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Information on EC 2.7.6.1 - ribose-phosphate diphosphokinase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58761

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IUBMB Comments
dATP can also act as donor.
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This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q58761
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
prps1, prpp synthetase, phosphoribosylpyrophosphate synthetase, phosphoribosyl pyrophosphate synthetase, prpp synthase, prpps, prs-i, ribose-phosphate pyrophosphokinase, ppribp synthetase, 5-phosphoribosyl-1-pyrophosphate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoribosyl diphosphate synthase
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5-phosphoribose pyrophosphorylase
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-
-
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5-phosphoribosyl-1-pyrophosphate synthetase
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-
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5-phosphoribosyl-alpha-1-pyrophosphate synthetase
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-
-
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ATP:D-ribose-5-phosphate pyrophosphotransferase
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-
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phosphoribosyl-diphosphate synthetase
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-
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phosphoribosylpyrophosphate synthase
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-
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phosphoribosylpyrophosphate synthetase
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-
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PP-ribose P synthetase
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-
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PPRibP synthetase
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PRPP synthase
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PRPP synthetase
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pyrophosphokinase, ribose phosphate
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pyrophosphoribosylphosphate synthetase
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ribophosphate pyrophosphokinase
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ribose-5-phosphate pyrophosphokinase
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ribose-phosphate pyrophosphokinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphate transfer
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-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose-5-phosphate diphosphotransferase
dATP can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9015-83-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
the enzyme accepts ATP and dATP equally well as diphosphoryl donor
-
-
?
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
the enzyme accepts ATP and dATP equally well as diphosphoryl donor
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the activity of the enzyme depends on the presence of divalent cations, of which Mg2+ is the most effective. Mn2+ is also accepted, but the activity is less than 15% of that obtained with Mg2+, when assayed at pH 9.5
Mn2+
the activity of the enzyme depends on the presence of divalent cations, of which Mg2+ is the most effective. Mn2+ is also accepted, but the activity is less than 15% of that obtained with Mg2+, when assayed at pH 9.5
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
a single ADP binding site, the active site, is present per subunit
alpha,beta-methylene ATP
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
activates, maximal activity at 190 mM phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
ATP
pH and temperature not specified in the publication
2.8
D-ribose 5-phosphate
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057
ADP
pH and temperature not specified in the publication
0.85
alpha,beta-methylene ATP
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
the activity profile declines steeply above pH 10. At least in part, this reduction in activity at high pH values may be caused by the formation of a magnesium phosphate precipitate, and consequently cause Mg2+ depletion. At lower pH the activity increases more or less linearly from pH 6.0 to pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72 - 95
70% of maximal activity at 72°C and 95°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32229
4 * 32229, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 32229, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion technique
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
at pH 9.0, half-life: 8 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or -20°C in 25 mM Tris–HCl (pH 7.6), 50% (v/v) glycerol, purified enzyme is stable for at least 90 days when stored at
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kadziola, A.; Jepsen, C.H.; Johansson, E.; McGuire, J.; Larsen, S.; Hove-Jensen, B.
Novel class III phosphoribosyl diphosphate synthase: structure and properties of the tetrameric, phosphate-activated, non-allosterically inhibited enzyme from Methanocaldococcus jannaschii
J. Mol. Biol.
354
815-828
2005
Methanocaldococcus jannaschii (Q58761), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58761)
Manually annotated by BRENDA team