Phosphoribosylamine—glycine ligase

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phosphoribosylamine-glycine ligase
Identifiers
EC number 6.3.4.13
CAS number 9032-01-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Phosphoribosylglycinamide synthetase, N domain
PDB 1gso EBI.jpg
glycinamide ribonucleotide synthetase (gar-syn) from e. coli.
Identifiers
Symbol GARS_N
Pfam PF02844
InterPro IPR020562
PROSITE PDOC00164
SCOP 1gso
SUPERFAMILY 1gso
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain
PDB 1gso EBI.jpg
glycinamide ribonucleotide synthetase (gar-syn) from e. coli.
Identifiers
Symbol GARS_A
Pfam PF01071
Pfam clan CL0179
InterPro IPR020561
PROSITE PDOC00164
SCOP 1gso
SUPERFAMILY 1gso
Phosphoribosylglycinamide synthetase, C domain
PDB 1vkz EBI.jpg
crystal structure of phosphoribosylamine--glycine ligase (tm1250) from thermotoga maritima at 2.30 a resolution
Identifiers
Symbol GARS_C
Pfam PF02843
InterPro IPR020560
PROSITE PDOC00164
SCOP 1gso
SUPERFAMILY 1gso

In enzymology, a phosphoribosylamine-glycine ligase (EC 6.3.4.13) is an enzyme that catalyzes the chemical reaction

ATP + 5-phospho-D-ribosylamine + glycine \rightleftharpoons ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide

The 3 substrates of this enzyme are ATP, 5-phospho-D-ribosylamine, and glycine, whereas its 3 products are ADP, phosphate, and N1-(5-phospho-D-ribosyl)glycinamide.

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme participates in purine metabolism.

Bacterial genes that encode this enzyme are often named purD. The purD genes often contain PurD RNA motif in their 5' UTR.[1]

In bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). In yeast, GARS is part of a bifunctional enzyme (encoded by the ADE5/7 gene) in conjunction with phosphoribosylformylglycinamidine cyclo-ligase (AIRS). In higher eukaryotes, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART.

Nomenclature[edit]

The systematic name of this enzyme class is 5-phospho-D-ribosylamine:glycine ligase (ADP-forming). Other names in common use include:

  • phosphoribosylglycinamide synthetase,
  • glycinamide ribonucleotide synthetase,
  • phosphoribosylglycineamide synthetase,
  • glycineamide ribonucleotide synthetase,
  • 2-amino-N-ribosylacetamide 5'-phosphate kinosynthase,
  • 5'-phosphoribosylglycinamide synthetase, and
  • GAR synthetase.

Structural studies[edit]

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1GSO, 1VKZ, and 2QK4.

References[edit]

  1. ^ Weinberg Z, Barrick JE, Yao Z, et al. (2007). "Identification of 22 candidate structured RNAs in bacteria using the CMfinder comparative genomics pipeline". Nucleic Acids Res. 35 (14): 4809–19. doi:10.1093/nar/gkm487. PMC 1950547. PMID 17621584. 

Further reading[edit]

  • GOLDTHWAIT DA, GREENBERG GR, PEABODY RA (1956). "On the mechanism of synthesis of glycinamide ribotide and its formyl derivative". J. Biol. Chem. 221 (2): 569–77. PMID 13357451. 
  • HARTMAN SC, BUCHANAN JM (1958). "Biosynthesis of the purines. XXII 2-Amino-N-ribosylacetamide-5'-phosphate kinosynthase". J. Biol. Chem. 233 (2): 456–61. PMID 13563520. 

This article incorporates text from the public domain Pfam and InterPro IPR020560

This article incorporates text from the public domain Pfam and InterPro IPR020562

This article incorporates text from the public domain Pfam and InterPro IPR020561