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Information on EC 6.3.4.13 - phosphoribosylamine-glycine ligase and Organism(s) Gallus gallus
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6.3.4.13 phosphoribosylamine-glycine ligaseSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Gallus gallus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glycinamide ribonucleotide synthetase, gar synthetase, gar-syn, phosphoribosylglycinamide synthetase, phosphoribosylamine-glycine ligase, glycinamide ribotide synthetase, phosphoribosylglycineamide synthetase, 5'-phosphoribosylglycinamide synthetase, prg synthetase, trifunctional purine biosynthetic protein adenosine-3, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-Amino-N-ribosylacetamide 5'-phosphate kinosynthase
-
-
-
-
5'-Phosphoribosylglycinamide synthetase
-
-
-
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GAR synthetase
-
-
-
-
GARS
-
-
-
-
GARSase
-
-
-
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Glycinamide ribonucleotide synthetase
-
-
-
-
Glycineamide ribonucleotide synthetase
-
-
-
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Phosphoribosylglycinamide synthetase
-
-
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Phosphoribosylglycineamide synthetase
-
-
-
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PRG synthetase
-
-
-
-
Synthetase, phosphoribosylglycinamide
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-
-
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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
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-phospho-D-ribosylamine:glycine ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9032-01-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
-
ADP in form of MgADP-
-
-
r
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
ATP + carbocyclic 5-phosphoribosylamine + Gly
ADP + phosphate + carbocyclic glycinamide ribonucleotide
-
r
-
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
-
-
-
?
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
-
-
-
?
ATP + 5-phosphoribosylamine + Gly
?
-
enzyme of purine biosynthetic pathway
-
-
?
ATP + 5-phosphoribosylamine + Gly
?
-
enzyme of the de novo purine biosynthetic pathway
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
-
r
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
second step in de novo purine biosynthesis pathway
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
second step in de novo purine biosynthesis pathway
-
?
ATP + 5-phosphoribosylamine + Gly
?
-
enzyme of purine biosynthetic pathway
-
-
?
ATP + 5-phosphoribosylamine + Gly
?
-
enzyme of the de novo purine biosynthetic pathway
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trifunctional enzyme with phosphoribosylamine-glycine ligase activity, glycinamide ribonucleotide transformylase activity, and aminoimidazole ribonucleotide synthetase activity
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PUR2_CHICK
1003
0
106544
Swiss-Prot
other Location (Reliability: 4)
C5J075_CHICK
368
0
39072
TrEMBL
other Location (Reliability: 4)
A0A1D5NU16_CHICK
863
0
93387
TrEMBL
Mitochondrion (Reliability: 5)
A0A3Q2U3P5_CHICK
433
0
45990
TrEMBL
other Location (Reliability: 4)
A0A547_CHICK
1003
0
106529
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MW 49000, GAR domain of the trifunctional enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
GAR domain of the multifunctional enzyme has a MW of 49000, SDS-PAGE, the multifunctional enzyme has a MW of 110000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
on repeated freeze-thawing activity is lost due to the precipitation of protein
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of phosphoribosylamine-glycine ligase and glycinamide ribonucleotide transformylase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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, Drosophila melanogaster, Escherichia coli, Schizosaccharomyces pombe
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
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
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
Synechocystis sp., Arabidopsis thaliana, Archaeoglobus fulgidus, Bacillus subtilis, Saccharomyces cerevisiae, Yarrowia lipolytica, Gallus gallus, Drosophila melanogaster, Drosophila pseudoobscura, Escherichia coli, Haemophilus influenzae, Homo sapiens, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Mus musculus, Pyrococcus horikoshii, Salmonella enterica subsp. enterica serovar Typhimurium, Schizosaccharomyces pombe, Chironomus tentans, Pyrococcus horikoshii OT-3
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