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MetaCyc Reaction: 1.4.4.2

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

EC Number: 1.4.4.2

Enzymes and Genes:

Arabidopsis thaliana col: glycine decarboxylase: AT2G35120
glycine decarboxylase: AT2G35370
Escherichia coli K-12 substr. MG1655: glycine decarboxylaseInferred from experiment: gcvP
Gallus gallus: glycine decarboxylaseInferred from experiment: GLDC
Homo sapiens: glycine decarboxylaseInferred from experiment: GLDC

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

In Pathway: glycine cleavage, glycine biosynthesis II

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.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: glycine dehydrogenase (aminomethyl-transferring)

Enzyme Commission Synonyms: P-protein, glycine decarboxylase, glycine-cleavage complex, glycine:lipoylprotein oxidoreductase (decarboxylating and acceptor-aminomethylating), protein P1, glycine dehydrogenase (decarboxylating), glycine cleavage system P-protein, glycine-cleavage complex P-protein

Standard Gibbs Free Energy (ΔrG in kcal/mol): -56.676727Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein ( EC 1.4.4.2), the T protein ( EC 2.1.2.10), the L protein ( EC 1.8.1.4) and the lipoyl-bearing H protein [Nesbitt05]. Previously known as glycine synthase.

Citations: [Hiraga80a, Perham00]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R03425

Relationship Links: BRENDA:EC:1.4.4.2, ENZYME:EC:1.4.4.2, IUBMB-ExplorEnz:EC:1.4.4.2, UniProt:RELATED-TO:O22575, UniProt:RELATED-TO:O32915, UniProt:RELATED-TO:O80988, UniProt:RELATED-TO:P23378, UniProt:RELATED-TO:P26969, UniProt:RELATED-TO:P33195, UniProt:RELATED-TO:Q94B78, UniProt:RELATED-TO:Q9JT86, UniProt:RELATED-TO:Q9UXT0, UniProt:RELATED-TO:Q9UXT1

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


References

Hiraga80a: Hiraga K, Kikuchi G (1980). "The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein." J Biol Chem 255(24);11671-6. PMID: 7440563

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

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 Sat Apr 30, 2016, biocyc11.