Oxaloacetate decarboxylase

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oxaloacetate decarboxylase
Identifiers
EC number 4.1.1.3
CAS number 9024-98-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Na+-transporting oxaloacetate decarboxylase beta subunit
Identifiers
Symbol OAD_beta
Pfam PF03977
Pfam clan CL0064
InterPro IPR005661
TCDB 3.B.1
Oxaloacetate decarboxylase, gamma chain
Identifiers
Symbol OAD_gamma
Pfam PF04277
InterPro IPR005899
TCDB 3.B.1

Oxaloacetate decarboxylase is a carboxy-lyase involved in the conversion of oxaloacetate into pyruvate.

It is categorized under EC 4.1.1.3.

In some bacteria this enzyme is a trimer, composed of alpha, beta and gamma subunits.[1][2] The beta and gamma subunits are integral membrane proteins.[2][3]

See also

References

  1. Bott M, Pfister K, Burda P, Kalbermatter O, Woehlke G, Dimroth P (December 1997). "Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex". Eur. J. Biochem. 250 (2): 590–9. doi:10.1111/j.1432-1033.1997.0590a.x. PMID 9428714. 
  2. 2.0 2.1 Laussermair E, Schwarz E, Oesterhelt D, Reinke H, Beyreuther K, Dimroth P (1989). "The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane-bound subunits beta and gamma.". J Biol Chem 264 (25): 14710–5. PMID 2549031. 
  3. Schmid M, Wild MR, Dahinden P, Dimroth P (2002). "Subunit gamma of the oxaloacetate decarboxylase Na(+) pump: interaction with other subunits/domains of the complex and binding site for the Zn(2+) metal ion.". Biochemistry 41 (4): 1285–92. doi:10.1021/bi015764l. PMID 11802728. 

Further reading

  • Dahinden P, Auchli Y, Granjon T et al. (2005). "Oxaloacetate decarboxylase of Vibrio cholerae: purification, characterization, and expression of the genes in Escherichia coli". Arch. Microbiol. 183 (2): 121–9. doi:10.1007/s00203-004-0754-5. PMID 15647905. 

External links

This article incorporates text from the public domain Pfam and InterPro IPR005661

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