|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
In Pathway: threonine degradation II
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: glycine C-acetyltransferase
Enzyme Commission Synonyms: 2-amino-3-ketobutyrate CoA ligase, 2-amino-3-ketobutyrate coenzyme A ligase, 2-amino-3-ketobutyrate-CoA ligase, glycine acetyltransferase, aminoacetone synthase, aminoacetone synθse, KBL, AKB ligase
This reaction is part of the primary route of threonine utilization, and is also a highly efficient alternate pathway for glycine and serine biosynthesis.
Enzyme Commission Summary:
This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 184.108.40.206, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine [Edgar00]. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [Schmidt01].
Mukherjee87: Mukherjee JJ, Dekker EE (1987). "Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme." J Biol Chem 1987;262(30);14441-7. PMID: 3117785
Schmidt01: Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, 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(17);5151-60. PMID: 11318637
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