Oxaloacetate decarboxylase

Na+-transporting oxaloacetate decarboxylase beta subunit
Na+-transporting oxaloacetate decarboxylase beta subunit
Identifiers
Symbol	OAD_beta
Pfam	PF03977
Pfam clan	CL0064
InterPro	IPR005661
TCDB	3.B.1
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

oxaloacetate decarboxylase
oxaloacetate decarboxylase
Identifiers
EC no.	4.1.1.3
CAS no.	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 / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Oxaloacetate decarboxylase, gamma chain

Identifiers

Symbol

OAD_gamma

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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]

References

^ 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.
^ ^a ^b 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.
^ 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.

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

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v t e Carbon–carbon lyases (EC 4.1)
4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Arginine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase
4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase
4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase
4.1.99: Other	Tryptophanase Photolyase CPD lyase Spore photoproduct lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)