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Literature summary for 2.3.1.29 extracted from

  • Tong, H.; Davis, L.
    2-Amino-3-ketobutyrate-CoA ligase from beef liver mitochondria: An NMR spectroscopic study of low-barrier hydrogen bonds of a pyridoxal 5'-phosphate-dependent enzyme (1995), Biochemistry, 34, 3362-3367.
    View publication on PubMed
Search for more literature for 2.3.1.29

Inhibitors

Inhibitors Comment Organism Structure
L-cysteine enzyme reacts reversibly with L-cysteine Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Bos taurus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
-
 Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + glycine Bos taurus involved in L-threonine catabolism, inducible CoA + 2-amino-3-oxobutanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + glycine
-
 Bos taurus CoA + 2-amino-3-oxobutanoate
-
 ?
acetyl-CoA + glycine involved in L-threonine catabolism, inducible Bos taurus CoA + 2-amino-3-oxobutanoate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 43000, SDS-PAGE Bos taurus

pH Range

pH Minimum pH Maximum Comment Organism
5.1 9.4 absorbtion spectrum does not change significantly Bos taurus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate pyridoxal 5'-phosphate is covalently bound to an active site lysine, formation of a Schiff base Bos taurus
pyridoxal 5'-phosphate requirement, stoichiometry: 1 mol per mol subunit Bos taurus