Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.4.13 - phosphoribosylamine-glycine ligase and Organism(s) Escherichia coli and UniProt Accession P15640

for references in articles please use BRENDA:EC6.3.4.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.13 phosphoribosylamine-glycine ligase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P15640 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
  • 6.3.4.13
  • transformylase
  • aminoimidazole
  • formyltransferase
  • amidotransferase
  • phosphoribosylaminoimidazole
  • phosphoribosylpyrophosphate
  • medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-Amino-N-ribosylacetamide 5'-phosphate kinosynthase
-
-
-
-
5'-Phosphoribosylglycinamide synthetase
-
-
-
-
GAR synthetase
-
-
-
-
GAR-syn
-
-
GARS
-
-
-
-
GARSase
-
-
-
-
Glycinamide ribonucleotide synthetase
-
-
-
-
Glycineamide ribonucleotide synthetase
-
-
-
-
Phosphoribosylglycinamide synthetase
-
-
-
-
Phosphoribosylglycineamide synthetase
-
-
-
-
PRG synthetase
-
-
-
-
Synthetase, phosphoribosylglycinamide
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-phospho-D-ribosylamine:glycine ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-01-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 5-phospho-D-ribosylamine + Gly
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
-
-
-
?
ATP + 5-phospho-D-ribosylamine + glycine
ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
-
ATP in form of MgATP2-
-
-
?
ATP + 5-phosphoribosylamine + Gly
?
show the reaction diagram
-
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
-
-
?
ATP + 5-phosphoribosylamine + Gly
ADP + phosphate + 5-phosphoribosylglycinamide
show the reaction diagram
ATP + carbocyclic 5-phosphoribosylamine + Gly
ADP + phosphate + carbocyclic glycinamide ribonucleotide
show the reaction diagram
-
r
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 5-phosphoribosylamine + Gly
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
5'-phosphoribosylamine
-
-
0.17
ATP
-
-
0.27
Gly
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19
methionine-substituted enzyme
2.3
selenomethionine-substituted enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18
no detectable activity at this temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48240
calculated from amino acid sequence
49000
gel filtration
45945
-
x * 45945, calculation from nucleotide sequence
47000
-
x * 47000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
selenomethionine incorporated enzyme, hanging drop vapor diffusion method
selenomethionine incorporated enzyme, hanging drop vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P294L
loss of function
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as the selenomethionine incorporated protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Liu, D.S.; Caperelli, C.A.
Carbocyclic substrates for de novo purine biosynthesis
J. Biol. Chem.
266
16699-16702
1991
Escherichia coli, eukaryota
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team