2-oxoisovalerate decarboxylation to isobutanoyl-CoA

Perham RN. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem. 2000;69():961–1004. doi: 10.1146/annurev.biochem.69.1.961. PMID: 10966480.; Wang GF, Kuriki T, Roy KL, Kaneda T. The primary structure of branched-chain alpha-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other alpha-oxo acid dehydrogenases. Eur J Biochem. 1993 May 01;213(3):1091–9. doi: 10.1111/j.1432-1033.1993.tb17858.x. PMID: 8504804.; MASSEY V, GIBSON QH, VEEGER C. Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase). Biochem J. 1960 Nov;77():341–51. PMID: 13767908; PMCID: PMC1204990.; SAVAGE N. Preparation and properties of highly purified diaphorase. Biochem J. 1957 Sep;67(1):146–55. PMID: 13471525; PMCID: PMC1200122.; Straub FB. Isolation and properties of a flavoprotein from heart muscle tissue. Biochem J. 1939 May;33(5):787–92. PMID: 16746974; PMCID: PMC1264446.

Metabolites

CO2

Formula: CO2 (43.98983)

CAS ID: 124-38-9

H+

Formula: H (1.0078246)

CAS ID: 12408-02-5

NAD(1-)

Formula: C21H26N7O14P2 (662.1012936000001)

CAS ID: 53-84-9



Enzyme

EC Number name full name note
1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating)
1.8.1.4 dihydrolipoyl dehydrogenase protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
2.3.1.168 dihydrolipoyllysine-residue (2-methylpropanoyl)transferase 2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase


Proteins

Protein ID name full name