-3-hydroxybutanoyl-CoA + H2O → (S)-3-hydroxybutanoate + coenzyme A + H+

Reactions known to both consume and produce the compound:

2'-deoxy-α-D-ribose 1-phosphate degradation , 2-oxopentenoate degradation , ethanol degradation I , threonine degradation IV :
acetaldehyde + coenzyme A + NAD+ ↔ acetyl-CoA + NADH + H+

2-oxoglutarate decarboxylation to succinyl-CoA :
succinyl-CoA + a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine → a [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine + coenzyme A

acetate formation from acetyl-CoA I :
acetyl-CoA + phosphate ↔ acetyl phosphate + coenzyme A

acetoacetate degradation (to acetyl CoA) :
2 acetyl-CoA ↔ acetoacetyl-CoA + coenzyme A

fatty acid biosynthesis initiation I :
a holo-[acyl-carrier protein] + malonyl-CoA ↔ a malonyl-[acp] + coenzyme A

fatty acid biosynthesis initiation II , superpathway of fatty acid biosynthesis initiation (E. coli) :
a holo-[acyl-carrier protein] + acetyl-CoA ↔ an acetyl-[acp] + coenzyme A

mixed acid fermentation :
acetyl-CoA + phosphate ↔ acetyl phosphate + coenzyme A
acetaldehyde + coenzyme A + NAD+ ↔ acetyl-CoA + NADH + H+

ornithine biosynthesis :
L-glutamate + acetyl-CoA ↔ N-acetyl-L-glutamate + coenzyme A + H+

TCA cycle I (prokaryotic) :
succinate + ATP + coenzyme A ↔ succinyl-CoA + ADP + phosphate

threonine degradation II :
glycine + acetyl-CoA ↔ 2-amino-3-oxobutanoate + coenzyme A + H+

Not in pathways:
a β-D-galactoside + acetyl-CoA ↔ a 6-acetyl-β-D-galactoside + coenzyme A
maltose + acetyl-CoA ↔ acetylmaltose + coenzyme A
propanoyl-CoA + glyoxylate + H2O ↔ 2-hydroxyglutarate + coenzyme A + H+
pyruvate + an oxidized flavodoxin + coenzyme A + H+ ↔ acetyl-CoA + CO2 + a reduced flavodoxin
pyruvate + 2 an oxidized ferredoxin + coenzyme A ↔ acetyl-CoA + CO2 + 2 a reduced ferredoxin + H+

In Reactions of unknown directionality:

Not in pathways:
an N-hydroxy-arylamine + acetyl-CoA = an N-acetoxyarylamine + coenzyme A
3,4-dihydroxyphenylacetyl-CoA + H2O = 3,4-dihydroxyphenylacetate + coenzyme A + H+
an aliphatic α,ω-diamine + acetyl-CoA = an aliphatic N-acetyl-diamine + coenzyme A + H+
aminomethylphosphonate + acetyl-CoA = 2-N-acetamidomethylphosphonate + coenzyme A
acetyl-CoA + dihydrolipoamide = S-acetyldihydrolipoamide + coenzyme A
L-methionine + acetyl-CoA = N-α-acetyl-L-methionine + coenzyme A + H+
an arylamine + acetyl-CoA = an N-acetylarylamine + coenzyme A
3-cis-dodecenoyl-CoA + acetyl-CoA = 3-keto-5-cis-tetradecenoyl-CoA + coenzyme A
2-hydroxycyclohepta-1,4,6-triene-1-carboxyl-CoA + H2O = 2-hydroxycyclohepta-1,4,6-triene-1-carboxylate + coenzyme A
phenylacetyl-CoA + H2O = phenylacetate + coenzyme A + H+

Enzymes inhibited by coenzyme A, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: oxalyl-CoA decarboxylase [Werther10] , phosphopantetheine adenylyltransferase [Miller07] , acetoacetyl-CoA transferase [Comment 1] , galactoside O-acetyltransferase [Musso73] , maltose acetyltransferase [Comment 2] , pantothenate kinase [Vallari87, Song94, Comment 3] , acetyl-CoA:ACP transacylase [Lowe88, Comment 4] , malonyl-CoA-ACP transacylase [Joshi71, Comment 5]

Inhibitor (Noncompetitive) of: phosphoglucomutase [Duckworth73, Sanwal72]

Inhibitor (Allosteric) of: malate dehydrogenase, NAD-requiring [Milne79]

Inhibitor (Mechanism unknown) of: formyl-CoA transferase [Toyota08] , acyl-CoA thioesterase [Zhuang08] , 3-methyl-2-oxobutanoate hydroxymethyltransferase [Powers76, Comment 6] , 6-phosphogluconate dehydrogenase , acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase [Green81, Helmward89] , glutamine synthetase adenylyltransferase [Ebner70, Comment 7] , 2-amino-3-ketobutyrate CoA ligase [Comment 8]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: pyruvate formate-lyase deactivase


References

Brand91: Brand B, Boos W (1991). "Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000." J Biol Chem 1991;266(21);14113-8. PMID: 1856235

Duckworth73: Duckworth HW, Barber BH, Sanwal BD (1973). "The interaction of phosphoglucomutase with nucleotide inhibitors." J Biol Chem 248(4);1431-5. PMID: 4568817

Ebner70: Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H (1970). "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties." Eur J Biochem 1970;14(3);535-44. PMID: 4920894

Green81: Green PR, Merrill AH, Bell RM (1981). "Membrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase." J Biol Chem 1981;256(21);11151-9. PMID: 7026564

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Joshi71: Joshi VC, Wakil SJ (1971). "Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli." Arch Biochem Biophys 1971;143(2);493-505. PMID: 4934182

Lowe88: Lowe PN, Rhodes S (1988). "Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli." Biochem J 1988;250(3);789-96. PMID: 3291856

Miller07: Miller JR, Ohren J, Sarver RW, Mueller WT, de Dreu P, Case H, Thanabal V (2007). "Phosphopantetheine adenylyltransferase from Escherichia coli: investigation of the kinetic mechanism and role in regulation of coenzyme A biosynthesis." J Bacteriol 189(22);8196-205. PMID: 17873050

Milne79: Milne JA, Cook RA (1979). "Role of metal cofactors in enzyme regulation. Differences in the regulatory properties of the Escherichia coli nicotinamide adenine dinucleotide specific malic enzyme depending on whether Mg2+ or Mn2+ serves as divalent cation." Biochemistry 18(16);3604-10. PMID: 224913

Mukherjee87: Mukherjee JJ, Dekker EE (1987). "Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme." J Biol Chem 1987;262(30);14441-7. PMID: 3117785

Musso73: Musso RE, Zabin I (1973). "Substrate specificity and kinetic studies on thiogalactoside transacetylase." Biochemistry 1973;12(3);553-7. PMID: 4630409

Powers76: Powers SG, Snell EE (1976). "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties." J Biol Chem 1976;251(12);3786-93. PMID: 6463

Rubio06: Rubio S, Larson TR, Gonzalez-Guzman M, Alejandro S, Graham IA, Serrano R, Rodriguez PL (2006). "An Arabidopsis mutant impaired in coenzyme A biosynthesis is sugar dependent for seedling establishment." Plant Physiol 140(3);830-43. PMID: 16415216

Sanwal72: Sanwal BD, Duckworth HW, Hollier ML (1972). "Regulation of phosphoglucomutase." Biochem J 128(1);26P-27P. PMID: 4563765

Song94: Song WJ, Jackowski S (1994). "Kinetics and regulation of pantothenate kinase from Escherichia coli." J Biol Chem 1994;269(43);27051-8. PMID: 7929447

Sramek77: Sramek SJ, Frerman FE, McCormick DJ, Duncombe GR (1977). "Substrate-induced conformational changes and half-the-sites reactivity in the Escherichia coli CoA transferase." Arch Biochem Biophys 1977;181(2);525-33. PMID: 332081

Toyota08: Toyota CG, Berthold CL, Gruez A, Jonsson S, Lindqvist Y, Cambillau C, Richards NG (2008). "Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase." J Bacteriol 190(7):2556-64. PMID: 18245280

Vallari87: Vallari DS, Jackowski S, Rock CO (1987). "Regulation of pantothenate kinase by coenzyme A and its thioesters." J Biol Chem 1987;262(6);2468-71. PMID: 3029083

Werther10: Werther T, Zimmer A, Wille G, Golbik R, Weiss MS, Konig S (2010). "New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli." FEBS J 277(12);2628-40. PMID: 20553497

Zhuang08: Zhuang Z, Song F, Zhao H, Li L, Cao J, Eisenstein E, Herzberg O, Dunaway-Mariano D (2008). "Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA." Biochemistry 47(9);2789-96. PMID: 18247525


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc13.