Pyruvate oxidase

In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction

pyruvate + phosphate + O2 acetyl phosphate + CO2 + H2O2
pyruvate oxidase
Identifiers
EC number1.2.3.3
CAS number9001-96-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use include pyruvic oxidase, and phosphate-dependent pyruvate oxidase. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1POW, 1POX, 1V5E, 1V5F, 1V5G, 1Y9D, 2DJI, 2EZ4, 2EZ8, 2EZ9, 2EZT, and 2EZU.

gollark: And yours seems to be doing some bizarre thing where it's hardcoding a table of the different things it should print for each modulus.
gollark: You can include "fizzbuzz" and stuff inline in the python version, but not in the assembly version.
gollark: No, I mean your code also relies on the data bits.
gollark: Er, that's a bad comparison.
gollark: I'm not sure exactly, since I'm not sure what precisely your code is doing and it is hardly an apples-to-apples comparison.

References
    • Williams FR, Hager LP (1966). "Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein". Arch. Biochem. Biophys. 116 (1): 168–76. doi:10.1016/0003-9861(66)90025-7. PMID 5336022.
    • Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G (2005). "Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair". Biochemistry. 44 (40): 13291–303. doi:10.1021/bi051058z. PMID 16201755.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.