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Phosphoribosylamine—glycine ligase

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, phosphoribosylamine-glycine ligase, also known as glycinamide ribonucleotide synthetase (GARS), (EC 6.3.4.13) is an enzyme that catalyzes the chemical reaction

which is the second step in purine biosynthesis. 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.

In bacteria, GARS is a monofunctional enzyme (encoded by the purD gene). The purD genes often contain PurD RNA motif in their 5' UTR. 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,including humans, GARS is part of a trifunctional enzyme in conjunction with AIRS and with phosphoribosylglycinamide formyltransferase (GART), forming GARS-AIRS-GART.


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Wikipedia

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