The Enzyme Database

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EC 2.4.2.52     
Accepted name: triphosphoribosyl-dephospho-CoA synthase
Reaction: ATP + 3′-dephospho-CoA = 2′-(5-triphospho-α-D-ribosyl)-3′-dephospho-CoA + adenine
For diagram of holo-citrate-lyase biosynthesis, click here
Other name(s): 2′-(5′′-triphosphoribosyl)-3-dephospho-CoA synthase; ATP:dephospho-CoA 5-triphosphoribosyl transferase; CitG; ATP:dephospho-CoA 5′-triphosphoribosyl transferase; MdcB; ATP:3-dephospho-CoA 5′′-triphosphoribosyltransferase; MadG
Systematic name: ATP:3′-dephospho-CoA 5-triphospho-α-D-ribosyltransferase
Comments: ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new α (1′′→2′) glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2′-(5-triphosphoribosyl)-3′-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (γ-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 313345-38-9
References:
1.  Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438–9450. [DOI] [PMID: 10924139]
2.  Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165–168. [DOI] [PMID: 11042274]
3.  Schneider, K., Kästner, C.N., Meyer, M., Wessel, M., Dimroth, P. and Bott, M. Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J. Bacteriol. 184 (2002) 2439–2446. [DOI] [PMID: 11948157]
4.  Hoenke, S., Wild, M.R. and Dimroth, P. Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase. Biochemistry 39 (2000) 13223–13232. [DOI] [PMID: 11052675]
[EC 2.4.2.52 created 2002 as EC 2.7.8.25, modified 2008, transferred 2013 to EC 2.4.2.52]
 
 
EC 2.7.7.61     
Accepted name: citrate lyase holo-[acyl-carrier protein] synthase
Reaction: 2′-(5-triphosphoribosyl)-3′-dephospho-CoA + apo-[citrate (pro-3S)-lyase] = diphosphate + holo-[citrate (pro-3S)-lyase]
For diagram of reaction, click here
Other name(s): 2′-(5′′-phosphoribosyl)-3′-dephospho-CoA transferase; 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA:apo-citrate lyase; CitX; holo-ACP synthase (ambiguous); 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA:apo-citrate lyase adenylyltransferase; 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA:apo-citrate lyase 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA transferase; 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA:apo-citrate-lyase adenylyltransferase; holo-citrate lyase synthase (incorrect); 2′-(5-triphosphoribosyl)-3′-dephospho-CoA:apo-citrate-lyase 2′-(5-phosphoribosyl)-3′-dephospho-CoA-transferase
Systematic name: 2′-(5-triphosphoribosyl)-3′-dephospho-CoA:apo-[citrate (pro-3S)-lyase] 2′-(5-phosphoribosyl)-3′-dephospho-CoA-transferase
Comments: The γ-subunit of EC 4.1.3.6, citrate (pro-3S) lyase, serves as an acyl-carrier protein (ACP) and contains the cofactor 2′-(5-triphosphoribosyl)-3′-dephospho-CoA [1,3]. Synthesis and attachment of the cofactor requires the concerted action of this enzyme and EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase [1]. In the enzyme from Escherichia coli, the cofactor is attached to serine-14 of the ACP via a phosphodiester bond.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 312492-44-7
References:
1.  Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438–9450. [DOI] [PMID: 10924139]
2.  Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165–168. [DOI] [PMID: 11042274]
3.  Schneider, K., Kästner, C.N., Meyer, M., Wessel, M., Dimroth, P. and Bott, M. Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J. Bacteriol. 184 (2002) 2439–2446. [DOI] [PMID: 11948157]
[EC 2.7.7.61 created 2002, modified 2008, modified 2023]
 
 
EC 2.7.7.66     
Accepted name: malonate decarboxylase holo-[acyl-carrier protein] synthase
Reaction: 2′-(5-triphosphoribosyl)-3′-dephospho-CoA + malonate decarboxylase apo-[acyl-carrier protein] = malonate decarboxylase holo-[acyl-carrier protein] + diphosphate
For diagram of reaction, click here
Other name(s): holo ACP synthase (ambiguous); 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA:apo ACP 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA transferase; MdcG; 2′-(5′′-triphosphoribosyl)-3′-dephospho-CoA:apo-malonate-decarboxylase adenylyltransferase; holo-malonate-decarboxylase synthase (incorrect)
Systematic name: 2′-(5-triphosphoribosyl)-3′-dephospho-CoA:apo-malonate-decarboxylase 2′-(5-phosphoribosyl)-3′-dephospho-CoA-transferase
Comments: The δ subunit of malonate decarboxylase serves as an an acyl-carrier protein (ACP) and contains the cofactor 2-(5-triphosphoribosyl)-3-dephospho-CoA. Two reactions are involved in the production of the holo-ACP form of this enzyme. The first reaction is catalysed by EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase. The resulting cofactor is then attached to the ACP subunit via a phosphodiester linkage to a serine residue, thus forming the holo form of the enzyme, in a manner analogous to that of EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hoenke, S., Wild, M.R. and Dimroth, P. Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase. Biochemistry 39 (2000) 13223–13232. [DOI] [PMID: 11052675]
2.  Hoenke, S., Schmid, M. and Dimroth, P. Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases. Biochemistry 39 (2000) 13233–13240. [DOI] [PMID: 11052676]
[EC 2.7.7.66 created 2008]
 
 
EC 2.7.8.7     
Accepted name: holo-[acyl-carrier-protein] synthase
Reaction: CoA-[4′-phosphopantetheine] + an apo-[acyl-carrier protein] = adenosine 3′,5′-bisphosphate + an [acyl-carrier protein]
Glossary: apo-[acyl-carrier protein] = a family of proteins or protein domains that contain a conserved serine residue, which are involved in acyl-group transfer.
[acyl-carrier protein] = holo-[acyl-carrier protein] = ACP = holo-ACP = the active form of apo-[acyl-carrier protein], in which the hydroxyl group of the conserved serine is substituted by a 4′-phosphopantetheine group, resulting in a sulfydryl group at which the acyl group to be transferred may then be substituted.
Other name(s): acyl carrier protein holoprotein (holo-ACP) synthetase; holo-ACP synthetase; coenzyme A:fatty acid synthetase apoenzyme 4′-phosphopantetheine transferase; holosynthase; acyl carrier protein synthetase; holo-ACP synthase; PPTase; AcpS; ACPS; acyl carrier protein synthase; P-pant transferase; CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase; CoA-[4′-phosphopantetheine]:apo-[acyl-carrier-protein] 4′-pantetheinephosphotransferase
Systematic name: CoA-[4′-phosphopantetheine]:apo-[acyl-carrier protein] 4′-pantetheinephosphotransferase
Comments: Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4′-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty-acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-30-1
References:
1.  Elovson, J. and Vagelos, P.R. Acyl carrier protein. X. Acyl carrier protein synthetase. J. Biol. Chem. 243 (1968) 3603–3611. [PMID: 4872726]
2.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013]
3.  Lambalot, R.H., Gehring, A.M., Flugel, R.S., Zuber, P., LaCelle, M., Marahiel, M.A., Reid, R., Khosla, C. and Walsh, C.T. A new enzyme superfamily - the phosphopantetheinyl transferases. Chem. Biol. 3 (1996) 923–936. [DOI] [PMID: 8939709]
4.  Walsh, C.T., Gehring, A.M., Weinreb, P.H., Quadri, L.E.N. and Flugel, R.S. Post-translational modification of polyketide and nonribosomal peptide synthases. Curr. Opin. Chem. Biol. 1 (1997) 309–315. [DOI] [PMID: 9667867]
5.  Mootz, H.D., Finking, R. and Marahiel, M.A. 4′-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J. Biol. Chem. 276 (2001) 37289–37298. [DOI] [PMID: 11489886]
6.  Joshi, A.K., Zhang, L., Rangan, V.S. and Smith, S. Cloning, expression, and characterization of a human 4′-phosphopantetheinyl transferase with broad substrate specificity. J. Biol. Chem. 278 (2003) 33142–33149. [DOI] [PMID: 12815048]
[EC 2.7.8.7 created 1972, modified 2006, modified 2022]
 
 
EC 2.7.8.25      
Transferred entry: triphosphoribosyl-dephospho-CoA synthase. Now EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase
[EC 2.7.8.25 created 2002, modified 2008, deleted 2013]
 
 
EC 3.1.1.85     
Accepted name: pimelyl-[acyl-carrier protein] methyl ester esterase
Reaction: pimeloyl-[acyl-carrier protein] methyl ester + H2O = pimeloyl-[acyl-carrier protein] + methanol
Other name(s): BioH
Systematic name: pimeloyl-[acyl-carrier protein] methyl ester hydrolase
Comments: Involved in biotin biosynthesis in Gram-negative bacteria. The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains [1,2]. Even though the enzyme can interact with coenzyme A thioesters [3], the in vivo role of the enzyme is to hydrolyse the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalysed by the fatty acid elongation enzymes [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sanishvili, R., Yakunin, A.F., Laskowski, R.A., Skarina, T., Evdokimova, E., Doherty-Kirby, A., Lajoie, G.A., Thornton, J.M., Arrowsmith, C.H., Savchenko, A., Joachimiak, A. and Edwards, A.M. Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli. J. Biol. Chem. 278 (2003) 26039–26045. [DOI] [PMID: 12732651]
2.  Lemoine, Y., Wach, A. and Jeltsch, J.M. To be free or not: the fate of pimelate in Bacillus sphaericus and in Escherichia coli. Mol. Microbiol. 19 (1996) 645–647. [DOI] [PMID: 8830257]
3.  Tomczyk, N.H., Nettleship, J.E., Baxter, R.L., Crichton, H.J., Webster, S.P. and Campopiano, D.J. Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway. FEBS Lett. 513 (2002) 299–304. [DOI] [PMID: 11904168]
4.  Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [DOI] [PMID: 20693992]
[EC 3.1.1.85 created 2011]
 
 
EC 3.1.2.14     
Accepted name: oleoyl-[acyl-carrier-protein] hydrolase
Reaction: an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate
Other name(s): acyl-[acyl-carrier-protein] hydrolase; acyl-ACP-hydrolase; acyl-acyl carrier protein hydrolase; oleoyl-ACP thioesterase; oleoyl-acyl carrier protein thioesterase; oleoyl-[acyl-carrier-protein] hydrolase
Systematic name: oleoyl-[acyl-carrier protein] hydrolase
Comments: Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68009-83-6
References:
1.  Ohlrogge, J.B., Shine, W.E. and Stumpf, P.K. Fat metabolism in higher plants. Characterization of plant acyl-ACP and acyl-CoA hydrolases. Arch. Biochem. Biophys. 189 (1978) 382–391. [DOI] [PMID: 30409]
2.  Shine, W.E., Mancha, M. and Stumpf, P.K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of acyl-coenzymes A and acyl-acyl carrier proteins. Arch. Biochem. Biophys. 172 (1976) 110–116. [DOI] [PMID: 3134]
[EC 3.1.2.14 created 1984]
 
 
EC 3.1.2.21     
Accepted name: dodecanoyl-[acyl-carrier-protein] hydrolase
Reaction: a dodecanoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + dodecanoate
Other name(s): lauryl-acyl-carrier-protein hydrolase; dodecanoyl-acyl-carrier-protein hydrolase; dodecyl-acyl-carrier protein hydrolase; dodecanoyl-[acyl-carrier protein] hydrolase; dodecanoyl-[acyl-carrier-protein] hydrolase
Systematic name: dodecanoyl-[acyl-carrier protein] hydrolase
Comments: Acts on the acyl-carrier-protein thioester of C12 and, with a much lower activity, C14 fatty acids. The derivative of oleic acid is hydrolysed very slowly (cf. EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 137903-37-8
References:
1.  Pollard, M.R., Anderson, L., Fan, C., Hawkins, D.J., Davies, H.M. A specific acyl-ACP thioesterase implicated in medium-chain fatty acid production in immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 284 (1991) 306–312. [DOI] [PMID: 1989513]
2.  Davies, H.M., Anderson, L., Fan, C., Hawkins, D.J. Developmental induction, purification, and further characterization of 12:0-ACP thioesterase from immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 290 (1991) 37–45. [DOI] [PMID: 1898097]
[EC 3.1.2.21 created 1999]
 
 
EC 3.1.4.14     
Accepted name: [acyl-carrier-protein] phosphodiesterase
Reaction: holo-[acyl-carrier protein] + H2O = 4′-phosphopantetheine + apo-[acyl-carrier protein]
Other name(s): ACP hydrolyase; ACP phosphodiesterase; AcpH; [acyl-carrier-protein] 4′-pantetheine-phosphohydrolase; holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase
Systematic name: holo-[acyl-carrier protein] 4′-pantetheine-phosphohydrolase
Comments: The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier protein (ACP) and short-chain ACPs over the medium- and long-chain species [3]. Deletion of the gene encoding this enzyme abolishes ACP cofactor turnover in vivo [3]. Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7, holo-[acyl-carrier-protein] synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-21-4
References:
1.  Sobhy, C. Regulation of fatty acid synthetase activity. The 4′-phosphopantetheine hydrolase of rat liver. J. Biol. Chem. 254 (1979) 8561–8566. [DOI] [PMID: 224058]
2.  Vagelos, P.R. and Larrabee, A.R. Acyl carrier protein. IX. Acyl carrier protein hydrolase. J. Biol. Chem. 242 (1967) 1776–1781. [DOI] [PMID: 4290442]
3.  Thomas, J. and Cronan, J.E. The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization. J. Biol. Chem. 280 (2005) 34675–34683. [DOI] [PMID: 16107329]
[EC 3.1.4.14 created 1972, modified 2006]
 
 
EC 4.1.1.124     
Accepted name: malonyl-[acp] decarboxylase
Reaction: malonyl-[acp] = acetyl-[acp] + CO2
Other name(s): decarboxylative ketosynthase; bryQ (gene name); mupG (gene name); pksF (gene name); curC (gene name); jamG (gene name); pedM (gene name)
Systematic name: malonyl-[acyl-carrier protein] carboxy-lyase
Comments: This family of enzymes participates in a process that introduces a methyl branch into nascent polyketide products. The process begins with EC 4.1.1.124, malonyl-[acp] decarboxylase, which converts the common extender unit malonyl-[acp] to acetyl-[acp]. The enzyme is a mutated form of a ketosynthase enzyme, in which a Cys residue in the active site is modified to a Ser residue, leaving the decarboxylase function intact, but nulifying the ability of the enzyme to form a carbon-carbon bond. Next, EC 2.3.3.22, 3-carboxymethyl-3-hydroxy-acyl-[acp] synthase, utilizes the acetyl group to introduce the branch at the β position of 3-oxoacyl intermediates attached to a polyketide synthase, forming a 3-hydroxy-3-carboxymethyl intermediate. This is followed by dehydration catalysed by EC 4.2.1.181, 3-carboxymethyl-3-hydroxy-acyl-[acp] dehydratase (often referred to as an ECH1 domain), leaving a 3-carboxymethyl group and forming a double bond between the α and β carbons. The process concludes with decarboxylation catalysed by EC 4.1.1.125, 4-carboxy-3-alkylbut-2-enoyl-[acp] decarboxylase (often referred to as an ECH2 domain), leaving a methyl branch at the β carbon. The enzymes are usually encoded by a cluster of genes referred to as an "HMGS cassette", based on the similarity of the key enzyme to EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase. cf. EC 4.1.1.87, malonyl-[malonate decarboxylase] decarboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Simunovic, V. and Muller, R. 3-hydroxy-3-methylglutaryl-CoA-like synthases direct the formation of methyl and ethyl side groups in the biosynthesis of the antibiotic myxovirescin A. Chembiochem 8 (2007) 497–500. [DOI] [PMID: 17330904]
2.  Wu, J., Hothersall, J., Mazzetti, C., O'Connell, Y., Shields, J.A., Rahman, A.S., Cox, R.J., Crosby, J., Simpson, T.J., Thomas, C.M. and Willis, C.L. In vivo mutational analysis of the mupirocin gene cluster reveals labile points in the biosynthetic pathway: the "leaky hosepipe" mechanism. Chembiochem 9 (2008) 1500–1508. [DOI] [PMID: 18465759]
3.  Buchholz, T.J., Rath, C.M., Lopanik, N.B., Gardner, N.P., Hakansson, K. and Sherman, D.H. Polyketide β-branching in bryostatin biosynthesis: identification of surrogate acetyl-ACP donors for BryR, an HMG-ACP synthase. Chem. Biol. 17 (2010) 1092–1100. [DOI] [PMID: 21035732]
[EC 4.1.1.124 created 2023]
 
 
EC 4.1.1.125     
Accepted name: 4-carboxy-3-alkylbut-2-enoyl-[acp] decarboxylase
Reaction: a 4-carboxy-3-alkylbut-2-enoyl-[acp] = a 3-alkylbut-2-enoyl-[acp] + CO2
Other name(s): aprG (gene name); corG (gene name); pedI (gene name); mupK (gene name); 3-carboxymethyl-alk-2-enyl-[acyl-carrier protein] decarboxylase
Systematic name: 4-carboxy-3-alkylbut-2-enoyl-[acyl-carrier protein] carboxy-lyase
Comments: This family of enzymes participates in a process that introduces a methyl branch into nascent polyketide products. The process begins with EC 4.1.1.124, malonyl-[acp] decarboxylase, which converts the common extender unit malonyl-[acp] to acetyl-[acp]. The enzyme is a mutated form of a ketosynthase enzyme, in which a Cys residue in the active site is modified to a Ser residue, leaving the decarboxylase function intact, but nulifying the ability of the enzyme to form a carbon-carbon bond. Next, EC 2.3.3.22, 3-carboxymethyl-3-hydroxy-acyl-[acp] synthase, utilizes the acetyl group to introduce the branch at the β position of 3-oxoacyl intermediates attached to a polyketide synthase, forming a 3-hydroxy-3-carboxymethyl intermediate. This is followed by dehydration catalysed by EC 4.2.1.181, 3-carboxymethyl-3-hydroxy-acyl-[acp] dehydratase (often referred to as an ECH1 domain), leaving a 3-carboxymethyl group and forming a double bond between the α and β carbons. The process concludes with decarboxylation catalysed by EC 4.1.1.125, 4-carboxy-3-alkylbut-2-enoyl-[acp] decarboxylase (often referred to as an ECH2 domain), leaving a methyl branch at the β carbon. The enzymes are usually encoded by a cluster of genes referred to as an "HMGS cassette", based on the similarity of the key enzyme to EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Geders, T.W., Gu, L., Mowers, J.C., Liu, H., Gerwick, W.H., Hakansson, K., Sherman, D.H. and Smith, J.L. Crystal structure of the ECH2 catalytic domain of CurF from Lyngbya majuscula. Insights into a decarboxylase involved in polyketide chain β-branching. J. Biol. Chem. 282 (2007) 35954–35963. [DOI] [PMID: 17928301]
2.  Erol, O., Schaberle, T.F., Schmitz, A., Rachid, S., Gurgui, C., El Omari, M., Lohr, F., Kehraus, S., Piel, J., Muller, R. and Konig, G.M. Biosynthesis of the myxobacterial antibiotic corallopyronin A. Chembiochem 11 (2010) 1253–1265. [DOI] [PMID: 20503218]
3.  Grindberg, R.V., Ishoey, T., Brinza, D., Esquenazi, E., Coates, R.C., Liu, W.T., Gerwick, L., Dorrestein, P.C., Pevzner, P., Lasken, R. and Gerwick, W.H. Single cell genome amplification accelerates identification of the apratoxin biosynthetic pathway from a complex microbial assemblage. PLoS One 6:e18565 (2011). [DOI] [PMID: 21533272]
[EC 4.1.1.125 created 2023]
 
 
EC 4.1.99.5     
Accepted name: aldehyde oxygenase (deformylating)
Reaction: a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+
Glossary: a long-chain aldehyde = an aldehyde derived from a fatty acid with an aliphatic chain of 13-22 carbons.
Other name(s): decarbonylase; aldehyde decarbonylase; octadecanal decarbonylase; octadecanal alkane-lyase
Systematic name: a long-chain aldehyde alkane-lyase
Comments: Contains a diiron center. Involved in the biosynthesis of alkanes. The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C15 and C17 alkanes [2,3]. The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents [1]. The substrate for this enzyme is formed by EC 1.2.1.80, acyl-[acyl-carrier protein] reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 94185-90-7
References:
1.  Cheesbrough, T.M. and, K olattukudy, P.E. Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum. Proc. Natl. Acad. Sci. USA 81 (1984) 6613–6617. [DOI] [PMID: 6593720]
2.  Schirmer, A., Rude, M.A., Li, X., Popova, E. and del Cardayre, S.B. Microbial biosynthesis of alkanes. Science 329 (2010) 559–562. [DOI] [PMID: 20671186]
3.  Warui, D.M., Li, N., Nørgaard, H., Krebs, C., Bollinger, J.M. and Booker, S.J. Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase. J. Am. Chem. Soc. 133 (2011) 3316–3319. [DOI] [PMID: 21341652]
4.  Li, N., Chang, W.C., Warui, D.M., Booker, S.J., Krebs, C. and Bollinger, J.M., Jr. Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases. Biochemistry 51 (2012) 7908–7916. [DOI] [PMID: 22947199]
[EC 4.1.99.5 created 1989, modified 2011, modified 2013]
 
 
EC 4.2.1.58      
Deleted entry: crotonoyl-[acyl-carrier-protein] hydratase. The reaction described is covered by EC 4.2.1.59.
[EC 4.2.1.58 created 1972, deleted 2012]
 
 
EC 4.2.1.59     
Accepted name: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
Reaction: a (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O
Other name(s): fabZ (gene name); fabA (gene name); D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase; D-3-hydroxyoctanoyl-acyl carrier protein dehydratase; β-hydroxyoctanoyl-acyl carrier protein dehydrase; β-hydroxyoctanoyl thioester dehydratase; β-hydroxyoctanoyl-ACP-dehydrase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase (oct-2-enoyl-[acyl-carrier protein]-forming); 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase
Systematic name: (3R)-3-hydroxyacyl-[acyl-carrier protein] hydro-lyase (trans-2-enoyl-[acyl-carrier protein]-forming)
Comments: This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The enzyme uses fatty acyl thioesters of ACP in vivo. Different forms of the enzyme may have preferences for substrates with different chain length. For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyses EC 5.3.3.14, trans-2-decenoyl-[acyl-carrier protein] isomerase. Despite the differences both forms can catalyse all steps leading to the synthesis of palmitate (C16:0). FabZ, but not FabA, can also accept unsaturated substrates [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-85-7
References:
1.  Mizugaki, M., Swindell, A.C. and Wkil, S.J. Intermediate- and long-chain β-hydroxyacyl-ACP dehydrases from E. coli fatty acid synthetase. Biochem. Biophys. Res. Commun. 33 (1968) 520–527. [DOI] [PMID: 4881058]
2.  Sharma, A., Henderson, B.S., Schwab, J.M. and Smith, J.L. Crystallization and preliminary X-ray analysis of β-hydroxydecanoyl thiol ester dehydrase from Escherichia coli. J. Biol. Chem. 265 (1990) 5110–5112. [PMID: 2180957]
3.  Mohan, S., Kelly, T.M., Eveland, S.S., Raetz, C.R. and Anderson, M.S. An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis. J. Biol. Chem. 269 (1994) 32896–32903. [PMID: 7806516]
4.  Heath, R.J. and Rock, C.O. Roles of the FabA and FabZ β-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J. Biol. Chem. 271 (1996) 27795–27801. [DOI] [PMID: 8910376]
[EC 4.2.1.59 created 1972, modified 2012]
 
 
EC 4.2.1.60      
Deleted entry: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59.
[EC 4.2.1.60 created 1972, modified 2006, deleted 2012]
 
 
EC 4.2.1.61      
Deleted entry: 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. The reaction described is covered by EC 4.2.1.59.
[EC 4.2.1.61 created 1972, deleted 2012]
 
 
EC 4.2.1.181     
Accepted name: 3-carboxymethyl-3-hydroxy-acyl-[acp] dehydratase
Reaction: a 3-carboxymethyl-3-hydroxy-acyl-[acyl-carrier protein] = a 4-carboxy-3-alkylbut-2-enoyl-[acyl-carrier protein] + H2O
Other name(s): aprF (gene name); corF (gene name); curE (gene name); pedL (gene name); 3-carboxymethyl-3-hydroxy-acyl-[acyl-carrier protein] dehydratase
Systematic name: 3-carboxymethyl-3-hydroxy-acyl-[acyl-carrier protein] hydro-lyase
Comments: This family of enzymes participates in a process that introduces a methyl branch into nascent polyketide products. The process begins with EC 4.1.1.124, malonyl-[acp] decarboxylase, which converts the common extender unit malonyl-[acp] to acetyl-[acp]. The enzyme is a mutated form of a ketosynthase enzyme, in which a Cys residue in the active site is modified to a Ser residue, leaving the decarboxylase function intact, but nulifying the ability of the enzyme to form a carbon-carbon bond. Next, EC 2.3.3.22, 3-carboxymethyl-3-hydroxy-acyl-[acp] synthase, utilizes the acetyl group to introduce the branch at the β position of 3-oxoacyl intermediates attached to a polyketide synthase, forming a 3-hydroxy-3-carboxymethyl intermediate. This is followed by dehydration catalysed by EC 4.2.1.181, 3-carboxymethyl-3-hydroxy-acyl-[acp] dehydratase (often referred to as an ECH1 domain), leaving a 3-carboxymethyl group and forming a double bond between the α and β carbons. The process concludes with decarboxylation catalysed by EC 4.1.1.125, 4-carboxy-3-alkylbut-2-enoyl-[acp] decarboxylase (often referred to as an ECH2 domain), leaving a methyl branch at the β carbon. The enzymes are usually encoded by a cluster of genes referred to as an "HMGS cassette", based on the similarity of the key enzyme to EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase. cf. EC 4.2.1.18, methylglutaconyl-CoA hydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gu, L., Jia, J., Liu, H., Hakansson, K., Gerwick, W.H. and Sherman, D.H. Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: functional identification of a mechanistically diverse enzyme pair. J. Am. Chem. Soc. 128 (2006) 9014–9015. [DOI] [PMID: 16834357]
2.  Gu, L., Wang, B., Kulkarni, A., Geders, T.W., Grindberg, R.V., Gerwick, L., Hakansson, K., Wipf, P., Smith, J.L., Gerwick, W.H. and Sherman, D.H. Metamorphic enzyme assembly in polyketide diversification. Nature 459 (2009) 731–735. [DOI] [PMID: 19494914]
3.  Erol, O., Schaberle, T.F., Schmitz, A., Rachid, S., Gurgui, C., El Omari, M., Lohr, F., Kehraus, S., Piel, J., Muller, R. and Konig, G.M. Biosynthesis of the myxobacterial antibiotic corallopyronin A. Chembiochem 11 (2010) 1253–1265. [DOI] [PMID: 20503218]
4.  Grindberg, R.V., Ishoey, T., Brinza, D., Esquenazi, E., Coates, R.C., Liu, W.T., Gerwick, L., Dorrestein, P.C., Pevzner, P., Lasken, R. and Gerwick, W.H. Single cell genome amplification accelerates identification of the apratoxin biosynthetic pathway from a complex microbial assemblage. PLoS One 6:e18565 (2011). [DOI] [PMID: 21533272]
[EC 4.2.1.181 created 2023]
 
 
EC 4.3.2.11     
Accepted name: (3R)-3-[(carboxylmethyl)amino]fatty acid synthase
Reaction: (3R)-3-[(carboxylmethyl)amino]fatty acid + an [acyl-carrier protein] = a (2E)-unsaturated fatty acyl-[acyl-carrier protein] + glycine + H2O
Other name(s): scoD (gene name); mmaD (gene name)
Systematic name: (3R)-3-[(carboxylmethyl)amino]fatty acid glycine-lyase ((2E)-unsaturated fatty acyl-[acyl-carrier protein]-forming)
Comments: The enzyme, found in some actinobacterial species, participates in the biosynthesis of isonitrile-containing lipopeptides. It catalyses the formation of (3R)-3-[(carboxylmethyl)amino]fatty acid by the addition of glycine and the release of the product from the acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Harris, N.C., Sato, M., Herman, N.A., Twigg, F., Cai, W., Liu, J., Zhu, X., Downey, J., Khalaf, R., Martin, J., Koshino, H. and Zhang, W. Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria. Proc. Natl. Acad. Sci. USA 114 (2017) 7025–7030. [DOI] [PMID: 28634299]
2.  Harris, N.C., Born, D.A., Cai, W., Huang, Y., Martin, J., Khalaf, R., Drennan, C.L. and Zhang, W. Isonitrile formation by a non-heme iron(II)-dependent oxidase/decarboxylase. Angew. Chem. Int. Ed. Engl. 57 (2018) 9707–9710. [DOI] [PMID: 29906336]
[EC 4.3.2.11 created 2022]
 
 
EC 5.3.3.14     
Accepted name: trans-2-decenoyl-[acyl-carrier protein] isomerase
Reaction: a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]
Other name(s): β-hydroxydecanoyl thioester dehydrase; trans-2-cis-3-decenoyl-ACP isomerase; trans-2,cis-3-decenoyl-ACP isomerase; trans-2-decenoyl-ACP isomerase; FabM; decenoyl-[acyl-carrier-protein] Δ2-trans-Δ3-cis-isomerase
Systematic name: decenoyl-[acyl-carrier protein] Δ2-trans-Δ3-cis-isomerase
Comments: While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-80-2
References:
1.  Brock, D.J.H., Kass, L.R. and Bloch, K. β-Hydroxydecanoyl thioester dehydrase. II. Mode of action. J. Biol. Chem. 242 (1967) 4432–4440. [PMID: 4863740]
2.  Bloch, K. Enzymatic synthesis of monounsaturated fatty acids. Acc. Chem. Res. 2 (1969) 193–202.
3.  Marrakchi, H., Choi, K.H. and Rock, C.O. A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae. J. Biol. Chem. 277 (2002) 44809–44816. [DOI] [PMID: 12237320]
4.  Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612–636.
[EC 5.3.3.14 created 2006]
 
 
EC 6.2.1.20     
Accepted name: long-chain-fatty-acid—[acyl-carrier-protein] ligase
Reaction: ATP + a long-chain fatty acid + an [acyl-carrier protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
Other name(s): acyl-[acyl-carrier-protein] synthetase (ambiguous); acyl-ACP synthetase (ambiguous); stearoyl-ACP synthetase; acyl-acyl carrier protein synthetase (ambiguous); long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming)
Systematic name: long-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)
Comments: The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein. Not identical with EC 6.2.1.3 long-chain-fatty-acid—CoA ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 77322-37-3
References:
1.  Ray, T.K. and Cronan, J.E., Jr. Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli. Proc. Natl. Acad. Sci. USA 73 (1976) 4374–4378. [DOI] [PMID: 794875]
2.  Kaczmarzyk, D. and Fulda, M. Fatty acid activation in cyanobacteria mediated by acyl-acyl carrier protein synthetase enables fatty acid recycling. Plant Physiol. 152 (2010) 1598–1610. [DOI] [PMID: 20061450]
[EC 6.2.1.20 created 1986]
 
 
EC 6.2.1.35     
Accepted name: acetate—[acyl-carrier protein] ligase
Reaction: ATP + acetate + an [acyl-carrier protein] = AMP + diphosphate + an acetyl-[acyl-carrier protein]
For diagram of malonate decarboxylase, click here
Other name(s): HS-acyl-carrier protein:acetate ligase; [acyl-carrier protein]:acetate ligase; MadH; ACP-SH:acetate ligase
Systematic name: acetate:[acyl-carrier-protein] ligase (AMP-forming)
Comments: This enzyme, from the anaerobic bacterium Malonomonas rubra, is a component of the multienzyme complex EC 7.2.4.4, biotin-dependent malonate decarboxylase. The enzyme uses the energy from hydrolysis of ATP to convert the thiol group of the acyl-carrier-protein-bound 2′-(5-phosphoribosyl)-3′-dephospho-CoA cofactor into its acetyl thioester [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hilbi, H., Dehning, I., Schink, B. and Dimroth, P. Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem. 207 (1992) 117–123. [DOI] [PMID: 1628643]
2.  Berg, M., Hilbi, H. and Dimroth, P. The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5"-phosphoribosyl)-3′-dephosphocoenzyme A as a prosthetic group. Biochemistry 35 (1996) 4689–4696. [DOI] [PMID: 8664258]
3.  Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103–115. [DOI] [PMID: 9128730]
4.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 6.2.1.35 created 2008, modified 2018]
 
 
EC 6.2.1.47     
Accepted name: medium-chain-fatty-acid—[acyl-carrier-protein] ligase
Reaction: ATP + a medium-chain fatty acid + a holo-[acyl-carrier protein] = AMP + diphosphate + a medium-chain acyl-[acyl-carrier protein]
Other name(s): jamA (gene name)
Systematic name: medium-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)
Comments: The enzyme ligates medium chain fatty acids (with aliphatic chain of 6-12 carbons) to an acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77322-37-3
References:
1.  Edwards, D.J., Marquez, B.L., Nogle, L.M., McPhail, K., Goeger, D.E., Roberts, M.A. and Gerwick, W.H. Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula. Chem. Biol. 11 (2004) 817–833. [DOI] [PMID: 15217615]
2.  Zhu, X., Liu, J. and Zhang, W. De novo biosynthesis of terminal alkyne-labeled natural products. Nat. Chem. Biol. 11 (2015) 115–120. [DOI] [PMID: 25531891]
[EC 6.2.1.47 created 2016]
 
 
EC 6.2.1.74     
Accepted name: 3-amino-5-hydroxybenzoate—[acyl-carrier protein] ligase
Reaction: ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein] = 3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate
Other name(s): rifA (gene name); mitE (gene name)
Systematic name: 3-amino-5-hydroxybenzoate:[acyl carrier protein] ligase (AMP-forming)
Comments: During the biosynthesis of most ansamycin antibiotics such as rifamycins, streptovaricins, naphthomycins, and chaxamycins, the activity is catalysed by the loading domain of the respective polyketide synthase (PKS), which transfers the substrate to the acyl-carrier protein domain of the first extension module of the PKS. During the biosynthesis of the mitomycins the reaction is catalysed by the MitE protein, which transfers the substrate to a dedicated acyl-carrier protein (MmcB).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Admiraal, S.J., Walsh, C.T. and Khosla, C. The loading module of rifamycin synthetase is an adenylation-thiolation didomain with substrate tolerance for substituted benzoates. Biochemistry 40 (2001) 6116–6123. [PMID: 11352749]
2.  Admiraal, S.J., Khosla, C. and Walsh, C.T. The loading and initial elongation modules of rifamycin synthetase collaborate to produce mixed aryl ketide products. Biochemistry 41 (2002) 5313–5324. [PMID: 11955082]
3.  Admiraal, S.J., Khosla, C. and Walsh, C.T. A Switch for the transfer of substrate between nonribosomal peptide and polyketide modules of the rifamycin synthetase assembly line. J. Am. Chem. Soc. 125 (2003) 13664–13665. [DOI] [PMID: 14599196]
4.  Chamberland, S., Gruschow, S., Sherman, D.H. and Williams, R.M. Synthesis of potential early-stage intermediates in the biosynthesis of FR900482 and mitomycin C. Org. Lett. 11 (2009) 791–794. [DOI] [PMID: 19161340]
[EC 6.2.1.74 created 2021]
 
 
EC 7.2.4.4     
Accepted name: biotin-dependent malonate decarboxylase
Reaction: malonate + H+ + Na+[side 1] = acetate + CO2 + Na+[side 2]
For diagram of the reactions involved in the multienzyme complex malonate decarboxylase, click here
Other name(s): malonate decarboxylase (with biotin); malonate decarboxylase (ambiguous)
Systematic name: malonate carboxy-lyase (biotin-dependent)
Comments: Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. The enzyme described here is a membrane-bound biotin-dependent, Na+-translocating enzyme [6]. The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88, biotin-independent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. Both enzymes achieve this by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-bound form of the enzyme. The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side-chain as 2-(5-triphosphoribosyl)-3-dephospho-CoA rather than as phosphopantetheine 4′-phosphate. In the anaerobic bacterium Malonomonas rubra, the components of the multienzyme complex/enzymes involved in carrying out the reactions of this enzyme are as follows: MadA (EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase), MadB (EC 7.2.4.1, carboxybiotin decarboxylase), MadC/MadD (EC 2.1.3.10, malonyl-S-ACP:biotin-protein carboxyltransferase) and MadH (EC 6.2.1.35, acetate—[acyl-carrier protein] ligase). Two other components that are involved are MadE, the acyl-carrier protein and MadF, the biotin protein. The carboxy group is lost with retention of configuration [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hilbi, H., Dehning, I., Schink, B. and Dimroth, P. Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem. 207 (1992) 117–123. [DOI] [PMID: 1628643]
2.  Hilbi, H. and Dimroth, P. Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase. Arch. Microbiol. 162 (1994) 48–56. [PMID: 18251085]
3.  Berg, M., Hilbi, H. and Dimroth, P. The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5"-phosphoribosyl)-3′-dephosphocoenzyme A as a prosthetic group. Biochemistry 35 (1996) 4689–4696. [DOI] [PMID: 8664258]
4.  Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103–115. [DOI] [PMID: 9128730]
5.  Micklefield, J., Harris, K.J., Gröger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G. Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention. J. Am. Chem. Soc. 117 (1995) 1153–1154. [DOI]
6.  Kim, Y.S. Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application. J. Biochem. Mol. Biol. 35 (2002) 443–451. [PMID: 12359084]
7.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 7.2.4.4 created 2008 as EC 4.1.1.89, transferred 2018 to EC 7.2.4.4]
 
 


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