EC 2.1.2.10 - Aminomethyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.2.10

Names

Accepted name:
aminomethyltransferase
Other names:
S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming)
T-protein
glycine synthase
tetrahydrofolate aminomethyltransferase
glycine-cleavage system T-protein
[protein]-8-S-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
Systematic name:
[protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)

Reaction

Comments:

A component, with EC 1.4.4.2, glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, 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 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 [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004047
CAS Registry Number: 37257-08-2
UniProtKB/Swiss-Prot: (334) [show] [UniProt]

References

  1. Okamura-Ikeda, J., Fujiwara, K. and Motokawa, Y.
    Purification and characterization of chicken liver T protein, a component of the glycine cleavage system.
    J. Biol. Chem. 257: 135-139 (1982). [PMID: 7053363]
  2. Perham, R.N.
    Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
    Annu. Rev. Biochem. 69: 961-1004 (2000). [PMID: 10966480]
  3. Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J.
    Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase.
    Protein Expr. Purif. 39: 269-282 (2005). [PMID: 15642479]

[EC 2.1.2.10 created 1972, modified 2003, modified 2006]