EzCatDB: D00254

DB codeD00254
CATH domainDomain 11.10.12.10
Domain 23.90.226.10Catalytic domain
E.C.4.1.1.41
CSA1ef8
MACiEM0070

CATH domainRelated DB codes (homologues)
3.90.226.10M00145,M00122,S00849

Enzyme Name
Swiss-protKEGG

P52045
Protein nameMethylmalonyl-CoA decarboxylasemethylmalonyl-CoA decarboxylase
propionyl-CoA carboxylase
propionyl coenzyme A carboxylase
methylmalonyl-coenzyme A decarboxylase
(S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase [incorrect]
(S)-methylmalonyl-CoA carboxy-lyase
SynonymsMMCD
EC 4.1.1.41
Transcarboxylase

KEGG pathways
MAP codePathways
MAP00640Propanoate metabolism

Swiss-prot:Accession NumberP52045
Entry nameMMCD_ECOLI
Activity(S)-methylmalonyl-CoA = propanoyl-CoA + CO(2).
SubunitDimer of homotrimers.
Subcellular location
Cofactor


CofactorsSubstratesProducts
KEGG-idC00120C00683C00100C00011
CompoundBiotin(S)-2-Methyl-3-oxopropanoyl-CoAPropanoyl-CoACO2
Typeamide group,amine group,fatty acid,sulfide groupamine group,carbohydrate,carboxyl group,nucleotide,peptide/protein,sulfide groupamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupothers
1ef8A01UnboundUnboundUnboundUnbound
1ef8B01UnboundUnboundUnboundUnbound
1ef8C01UnboundUnboundUnboundUnbound
1ef9A01UnboundUnboundUnboundUnbound
1ef8A02UnboundUnboundUnboundUnbound
1ef8B02UnboundUnboundUnboundUnbound
1ef8C02UnboundUnboundUnboundUnbound
1ef9A02UnboundAnalogue:2CPUnboundUnbound

Active-site residues
resource
PDB;1ef8 & literature [12]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
1ef8A01
HIS 220(Nickel binding)

1ef8B01
HIS 220(Nickel binding)

1ef8C01
HIS 220(Nickel binding)

1ef9A01
                       

1ef8A02TYR 140

HIS 66;GLY 110
1ef8B02TYR 140

HIS 66;GLY 110
1ef8C02TYR 140

HIS 66;GLY 110
1ef9A02TYR 140

HIS 66;GLY 110

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.1, Fig.62
[12]Fig.6, p.4638-46392

references
[1]
PubMed ID6852015
JournalEur J Biochem
Year1983
Volume132
Pages579-87
AuthorsHilpert W, Dimroth P
TitlePurification and characterization of a new sodium-transport decarboxylase. Methylmalonyl-CoA decarboxylase from Veillonella alcalescens.
[2]
PubMed ID6705792
JournalEur J Biochem
Year1984
Volume140
Pages147-51
AuthorsHaase FC, Beegen H, Allen SH
TitlePropionyl-coenzyme A carboxylase of Mycobacterium smegmatis. An electron microscopic study.
[3]
PubMed ID3860170
JournalAnn N Y Acad Sci
Year1985
Volume447
Pages140-51
AuthorsFry DC, Fox T, Lane MD, Mildvan AS
TitleNMR studies of the exchange of the amide protons of d-biotin and its derivatives.
[4]
PubMed ID3464942
JournalProc Natl Acad Sci U S A
Year1986
Volume83
Pages8049-53
AuthorsKraus JP, Firgaira F, Novotny J, Kalousek F, Williams KR, Williamson C, Ohura T, Rosenberg LE
TitleCoding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.
[5]
PubMed ID3609308
JournalFEBS Lett
Year1987
Volume220
Pages121-5
AuthorsHoffmann A, Dimroth P
TitleStereochemistry of the methylmalonyl-CoA decarboxylation reaction.
[6]
PubMed ID1769208
JournalComp Biochem Physiol B
Year1991
Volume99
Pages613-7
AuthorsGarrastazu C, Iniesta MP, Aranguez MI, Ruiz Amil M
TitleComparative analysis of propionyl-CoA carboxylase from liver and mammary gland of mid-lactation cow.
[7]
PubMed ID8227015
JournalJ Biol Chem
Year1993
Volume268
Pages24564-71
AuthorsHuder JB, Dimroth P
TitleSequence of the sodium ion pump methylmalonyl-CoA decarboxylase from Veillonella parvula.
[8]
PubMed ID7601825
JournalJ Bacteriol
Year1995
Volume177
Pages3623-30
AuthorsHuder JB, Dimroth P
TitleExpression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli.
[9]
PubMed ID8865276
JournalPediatr Res
Year1996
Volume40
Pages404-9
AuthorsBergman AJ, Van der Knaap MS, Smeitink JA, Duran M, Dorland L, Valk J, Poll-The BT
TitleMagnetic resonance imaging and spectroscopy of the brain in propionic acidemia: clinical and biochemical considerations.
[10]
PubMed ID9683657
JournalArch Microbiol
Year1998
Volume170
Pages179-84
AuthorsKimura Y, Kojyo T, Kimura I, Sato M
TitlePropionyl-CoA carboxylase of Myxococcus xanthus: catalytic properties and function in developing cells.
[11]
PubMed ID9887338
JournalHum Mol Genet
Year1999
Volume8
Pages107-13
AuthorsCampeau E, Dupuis L, Leclerc D, Gravel RA
TitleDetection of a normally rare transcript in propionic acidemia patients with mRNA destabilizing mutations in the PCCA gene.
[12]
CommentsX-ray crystallography
PubMed ID10769118
JournalBiochemistry
Year2000
Volume39
Pages4630-9
AuthorsBenning MM, Haller T, Gerlt JA, Holden HM
TitleNew reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli.
Related PDB1ef8,1ef9
[13]
PubMed ID10769117
JournalBiochemistry
Year2000
Volume39
Pages4622-9
AuthorsHaller T, Buckel T, Retey J, Gerlt JA
TitleDiscovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli.
[14]
PubMed ID11136555
JournalMol Genet Metab
Year2000
Volume71
Pages623-32
AuthorsChloupkova M, Ravn K, Schwartz M, Kraus JP
TitleChanges in the carboxyl terminus of the beta subunit of human propionyl-CoA carboxylase affect the oligomer assembly and catalysis: expression and characterization of seven patient-derived mutant forms of PCC in Escherichia coli.
[15]
PubMed ID11414279
JournalMol Neurobiol
Year2000
Volume22
Pages21-40
AuthorsHassel B
TitleCarboxylation and anaplerosis in neurons and glia.


createdupdated
2004-05-212009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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