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Information on EC 3.1.3.99 - IMP-specific 5'-nucleotidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q99312

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.99 IMP-specific 5'-nucleotidase
IUBMB Comments
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+.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q99312
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
imp-specific 5'-nucleotidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMP-specific 5-nucleotidase
-
inosine 5'-monophosphate-specific 5'-nucleotidase
-
Isn1
formerly named YOR155c, gene name
IMP-specific 5-nucleotidase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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+.
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
-
-
-
?
IMP + H2O
inosine + phosphate
show the reaction diagram
-
highly specific substrate
-
-
?
additional information
?
-
-
no activity with AMP, dIMP, GMP, XMP, UMP, dTMP, CMP, 2'(3')-IMP, D-ribose 5-phosphate, phenyl phosphate, and beta-glyerophosphate
-
-
?
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
IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
?
IMP + H2O
inosine + phosphate
show the reaction diagram
-
highly specific substrate
-
-
?
additional information
?
-
-
no activity with AMP, dIMP, GMP, XMP, UMP, dTMP, CMP, 2'(3')-IMP, D-ribose 5-phosphate, phenyl phosphate, and beta-glyerophosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
may substitute Mg2+
Mg2+
-
enzyme activity is absolutely dependent on bivalent metals with Mg2+ as most potent one
Mn2+
-
may substitute Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CTP
-
86% residual activity at 2.5 mM
GTP
-
75% residual activity at 2.5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
121% activity at 2.5 mM
ATP
-
243% activity at 2.5 mM
cyclic AMP
-
130% activity at 2.5 mM
diadenosine pentaphosphate
-
252% activity at 2.5 mM
Diadenosine tetraphosphate
-
283% activity at 2.5 mM
diadenosine triphosphate
-
200% activity at 2.5 mM
UTP
-
139% activity at 2.5 mM
additional information
-
not stimulated by AMP, GTP, CTP, adenosine 5'-[alpha,beta-methylene]diphosphate, and 2,3-bisphosphoglycerate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.056
-
crude extract, at pH 6.5 and 37°C
102.5
-
after 1830.4fold purification, at pH 6.5 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
with 100 mM imidazole/HCl buffer or 100 mM sodium acetate buffer in the presence of 25 mM Mg2+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme regulates intracellular IMP amounts
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220000
-
gel filtration
55400
-
2 * 55400, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 1480, calculated from amino acid sequence
homotetramer
-
2 * 55400, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-Toyopearl column chromatography
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, R.
Purification and some properties of an IMP-specific 5'-nucleotidase from yeast
Biochem. J.
298
593-598
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Itoh, R.; Saint-Marc, C.; Chaignepain, S.; Katahira, R.; Schmitter, J.M.; Daignan-Fornier, B.
The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5-nucleotidase
BMC Biochem.
4
4-4
2003
Saccharomyces cerevisiae (Q99312), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q99312)
Manually annotated by BRENDA team