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Information on EC 2.4.2.14 - amidophosphoribosyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P00497
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2.4.2.14 amidophosphoribosyltransferaseSpecify your search results
Word Map
- 2.4.2.14
- purine
-
phosphoribosylamine
-
glutamine-dependent
- glycinamide
- 6-diazo-5-oxo-l-norleucine
-
14cglycine
-
pp-ribose-p
- acivicin
- phosphoribosyltransferases
- ribotide
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p-rib-pp
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
amidophosphoribosyltransferase, glutamine phosphoribosylpyrophosphate amidotransferase, phosphoribosyl pyrophosphate amidotransferase, amido phosphoribosyltransferase, phosphoribosylamidotransferase, 5-phosphoribosyl-1-pyrophosphate amidotransferase, gpatase, glutamine phosphoribosyl pyrophosphate amidotransferase, phosphoribosyl amidotransferase, gprat, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-phosphoribosylpyrophosphate amidotransferase
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-
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5-phosphoribosyl-1-pyrophosphate amidotransferase
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-
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5-phosphoribosylpyrophosphate amidotransferase
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-
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5-phosphororibosyl-1-pyrophosphate amidotransferase
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alpha-5-phosphoribosyl-1-pyrophosphate amidotransferase
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amidotransferase, phosphoribosyl pyrophosphate
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ATASE
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glutamine 5-phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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glutamine ribosylpyrophosphate 5-phosphate amidotransferase
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GPAT
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GPATase
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phosphoribose pyrophosphate amidotransferase
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-
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phosphoribosyl pyrophosphate amidotransferase
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-
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phosphoribosyldiphosphate 5-amidotransferase
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-
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phosphoribosylpyrophosphate glutamyl amidotransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
mechanism of glutamine amide transfer
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-phospho-beta-D-ribosylamine:diphosphate phospho-alpha-D-ribosyltransferase (glutamate-amidating)
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CAS REGISTRY NUMBER
COMMENTARY
9031-82-7
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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
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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reaction at 70% the rate of aminotransferase activity
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
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-
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
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no activity with NH4+
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?
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
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
additional information
Fe
-
low temperature magnetic circular dichroism, electron paramagnetic resonance and resonance Raman spectroscopy of oxidized and reduced [4Fe-4S] cluster, native enzyme contains an [4Fe-4S]2+ cluster
Fe
-
iron-sulfur center can be removed with 1,10-phenanthroline, resulting apoprotein is devoid of amino- and amidotransferase activity
additional information
-
low temperature magnetic circular dichroism, electron paramagnetic resonance and resonance Raman spectroscopy
additional information
-
S2- is oxidized by O2 to a mixture of sulfur oxides bound as thiocysteine and yet unidentified products
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 4.7 mM, 24 mM, 31 mM, 28 mM and 8.1 mM respectively
AMP
50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 0.9 mM, 6.1 mM, 2.5 mM, 2.6 mM and 1.5 mM respectively
GMP
50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 9.4 mM, 6.6 mM, 50 mM, 50 mM and 145 mM respectively
IMP
50% inhibition of wild-type and S347A mutant enzyme at 26 mM and 41 mM respectively
additional information
strong synergistic inhibition with ADP and GMP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
185000
-
highly concentrated enzyme solution, sucrose density gradient centrifugation, enzyme exists in equilibrium of tetramer, dimer and monomeric forms, conversion of dimer to tetramer within 10fold increase in protein concentration
200000
-
highly concentrated enzyme solution, gel filtration, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms, conversion of dimer to tetramer within 10fold increase in protein concentration, AMP and GMP stabilize the dimeric form, GDP stabilizes the tetrameric form
93000
-
sucrose density gradient centrifugation, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the ternary enzyme-ADP-GMP complex are grown in glass melting point capillaries by the microbath method, 20 mg/ml enzyme are incubated with 1 mM ADP, 1 mM GMP, and 5 mM MgCl2 and mixed with an equal volume of 24% polyethylene glycol 8000, 200 mM KCl, 50 mM N-(2-hydroxyethyl)piperazine-N'-3-propanesulfonic acid, pH 7.9, brown crystals emerge after 6-12 weeks
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADP or ADP and GMP, ratio 1/1, stabilize equilibrium between dimeric and tetrameric form
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phosphoribosyldiphosphate and other nucleotides antagonize stabilizing effect of AMP
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
in vitro O2 oxidizes iron in the Fe-S cluster to the high spin ferric state and sulfur to a mixtur of S in thiocystine residues plus other unidentified products
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489755
O2, rather than peroxide, superoxide, hydroxyl radical or singlet oxygen, inactivates, allosteric inhibitors, such as AMP, ADP, GMP or GDP modulate the rate of inactivation
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489753
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wong, J.Y.; Bernlohr, D.A.; Turnbough, C.L.; Switzer, R.L.
Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis
Biochemistry
20
5669-5674
1981
Bacillus subtilis
Wong, J.Y.; Switzer, R.L.
Affinity chromatography of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase
Arch. Biochem. Biophys.
196
134-137
1979
Bacillus subtilis
Bernlohr, D.A.; Switzer, R.L.
Reaction of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase with oxygen: chemistry and regulation by ligands
Biochemistry
20
5675-5681
1981
Bacillus subtilis
Holmes, E.W.
Kinetic, physical, and regulatory properties of amidophosphoribosyltransferase
Adv. Enzyme Regul.
19
215-231
1981
Bacillus subtilis, Cricetulus griseus, Columba livia, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus
Zalkin, H.
Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes
Adv. Enzyme Regul.
21
225-237
1983
Bacillus subtilis, Escherichia coli, Gallus gallus
Onate, Y.A.; Vollmer, S.J.; Switzer, R.L.; Johnson, M.K.
Spectroscopic characterization of the iron-sulfur cluster in Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase
J. Biol. Chem.
264
18386-18391
1989
Bacillus subtilis
Chen, S.; Tomchick, D.R.; Wolle, D.; Hu, P.; Smith, J.L.; Switzer, R.L.; Zalkin, H.
Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
Biochemistry
36
10718-10726
1997
Bacillus subtilis (P00497), Bacillus subtilis
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