Information on EC 3.1.3.99 - IMP-specific 5'-nucleotidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.99
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RECOMMENDED NAME
GeneOntology No.
IMP-specific 5'-nucleotidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
IMP + H2O = inosine + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine nucleotides degradation I
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Purine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
inosine 5'-phosphate phosphohydrolase
The enzyme, isolated from the yeast Saccharomyces cerevisiae, is highly specific for inosine 5'-phosphate, and has no detectable activity with other purine and pyrimidine nucleotides. Requires divalent metals, such as Mg2+, Co2+ or Mn2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
IMP + H2O
inosine + phosphate
show the reaction diagram
additional information
?
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no activity with AMP, dIMP, GMP, XMP, UMP, dTMP, CMP, 2'(3')-IMP, D-ribose 5-phosphate, phenyl phosphate, and beta-glyerophosphate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
IMP + H2O
inosine + phosphate
show the reaction diagram
additional information
?
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no activity with AMP, dIMP, GMP, XMP, UMP, dTMP, CMP, 2'(3')-IMP, D-ribose 5-phosphate, phenyl phosphate, and beta-glyerophosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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may substitute Mg2+
Mg2+
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enzyme activity is absolutely dependent on bivalent metals with Mg2+ as most potent one
Mn2+
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may substitute Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-deoxy-5'-isobutylthioadenosine
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noncompetitive inhibition
5'-deoxy-5'-isobutylthioinosine
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noncompetitive inhibition
CTP
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86% residual activity at 2.5 mM
GTP
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75% residual activity at 2.5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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121% activity at 2.5 mM
ATP
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243% activity at 2.5 mM
cyclic AMP
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130% activity at 2.5 mM
diadenosine pentaphosphate
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252% activity at 2.5 mM
Diadenosine tetraphosphate
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283% activity at 2.5 mM
diadenosine triphosphate
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200% activity at 2.5 mM
UTP
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139% activity at 2.5 mM
additional information
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not stimulated by AMP, GTP, CTP, adenosine 5'-[alpha,beta-methylene]diphosphate, and 2,3-bisphosphoglycerate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
5'-deoxy-5'-isobutylthioadenosine
Rattus norvegicus
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at pH 7.4 and 37C
710
5'-deoxy-5'-isobutylthioinosine
Rattus norvegicus
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at pH 7.4 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.056
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crude extract, at pH 6.5 and 37C
102.5
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after 1830.4fold purification, at pH 6.5 and 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
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with 100 mM imidazole/HCl buffer or 100 mM sodium acetate buffer in the presence of 25 mM Mg2+
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55400
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2 * 55400, SDS-PAGE
220000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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2 * 55400, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-Toyopearl column chromatography
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