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Information on EC 2.4.2.17 - ATP phosphoribosyltransferase and Organism(s) Escherichia coli and UniProt Accession P60757
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2.4.2.17 ATP phosphoribosyltransferaseIUBMB Comments
Involved in histidine biosynthesis.
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Word Map
- 2.4.2.17
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hisgs
- l-histidine
- glutamicum
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hexameric
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hetero-octameric
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histidyl-trna
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long-form
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short-form
- drug development
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
atp-prt, atp phosphoribosyltransferase, atp-phosphoribosyltransferase, adenosine triphosphate phosphoribosyltransferase, atp phosphoribosyl transferase, atpprt, atp-phosphoribosyl transferase, atp-prtase, n-1-(5'-phosphoribosyl)-atp transferase, adenosine-triphosphate phosphoribosyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase
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adenosine triphosphate phosphoribosyltransferase
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ATP-PRT
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phosphoribosyl ATP synthetase
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phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase
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phosphoribosyl-ATP pyrophosphorylase
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phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase
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phosphoribosyladenosine triphosphate pyrophosphorylase
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phosphoribosyladenosine triphosphate synthetase
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phosphoribosyltransferase, adenosine triphosphate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
substrate binding sites, e.g. Cys104, Asn75, Ser154, Glu156, and Val155, reaction mechanism
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes
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1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
double displacement mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-alpha-D-ribosyl-transferase
Involved in histidine biosynthesis.
CAS REGISTRY NUMBER
COMMENTARY
9031-46-3
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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
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
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first step in histidine biosynthesis
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway
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ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
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r
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
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway
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?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
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first step in histidine biosynthesis
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
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linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation
dicoumarol
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competitive with respect to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
dinitrophenol
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diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
Pentachlorophenol
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competitive to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
additional information
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carbonylcyanide m-chlorophenylhydrazone, which is a potent inhibitor of several enzymes with adenine-containing substrates or coenzymes has no effect
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L-histidine
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stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant selenomethionine-labeled enzyme in complex with inhibitor AMP or with product 1-(5-phospho-D-ribosyl)-ATP, X-ray diffraction enzyme-inhibitor complex structure determination and analysis at 2.7 A resolution, X-ray diffraction enzyme-product complex structure determination and analysis at 2.9 A resolution, modeling
vapour diffusion method, trigonal prisms are obtained using 1.3 M sodium tartrate, 50-200 mM magnesium chloride, 100 mM citrate buffer pH 5.6 and enzyme in the presence of 2 mM AMP, round shaped crystals are obtained with 1.36-1.44 M ammonium sulfate, 0-0.3 M sodium chloride, 100 mM HEPES buffer pH 7.5 and enzyme in the presence of 2 mM AMP
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47.5
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1.9 mg enzyme/ml, 80 min, 75% loss of activity without addition of AMP, with 0.05 mM AMP about 60% loss of activity, with 0.5 mM AMP about 40% loss of activity, with 5 mM AMP about 25% loss of activity
48
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3 mg enzyme/ml, 10 min, 15% remaining activity without addition of histidine, with 0.000086 mM histidine about 15% remaining activity after 15 min, with 0.00069 mM histidine about 70% remaining activity after 80 min, with 0.00345 mM histidine about 80% remaining activity after 80 min, with 0.0069 mM histidine about 55% remaining activity after 50 min
additional information
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heat inactivation depends on protein concentration and inhibitors
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
histidine or AMP stabilizes the enzyme with respect to thermal inactivation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.5, 0.4 mM DTT and one protease inhibitor per litre, 50% v/v glycerol, long term storage
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tebar, A.R.; Ballesteros, A.O.
Kinetic properties of ATP phosphoribosyltransferase of Escherichia coli
Mol. Cell. Biochem.
11
131-136
1976
Escherichia coli
Dall-Larsen, T.; Kryvi, H.; Klungsoyr, L.
Dinitrophenol, dicoumarol and pentachlorophenol as inhibitors and parasite substrates in the ATP phosphoribosyltransferase reaction
Eur. J. Biochem.
66
443-446
1976
Escherichia coli
Kryvi, H.
Thermal stability of phosphoribosyladenosine triphosphate synthetase as reflected in its circular dichroism and activity properties. Effect of inhibitors
Biochim. Biophys. Acta
317
123-130
1973
Escherichia coli
Lohkamp, B.; Coggins, J.R.; Lapthorn, A.J.
Purification, crystallization and preliminary x-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli
Acta Crystallogr. Sect. D
56
1488-1491
2000
Escherichia coli
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