Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 2.3.1.29

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.3.1.29

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

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

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: ?

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 SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, biocyc13.