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MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

Arabidopsis thaliana col: glycine decarboxylase: AT2G35120
glycine decarboxylase: AT2G35370
Escherichia coli K-12 substr. MG1655: aminomethyltransferaseInferred from experiment: gcvT
Gallus gallus: aminomethyltransferaseInferred from experiment: AMT
Homo sapiens: aminomethyltransferaseTraceable author statement to experimental support: AMT

Sub-reaction of:
glycine + a tetrahydrofolate + NAD+ ↔ a 5,10-methylene-tetrahydrofolate + ammonium + CO2 + NADH

In Pathway: glycine cleavage

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: aminomethyltransferase

Enzyme Commission Synonyms: S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming), T-protein, glycine synthase, tetrahydrofolate aminomethyltransferase, [protein]-8-S-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)

Standard Gibbs Free Energy (ΔrG in kcal/mol): 37.564484Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A component, with EC, glycine dehydrogenase (decarboxylating) and EC, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase. The glycine cleavage system is composed of four components that only loosely associate: the P protein ( EC, the T protein ( EC, the L protein ( EC and the lipoyl-bearing H protein [Nesbitt05].

Citations: [OkamuraIkeda82, Perham00]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R04125, Rhea:16945

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O32955, UniProt:RELATED-TO:O49954, UniProt:RELATED-TO:P25285, UniProt:RELATED-TO:P27248, UniProt:RELATED-TO:P28337, UniProt:RELATED-TO:P48728, UniProt:RELATED-TO:P49095, UniProt:RELATED-TO:P49361, UniProt:RELATED-TO:P49362, UniProt:RELATED-TO:P49363, UniProt:RELATED-TO:P49364, UniProt:RELATED-TO:P54260, UniProt:RELATED-TO:P93256, UniProt:RELATED-TO:Q9JVP2, UniProt:RELATED-TO:Q9UZP8

Revised 18-Sep-2012 by Caspi R, SRI International


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Nesbitt05: Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF, Broadwater JA, Haas JA, Fox BG, Booker SJ (2005). "Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase." Protein Expr Purif 39(2);269-82. PMID: 15642479

OkamuraIkeda82: Okamura-Ikeda K, Fujiwara K, Motokawa Y (1982). "Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system." J Biol Chem 257(1);135-9. PMID: 7053363

Perham00: Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions." Annu Rev Biochem 69;961-1004. PMID: 10966480

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Thu Apr 28, 2016, biocyc14.