glycine C-acetyltransferase [Escherichia coli str. K-12 substr. MG1655 - Protein

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Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes. [Chem Commun (Camb). 2006]
Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes.
Bashir Q, Rashid N, Akhtar M. Chem Commun (Camb). 2006 Dec 28; (48):5065-7. Epub 2006 Oct 13.
Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. [Biochemistry. 2001]
Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, Cygler M. Biochemistry. 2001 May 1; 40(17):5151-60.
2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme. [Biochim Biophys Acta. 1990]
2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme.
Mukherjee JJ, Dekker EE. Biochim Biophys Acta. 1990 Jan 19; 1037(1):24-9.

RefSeq protein
See the reference protein sequence for 2-amino-3-ketobutyrate CoA ligase (NP_418074.1).

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