Phosphoribosylaminoimidazolecarboxamide formyltransferase

From Wikipedia, the free encyclopedia
phosphoribosylaminoimidazolecarboxamide formyltransferase
Identifiers
EC no.2.1.2.3
CAS no.9032-03-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3), also known by the shorter name AICAR transformylase, is an enzyme that catalyzes the chemical reaction

10-formyltetrahydrofolate + AICAR tetrahydrofolate + FAICAR

Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and AICAR, whereas its two products are tetrahydrofolate and FAICAR.

This enzyme participates in purine metabolism and one carbon pool by folate.

Nomenclature[]

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazole-carb oxamide N-formyltransferase. Other names in common use include:

  • 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
  • 5-amino-1-ribosyl-4-imidazolecarboxamide 5-phosphate,
  • 5-amino-4-imidazolecarboxamide ribonucleotide transformylase,
  • 5-amino-4-imidazolecarboxamide ribotide transformylase,
  • 5-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase,
  • AICAR formyltransferase,
  • AICAR transformylase,
  • aminoimidazolecarboxamide ribonucleotide transformylase, and
  • transformylase,
  • bifunctional purine biosynthesis protein PURH,
  • ATIC.

Structural studies[]

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1G8M, 1M9N, 1OZ0, 1P4R, 1PKX, 1PL0, 1THZ, 2B1G, 2B1I, 2IU0, and 2IU3.

References[]

  • HARTMAN SC, BUCHANAN JM (1959). "Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reactions". J. Biol. Chem. 234 (7): 1812–6. PMID 13672969.


Retrieved from ""