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2.3.1.29 |
Description |
Glycine C-acetyltransferase |
Alternative names |
2-amino-3-ketobutyrate coenzyme A ligase. |
Catalyzed reaction |
Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate. |
Cofactor |
Pyridoxal-phosphate. |
Prosite |
PROSITE; PDOC00518; |
PDB |
1FC4; |
Organisms |
-Eubacteria -Metazoa -Human |
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Family |
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Links |
Enzyme (activities) 2.3.1.29
BRENDA (activities) 2.3.1.29
KEGG (pathways) 2.3.1.29
PLPMDB (PLP mutants) 2.3.1.29
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References |
Schmidt, A.; Sivaraman, J.; Li, Y.; Larocque, R.; Barbosa, J.A.; Smith, C.; Matte, A.; Schrag, J.D.; Cygler, M. (2001) Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism Biochemistry 40 5151-60. Edgar, A. J.; Polak, J. M. (2000) Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs Eur J Biochem 267 1805-12. Tong, H.; Davis, L. (1994) 2-Amino-3-ketobutyrate-CoA ligase from beef liver mitochondria. Purification and partial sequence J Biol Chem 269 4057-64. Aronson, B.D.; Ravnikar, P.D.; Somerville, R.L. (1988) Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli Nucleic Acids Res 16 3586-7. Articles on 2.3.1.29 |
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last changed |
2017/10/10 14:12 |
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