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Information on EC 6.3.4.13 - phosphoribosylamine-glycine ligase
for references in articles please use BRENDA:EC6.3.4.13
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.4 Other carbon-nitrogen ligases
6.3.4.13 phosphoribosylamine-glycine ligase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
glycinamide ribonucleotide synthetase, gar synthetase, gar-syn, phosphoribosylglycinamide synthetase, phosphoribosylamine-glycine ligase, glycinamide ribotide synthetase, phosphoribosylglycineamide synthetase, garsase, pur2,5, phosphoribosyl-glycinamide synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-Amino-N-ribosylacetamide 5'-phosphate kinosynthase
-
-
-
-
5'-Phosphoribosylglycinamide synthetase
-
-
-
-
ade5
EC 6.3.1.3
-
-
formerly
-
GAR synthetase
-
-
-
-
GARS
GARSase
-
-
-
-
Glycinamide ribonucleotide synthetase
-
-
-
-
Glycineamide ribonucleotide synthetase
-
-
-
-
Phosphoribosylglycinamide synthetase
Phosphoribosylglycineamide synthetase
-
-
-
-
PRG synthetase
-
-
-
-
Synthetase, phosphoribosylglycinamide
-
-
-
-
GARS
-
-
-
-
Phosphoribosylglycinamide synthetase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
-
-
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
mechanism
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
5-aminoimidazole ribonucleotide biosynthesis I, 5-aminoimidazole ribonucleotide biosynthesis II, superpathway of 5-aminoimidazole ribonucleotide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
5-phospho-D-ribosylamine:glycine ligase (ADP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9032-01-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
ATP + 5-phospho-D-ribosylamine + glycine
-
Substrates: ADP in form of MgADP-
Products: -
Products: -
r
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
ATP + 5-phospho-D-ribosylamine + glycine
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
ATP + carbocyclic 5-phosphoribosylamine + Gly
ADP + phosphate + carbocyclic glycinamide ribonucleotide
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: labile product
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + glycine
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
Substrates: ATP in form of MgATP2-
Products: -
Products: -
?
ATP + 5-phospho-D-ribosylamine + glycine
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: sequential ordered mechanism of substrate binding and product release in which 5-phosphoribosylamine binds first followed by MgATP2- and then Gly. Phosphate leaves first followed by loss of MgADP- and finally phosphoribosylglycinamide
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of the de novo purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: second step in de novo path of purine biosynthesis
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: second step in de novo path of purine biosynthesis
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of the de novo purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of the de novo purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: r
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: r
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
Pigeon
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
Substrates: -
Products: -
Products: -
?
ATP + carbocyclic 5-phosphoribosylamine + Gly
ADP + phosphate + carbocyclic glycinamide ribonucleotide
-
Substrates: r
Products: -
Products: -
?
ATP + carbocyclic 5-phosphoribosylamine + Gly
ADP + phosphate + carbocyclic glycinamide ribonucleotide
-
Substrates: r
Products: -
Products: -
?
ATP + carbocyclic 5-phosphoribosylamine + Gly
ADP + phosphate + carbocyclic glycinamide ribonucleotide
-
Substrates: r
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is trifunctional exhibiting phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, and phosphoribosylaminoimidazole synthetase activities, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: requirement for ATP and a substrate with a carboxyl group or its relatives, transfer of a phosphate group from ATP to the carboxyl group or its relatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 5-phospho-D-ribosylamine + glycine
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
Substrates: -
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: sequential ordered mechanism of substrate binding and product release in which 5-phosphoribosylamine binds first followed by MgATP2- and then Gly. Phosphate leaves first followed by loss of MgADP- and finally phosphoribosylglycinamide
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of the de novo purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: second step in de novo path of purine biosynthesis
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: second step in de novo path of purine biosynthesis
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of the de novo purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: enzyme of the de novo purine biosynthetic pathway
Products: -
Products: -
?
ATP + 5-phosphoribosylamine + Gly
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is trifunctional exhibiting phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, and phosphoribosylaminoimidazole synthetase activities, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: second step in de novo purine biosynthesis pathway
Products: -
Products: -
?
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Glycinamide ribonucleotide synthetase activity in lymphocytes from patients with Alzheimer's disease and normal controls.
Down Syndrome
Variation of glycinamide ribonucleotide synthetase levels during in vitro aging of human fibroblasts: implications for gene dosage studies.
Lymphoma
Mammalian glycinamide ribonucleotide transformylase. Kinetic mechanism and associated de novo purine biosynthetic activities.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trifunctional enzyme with phosphoribosylamine-glycine ligase activity, glycinamide ribonucleotide transformylase activity, and aminoimidazole ribonucleotide synthetase activity
-
-
brenda
anamorph, Fusarium graminearum. Auxotrophic strains, designated S4B1279 and S4B3008, discovered from a collection of insertional mutants generated by restriction enzyme-mediated integration
-
-
brenda
trifunctional enzyme with phosphoribosylamine-glycine ligase activity, glycinamide ribonucleotide transformylase activity, and aminoimidazole ribonucleotide synthetase activity
-
-
brenda
enzyme displays phosphoribosylamine-glycine ligase activity, phosphoribosylformylglycinamidine cyclo-ligase activity and phosphoribosylglycinamide formyltransferase activity, cf. EC 2.1.2.2
Uniprot
brenda
trifunctional enzyme with phosphoribosylamine-glycine ligase activity, glycinamide ribonucleotide transformylase activity, and aminoimidazole ribonucleotide synthetase activity
-
-
brenda
trifunctional protein, catalyzes reactions of phosphoribosylglycinamide formyltransferase (EC 2.1.2.2), phosphoribosylglycinamide synthetase (EC 6.3.4.13), phosphoribosylaminoimidazole synthetase (EC 6.3.3.1)
Uniprot
brenda
trifunctional enzyme with phosphoribosylamine-glycine ligase activity, glycinamide ribonucleotide transformylase activity, and aminoimidazole ribonucleotide synthetase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
gart and paics mutants have pigmentation defects and microphthalmia
metabolism
physiological function
metabolism
-
the trifunctional enzyme catalyzes steps 2, 3, and 5 of inosine monophosphate synthesis, followed by paics encoded phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase, a bifunctional enzyme that catalyzes steps 6 and 7 of this process. Crucial requirement for maternally derived gart and paics. De novo purine synthesis pathway, overview
metabolism
Pur2,5 encodes a bifunctional enzyme that catalyzes the second and the fifth steps of de novo purine biosynthesis pathway andshows dual enzymatic activity - of glycinamide ribotide synthetase and of aminoim-idazole ribotide synthetase
metabolism
the phosphorylation of glycine by ATP in PurD requires an activation energy of 26.1 kcal/mol, and the total change in the free-energy reaches -17.0 kcal/mol at the end of the reaction. The partial atomic charges of the substrate molecules are redistributed to delocalize within two sites of glycylphosphate and Mg-ADP moieties at the end of the reaction
physiological function
-
gart and paics function are required for eye growth. IMP feeds into an ATP pathway required for retinoblast proliferation and a GTP pathway required for pigmentation
physiological function
deficiency in the de novo purine synthesis in a GART null mutant cell line affects the cellular transcriptome, significantly altering the expression of over 4000 genes. CD36 shows remarkable changes in transcript levels and protein expression in the mutant
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
trifunctional enzyme with act phosphoribosylamine-glycine ligase activity, glycinamide ribonucleotide transformylase activity, and aminoimidazole ribonucleotide synthetase activity
112000
-
x * 112000, enzyme protein with glycinamide phosphoribosylamine-glycine ligase and aminoimidazole ribonucleotide synthetase activity, SDS-PAGE
45000
55500
-
sucrose density gradient centrifugation
additional information
-
MW 49000, GAR domain of the trifunctional enzyme, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
GAR domain of the multifunctional enzyme has a MW of 49000, SDS-PAGE, the multifunctional enzyme has a MW of 110000, SDS-PAGE
?
-
x * 112000, enzyme protein with glycinamide phosphoribosylamine-glycine ligase and aminoimidazole ribonucleotide synthetase activity, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme and in complex with ATP, to 2.4 and 1.8 A resolution, respectively. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syns and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP
selenomethionine incorporated enzyme, hanging drop vapor diffusion method
native enzyme and in complex with phosphate, with AMP and phosphate, and with AMP and glycine, to 2.21, 2.20, 1.9 and 2.21 A resolution, respectively. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syn's and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP
selenomethionine derivative, to 2.8 A resolution. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syns and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP
selenomethionine incorporated enzyme, hanging drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
zygotic gart and paic mutants have pigmentation defects in which xanthophore and iridophore pigmentation is almost completely absent, and melanin-derived pigmentation is significantly decreased, even though pigment cells are present in normal amounts and distributions. Zygotic gart and paics mutants are also microphthalmic, resulting from defects in cell cycle exit of proliferative retinoblasts within the developing eye, severe phenotypes, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
on repeated freeze-thawing activity is lost due to the precipitation of protein
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, slight loss of activity after 3 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of phosphoribosylamine-glycine ligase and aminoimidazole ribonucleotide synthetase
-
copurification of phosphoribosylamine-glycine ligase and glycinamide ribonucleotide transformylase
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
12-gene cluster encoding nine enzymes for de novo purine nucleotide synthesis
-
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
high GART expression is observed in glioma and is related to the grade of malignancy. GART overexpression is significantly associated with overall survival. Transfecting cells with GART-siRNA suppresses proliferation and enhances temozolomide-induced apoptosis in glioma cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ebbole, D.J.; Zalkin, H.
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis
J. Biol. Chem.
262
8274-8287
1987
Bacillus subtilis
brenda
Schrimsher, J.L.; Schendel, F.J.; Stubbe, J.
Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase
Biochemistry
25
4356-4365
1986
Gallus gallus
brenda
Daubner, S.C.; Young, M.; Sammons, R.D.; Courtney, L.F.; Benkovic, S.J.
Structural and mechanistic studies on the HeLa and chicken liver proteins that catalyze glycinamide ribonucleotide synthesis and formylation and aminoimidazole ribonucleotide synthesis
Biochemistry
25
2951-2957
1986
Gallus gallus, Homo sapiens
brenda
Daubner, S.C.; Schrimsher, J.L.; Schendel, F.J.; Young, M.; Henikoff, S.; Patterson, D.; Stubbe, J.; Benkovic, S.J.
A multifunctional protein possessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotide transformylase, and aminoimidazole ribonucleotide synthetase activities in de novo purine biosynthesis
Biochemistry
24
7059-7062
1985
Gallus gallus
brenda
Gandhi, N.R.; Westby, C.A.
The synthesis of 5'-phosphoribosylglycinamide in Salmonella typhimurium
Enzymologia
42
185-200
1972
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Rowe, P.B.; McCairns, E.; Madsen, G.; Sauer, D.; Elliott, H.
De novo purine synthesis in avian liver. Co-purification of the enzymes and properties of the pathway
J. Biol. Chem.
253
7711-7721
1978
Pigeon
brenda
Nierlich, D.P.
Phosphoribosylglycinamide synthetase from Aerobacter aerogenes
Methods Enzymol.
51
179-185
1978
Klebsiella aerogenes
brenda
Cheng, Y.S.; Murray, M.; Schendel, F.; Otvos, J.; Wehrli, S.; Stubbe, J.
Chemical characterization of phosphoribosylamine, a substrate for newly discovered trifunctional protein containing glycinamide ribonucleotide synthetase activity
Adv. Enzyme Regul.
26
319-333
1987
Gallus gallus, Escherichia coli, Schizosaccharomyces pombe, Drosophila melanogaster
brenda
Wheeler, P.R.
Enzymes for purine synthesis and scavening in pathogenic Mycobacterium leprae
J. Gen. Microbiol.
133
3013-3018
1987
Mycobacterium tuberculosis variant microti, Mycobacterium avium
brenda
Gnirke, A.; Barnes, T.S.; Patterson, D.; Schild, D.; Featherstone, T.; Olson, M.V.
Cloning and in vivo expression of the human GART gene using yeast artificial chromosomes
EMBO J.
10
1629-1634
1991
Homo sapiens
brenda
Antle, V.D.; Liu, D.; McKellar, B.R.; Caperelli, C.A.; Hua, M.; Vince, R.
Substrate specificity of glycinamide ribonucleotide synthetase from chicken liver
J. Biol. Chem.
271
8192-8195
1996
Gallus gallus
brenda
Caperelli, C.A.; Liu, D.
Carbocyclic substrates for de novo purine biosynthesis. Enantiospecific synthesis and enantiospecificity of enzymatic utilization
J. Biol. Chem.
267
9783-9787
1992
Gallus gallus
brenda
Shen, Y.; Rudolph, J.M.; Stern, J.R.; Stubbe, J.
Glycinamide ribonucleotide synthetase from Escherichia coli: cloning, overproduction, sequencing, isolation, and characterization
Biochemistry
29
218-227
1990
Escherichia coli
brenda
Poch, M.T.; Qin, W.; Caperelli, C.A.
The human trifunctional enzyme of de novo purine biosynthesis: heterologous expression, purification, and preliminary characterization
Protein Expr. Purif.
12
17-24
1998
Homo sapiens
brenda
Schnorr, K.M.; Laloue, M.; Hirel, B.
Isolation of cDNAs encoding two purine biosynthetic enzymes of soybean and expression of the corresponding transcripts in roots and root nodules
Plant Mol. Biol.
32
751-757
1996
Glycine max
brenda
Kan, J.L.; Jannatipour, M.; Taylor, S.M.; Moran, R.G.
Mouse cDNAs encoding a trifunctional protein of de novo purine biosynthesis and a related single-domain glycinamide ribonucleotide synthetase
Gene
137
195-202
1993
Mus musculus
brenda
Liu, D.S.; Caperelli, C.A.
Carbocyclic substrates for de novo purine biosynthesis
J. Biol. Chem.
266
16699-16702
1991
Escherichia coli, eukaryota
brenda
Henikoff, S.
The Saccharomyces cerevisiae ADE5,7 protein is homologous to overlapping Drosophila melanogaster Gart polypeptides
J. Mol. Biol.
190
519-528
1986
Saccharomyces cerevisiae
brenda
Bera, A.K.; Chen, S.; Smith, J.L.; Zalkin, H.
Temperature-dependent function of the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel and coupling with glycinamide ribonucleotide synthetase in a hyperthermophile
J. Bacteriol.
182
3734-3739
2000
Aquifex aeolicus
brenda
Weaver, T.M.; Wang, W.; Ealick, S.E.
Purification, crystallization and preliminary X-ray diffraction data from selenomethionine glycinamide ribonucleotide synthetase
Acta Crystallogr. Sect. D
55
518-521
1999
Escherichia coli
-
brenda
Wang, W.; Kappock, T.J.; Stubbe, J.; Ealick, S.E.
X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli
Biochemistry
37
15647-15662
1998
Escherichia coli (P15640), Escherichia coli
brenda
Kanai, S.; Toh, H.
Identification of new members of the GS ADP-forming family from the de novo purine biosynthesis pathway
J. Mol. Evol.
48
482-492
1999
Saccharomyces cerevisiae, Yarrowia lipolytica, Schizosaccharomyces pombe, Arabidopsis thaliana, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Haemophilus influenzae, Bacillus subtilis, Synechocystis sp., Methanocaldococcus jannaschii, Homo sapiens, Archaeoglobus fulgidus, Methanothermobacter thermautotrophicus, Pyrococcus horikoshii, Mus musculus, Gallus gallus, Drosophila melanogaster, Drosophila pseudoobscura, Chironomus tentans, Pyrococcus horikoshii OT-3
brenda
Kim, J.; Myong, K.; Shim, W.; Yun, S.; Lee, Y.
Functional characterization of acetylglutamate synthase and phosphoribosylamine-glycine ligase genes in Gibberella zeae
Curr. Genet.
51
99-108
2007
Fusarium graminearum
brenda
Ng, A.; Uribe, R.A.; Yieh, L.; Nuckels, R.; Gross, J.M.
Zebrafish mutations in gart and paics identify crucial roles for de novo purine synthesis in vertebrate pigmentation and ocular development
Development
136
2601-2611
2009
Danio rerio
brenda
Sampei, G.; Baba, S.; Kanagawa, M.; Yanai, H.; Ishii, T.; Kawai, H.; Fukai, Y.; Ebihara, A.; Nakagawa, N.; Kawai, G.
Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria
J. Biochem.
148
429-438
2010
Thermus thermophilus (Q5SK40), Thermus thermophilus, Geobacillus kaustophilus (Q5L3C7), Geobacillus kaustophilus, Aquifex aeolicus (O66949), Aquifex aeolicus
brenda
Stoyanov, A.; Petrova, P.; Lyutskanova, D.; Lahtchev, K.
Structural and functional analysis of PUR2,5 gene encoding bifunctional enzyme of de novo purine biosynthesis in Ogataea (Hansenula) polymorpha CBS 4732(T.)
Microbiol. Res.
169
378-387
2014
Ogataea angusta (G8EWC8)
brenda
Liu, X.; Ding, Z.; Liu, Y.; Zhang, J.; Liu, F.; Wang, X.; He, X.; Cui, G.; Wang, D.
Glycinamide ribonucleotide formyl transferase is frequently overexpressed in glioma and critically regulates the proliferation of glioma cells
Pathol. Res. Pract.
210
256-263
2014
Homo sapiens (P22102)
brenda
Yamamoto, N.; Sampei, G.; Kawai, G.
Free-energy profile analysis of the catalytic reaction of glycinamide ribonucleotide synthetase
Life (Basel)
12
281
2022
Aquifex aeolicus (O66949)
brenda
Mazzarino, R.; Baresova, V.; Zikanova, M.; Duval, N.; Wilkinson II, T.; Patterson, D.; Vacano, G.
Transcriptome and metabolome analysis of crGART, a novel cell model of de novo purine synthesis deficiency Alterations in CD36 expression and activity
PLoS ONE
16
e0247227
2021
Homo sapiens (P22102)
brenda
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