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Escherichia coli K-12 substr. MG1655 Reaction: 2.3.1.29


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 2.3.1.29

Enzymes and Genes:
2-amino-3-ketobutyrate CoA ligaseInferred from experiment: kbl

In Pathway: L-threonine degradation II

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

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 synthetase, KBL, AKB ligase

Summary:
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 1.1.1.103, 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].

Citations: [Mukherjee87, McGilvray69]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.3.1.29, ENZYME:EC:2.3.1.29, IUBMB-ExplorEnz:EC:2.3.1.29


References

Edgar00: Edgar AJ, Polak JM (2000). "Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs." Eur J Biochem 267(6);1805-12. PMID: 10712613

McGilvray69: McGilvray D, Morris JG (1969). "Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase"." Biochem J 112(5);657-71. PMID: 5821726

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue Jan 1, 2002, biocyc12.