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Enzyme Nomenclature
Information on EC 1.7.1.7 - GMP reductase
Word Map on EC 1.7.1.7
- 1.7.1.7
- purine
- guanine
- imp
-
salvage
-
phosphoribosyltransferase
- impdhs
- hypoxanthine
- adenylosuccinate
-
hypoxanthine-guanine
-
phosphoribosylpyrophosphate
-
6-linked
- medicine
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.7.1.7
-
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RECOMMENDED NAME
GeneOntology No.
GMP reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IMP + NH3 + NADP+ = GMP + NADPH + H+
mechanism: ordered sequential with GMP binding first
-
IMP + NH3 + NADP+ = GMP + NADPH + H+
ordered bi–bi kinetic mechanism, in which GMP binds first to the enzyme followed by NADPH binding, and NADP+ dissociates first followed by IMP release; ordered bi-bi kinetic mechanism, in which GMP binds first to the enzyme followed by NADPH binding, and NADP+ dissociates first followed by IMP release. GMP and IMP binding are thermodynamically favorable processes. Hydride transfer contributes to the rate-limiting step, and protonation and hydride transfer steps take place in the same transition state, lending support to a concerted mechanism. Product release does not contribute to the rate-limiting step of the reaction
-
IMP + NH3 + NADP+ = GMP + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive deamination
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
inosine-5'-phosphate:NADP+ oxidoreductase (aminating)
-
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CAS REGISTRY NUMBER
COMMENTARY
9029-32-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mutants containing mutations in the salvage pathway of purine synthesis
-
-
mRNA increases 30fold in brown adipose tissue within 6 h of cold exposure
SwissProt
enzyme synthesis is induced by 6-diazo-5-oxo-L-norleucine and glutamine starvation
-
-
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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
NADPH + H+ + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
the rate of the reverse reaction is 6% of the forward reaction
-
r
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
involved in salvage pathway of purine synthesis
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
specific for GMP
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
GMP and IMP binding are thermodynamically favorable processes. Protonation and hydride transfer steps take place in the same transition state. Product release does not contribute to the rate-limiting step of the reaction
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
specific for GMP
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
less than 10% of the NADPH rate: thionicotinamide-NADPH, deamino-NADPH, 3-acetylpyrimidine-NADPH
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
arabinosylGMP, 2'-dGMP and 8-azaGMP are reductively deaminated to their corresponding IMP analog at rates 1-2% the rate with GMP
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
essential for the salvage pathway of purine ribonucleotide biosynthesis
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
important for the maintenance of the intracellular adenine guanine balance, possible role in the regulation of differentiation of leukemia cells
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
enzyme may play a role in brown fat response
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
specific for GMP
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
enzyme is involved in interconversion of purine ribonucleotides
-
ir
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
involved in salvage pathway of purine synthesis
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
essential for the salvage pathway of purine ribonucleotide biosynthesis
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
important for the maintenance of the intracellular adenine guanine balance, possible role in the regulation of differentiation of leukemia cells
-
-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
Q9Z244
enzyme may play a role in brown fat response
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
enzyme is involved in interconversion of purine ribonucleotides
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no activity detected with NADH or adenosine 5'-phosphate; no cofactor: NADH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no requirement for monovalent or divalent cations
additional information
-
no requirement for monovalent or divalent cations
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-Chloro-9-beta-D-ribofuranosylpurine 5'-phosphate
-
0.01 mM, 80% inhibition after 40 min, 1 mM GMP protect
p-mercuribenzoate
-
2 mM, complete inhibition, complete protection by 2 mM GSH
ATP
-
no inhibition without Mg2+, MgATP: no inhibition at 0.010 mM-0.100 mM GMP, strong inhibition below 0.010 mM
XMP
-
0.001 mM, more than 50% inhibition; GTP and diguanosine tetraphosphate counteract inhibition
additional information
-
not inhibited by KCN
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
212.0 units/mg, 1 unit is defined as the amount of enzyme giving an optical density change of 1.00/min
additional information
-
72.4 units/mg, 1 unit is defined as the amount of enzyme producing a decrease in absorbancy at 340 nm of 0.1 per min
additional information
-
72.4 units/mg, 1 unit is defined as the amount of enzyme producing a decrease in absorbancy at 340 nm of 0.1 per min
additional information
-
72.4 units/mg, 1 unit is defined as the amount of enzyme producing a decrease in absorbancy at 340 nm of 0.1 per min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6: about 50% of activity at maximum, pH 9: about 70% of activity at maximum
7 - 9.5
-
pH 7: about 25% of activity at maximum, pH 9.5: about 30% of activity at maximum
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
not expressed in testis, lung, liver or spleen
5fold lower than in unstimulated brown adipose tisssue, no increase during cold-stress
5fold lower than in unstimulated brown adipose tisssue, no increase during cold-stress
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37382
-
4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
37384
-
4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
38000
-
4 * 38000, SDS-PAGE, 4 * 37383, calculated; 4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
40000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
4 * 38000, SDS-PAGE, 4 * 37383, calculated; 4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 2-mercaptoethanol, 6 months, less than 15% loss of activity after several rounds of freezing and thawing
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
transfection of HL-60 leukemia cells, expressed in COS-7 cells as His-tag fusion protein
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.7.1.7)
Information
