KEGG   ENZYME: 2.1.3.1
Entry
EC 2.1.3.1                  Enzyme                                 

Name
methylmalonyl-CoA carboxytransferase;
transcarboxylase;
methylmalonyl coenzyme A carboxyltransferase;
methylmalonyl-CoA transcarboxylase;
oxalacetic transcarboxylase;
methylmalonyl-CoA carboxyltransferase;
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase;
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase carboxytransferase [incorrect]
Class
Transferases;
Transferring one-carbon groups;
Carboxy- and carbamoyltransferases
Sysname
(S)-methylmalonyl-CoA:pyruvate carboxytransferase
Reaction(IUBMB)
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate [RN:R00930]
Reaction(KEGG)
R00930;
(other) R00353
Substrate
(S)-methylmalonyl-CoA [CPD:C00683];
pyruvate [CPD:C00022]
Product
propanoyl-CoA [CPD:C00100];
oxaloacetate [CPD:C00036]
Comment
A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.
History
EC 2.1.3.1 created 1961
Pathway
ec00640  Propanoate metabolism
ec01100  Metabolic pathways
Orthology
K03416  methylmalonyl-CoA carboxyltransferase 5S subunit
K17489  methylmalonyl-CoA carboxyltransferase 12S subunit
K17490  methylmalonyl-CoA carboxyltransferase 1.3S subunit
Genes
GEM: GM21_0316 GM21_0317 GM21_0318 GM21_0319
GBM: Gbem_0334 Gbem_0335 Gbem_0336 Gbem_0337
GER: KP004_00725 KP004_00730
PPD: Ppro_0033 Ppro_0034 Ppro_0035 Ppro_3082 Ppro_3083 Ppro_3084
BCHS: JNE38_23625
SSG: Selsp_0507
SRI: SELR_10340
MHG: MHY_07420
MYV: G155_29450
MYE: AB431_25530
MAIC: MAIC_06680
MALV: MALV_37140
MAUB: MAUB_31710
CDI: DIP0739(pycB) DIP0740(mmdA) DIP0741 DIP0742
PCOR: KS4_34690
 » show all
Reference
1  [PMID:16590594]
  Authors
Swick RW, Wood HG.
  Title
THE ROLE OF TRANSCARBOXYLATION IN PROPIONIC ACID FERMENTATION.
  Journal
Proc Natl Acad Sci U S A 46:28-41 (1960)
DOI:10.1073/pnas.46.1.28
Reference
2  [PMID:3893281]
  Authors
Wood HG, Kumar GK.
  Title
Transcarboxylase: its quaternary structure and the role of the biotinyl subunit in the assembly of the enzyme and in catalysis.
  Journal
Ann N Y Acad Sci 447:1-22 (1985)
DOI:10.1111/j.1749-6632.1985.tb18422.x
Reference
3  [PMID:15188046]
  Authors
Peikert C, Seeger K, Bhat RK, Berger S.
  Title
Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR.
  Journal
Org Biomol Chem 2:1777-81 (2004)
DOI:10.1039/b404238g
Reference
4  [PMID:17134979]
  Authors
Kumar Bhat R, Berger S.
  Title
New and easy strategy for cloning, expression, purification, and characterization of the 5S subunit of transcarboxylase from Propionibacterium f. shermanii.
  Journal
Prep Biochem Biotechnol 37:13-26 (2007)
DOI:10.1080/10826060601039394
Reference
5  [PMID:15814455]
  Authors
Carey PR, Sonnichsen FD, Yee VC.
  Title
Transcarboxylase: one of nature's early nanomachines.
  Journal
IUBMB Life 56:575-83 (2004)
DOI:10.1080/15216540400022417
Other DBs
ExplorEnz - The Enzyme Database: 2.1.3.1
IUBMB Enzyme Nomenclature: 2.1.3.1
ExPASy - ENZYME nomenclature database: 2.1.3.1
UM-BBD (Biocatalysis/Biodegradation Database): 2.1.3.1
BRENDA, the Enzyme Database: 2.1.3.1
CAS: 9029-86-1
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