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Information on EC 1.7.1.7 - GMP reductase
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1.7.1.7 GMP reductaseSpecify your search results
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
EC 1.6.6.8, GMPR, GMPR2, guaC, Guanosine 5'-monophosphate oxidoreductase, guanosine 5'-monophosphate reductase, guanosine monophosphate reductase, guanosine monophosphate reductase 2, guanosine-5'-monophosphate reductase, guanylate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.6.6.8
GMPR
GMPR2
Guanosine 5'-monophosphate oxidoreductase
-
-
-
-
guanosine 5'-monophosphate reductase
guanosine monophosphate reductase
guanosine-5'-monophosphate reductase
guanylate reductase
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-
-
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NADPH:GMP oxidoreductase (deaminating)
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-
-
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reductase, guanylate
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-
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Tb927.5.2080
TbGMPR
TcGMPR
TCIL3000_5_1940
EC 1.6.6.8
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formerly
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guanosine 5'-monophosphate reductase
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guanosine monophosphate 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
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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
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IMP + NH3 + NADP+ = GMP + NADPH + H+
catalytic reaction mechanism, overview. GMPR catalyzes two different chemical transformations at the same active site via two different cofactor conformations, analysis by subtesla high resolution field cycling NMR relaxometry
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IMP + NH3 + NADP+ = GMP + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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reductive deamination
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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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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
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-
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?
additional information
?
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enzyme nucleotide bindng analysis, nucleotide binding alters the quarternary structure of the enzyme, overview
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GMP + NADPH + H+
IMP + NH3 + NADP+
reductive deamination of GMP, the back conversion of IMP to GMP is highly unfavorable
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-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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the rate of the reverse reaction is 6% of the forward reaction
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r
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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involved in salvage pathway of purine synthesis
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?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
-
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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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
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?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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specific for GMP
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
-
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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less than 10% of the NADPH rate: thionicotinamide-NADPH, deamino-NADPH, 3-acetylpyrimidine-NADPH
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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arabinosylGMP, 2'-dGMP and 8-azaGMP are reductively deaminated to their corresponding IMP analog at rates 1-2% the rate with GMP
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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essential for the salvage pathway of purine ribonucleotide biosynthesis
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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important for the maintenance of the intracellular adenine guanine balance, possible role in the regulation of differentiation of leukemia cells
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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specific for GMP
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
enzyme may play a role in brown fat response
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?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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-
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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specific for GMP
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ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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enzyme is involved in interconversion of purine ribonucleotides
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ir
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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
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
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-
ir
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
Q9Z244
enzyme may play a role in brown fat response
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?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
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enzyme is involved in interconversion of purine ribonucleotides
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ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no activity detected with NADH or adenosine 5'-phosphate; no cofactor: NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
highly activating, best monovalent cation, amino acid sequences of putative K+-binding sites of TbGMPR, overview
NaCl
additional information
additional information
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the human enzyme is not activated in the presence of KCl instead of NaCl; the human enzyme is not activated in the presence of KCl instead of NaCl
additional information
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no requirement for monovalent or divalent cations
additional information
-
no requirement for monovalent or divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-Chloro-9-beta-D-ribofuranosylpurine 5'-phosphate
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0.01 mM, 80% inhibition after 40 min, 1 mM GMP protect
p-mercuribenzoate
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2 mM, complete inhibition, complete protection by 2 mM GSH
ATP
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no inhibition without Mg2+, MgATP: no inhibition at 0.010 mM-0.100 mM GMP, strong inhibition below 0.010 mM
mizoribine 5'-monophosphate
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MZP, moderate inhibition; MZP, moderate inhibition
XMP
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0.001 mM, more than 50% inhibition; GTP and diguanosine tetraphosphate counteract inhibition
additional information
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no inhibition by ribavirin 5'-monophosphate; no inhibition by ribavirin 5'-monophosphate
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additional information
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not inhibited by KCN
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additional information
ribavirin acts as an anti-trypanosomal drug in vitro with IC50 = 0.0254 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Guanosine monophosphate reductase 1 is a potential therapeutic target for Alzheimer's disease.
Breast Neoplasms
Lack of expression of the proteins GMPR2 and PPAR? are associated with the basal phenotype and patient outcome in breast cancer.
Carcinogenesis
Lack of expression of the proteins GMPR2 and PPAR? are associated with the basal phenotype and patient outcome in breast cancer.
Leukemia
Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells.
Leukemia
Reciprocal alterations of GMP reductase and IMP dehydrogenase activities during differentiation in HL-60 leukemia cells.
Melanoma
A purine nucleotide biosynthesis enzyme guanosine monophosphate reductase is a suppressor of melanoma invasion.
Neoplasms
Characterizing and optimizing human anticancer drug targets based on topological properties in the context of biological pathways.
Neoplasms
Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells.
Starvation
Inhibition of cellular growth by increased guanine nucleotide pools. Characterization of an Escherichia coli mutant with a guanosine kinase that is insensitive to feedback inhibition by GTP.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic analysis
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additional information
additional information
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Michaelis-Menten steady-state kinetics; Michaelis-Menten steady-state kinetics
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additional information
additional information
Michaelis-Menten steady-state kinetics
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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
additional information
additional information
inhibition kinetics
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IC50 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
-
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
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212.0 units/mg, 1 unit is defined as the amount of enzyme giving an optical density change of 1.00/min
additional information
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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
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pH 6: about 50% of activity at maximum, pH 9: about 70% of activity at maximum
7 - 9.5
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pH 7: about 25% of activity at maximum, pH 9.5: about 30% of activity at maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mutants containing mutations in the salvage pathway of purine synthesis
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brenda
mRNA increases 30fold in brown adipose tissue within 6 h of cold exposure
SwissProt
brenda
enzyme synthesis is induced by 6-diazo-5-oxo-L-norleucine and glutamine starvation
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of purine nucleotides, is downregulated in invasive stages of human melanoma. From 9 arbitrarily chosen human metastatic melanoma cell lines, GMPR is expressed in only one cell line
brenda
additional information
not expressed in testis, lung, liver or spleen
brenda
5fold lower than in unstimulated brown adipose tisssue, no increase during cold-stress
brenda
5fold lower than in unstimulated brown adipose tisssue, no increase during cold-stress
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
of Trypanosoma brucei bloodstream forms
brenda
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of Trypanosoma brucei bloodstream forms
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brenda
constitutive expression of TcGMPR in glycosomes at all of the parasite's developmental stages
brenda
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constitutive expression of TcGMPR in glycosomes at all of the parasite's developmental stages
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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the enzyme activity establishes a link between guanosine metabolism and RHOGTPase-dependent melanoma cell invasion
physiological function
additional information
evolution
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GMPR shows high similarities in amino acid sequence and structure to inosine 5'-monophosphate dehydrogenase (IMPDH), EC 1.1.1.205, the enzyme catalyzing the NAD+-dependent oxidation of IMP to xanthosine 5'-monophosphate (XMP). But GMPR and IMPDH are generally distinguished by the cystathionine beta-synthase (CBS) domain, which is well conserved in IMPDHs but absent in GMPRs; GMPR shows high similarities in amino acid sequence and structure to inosine 5'-monophosphate dehydrogenase (IMPDH), EC 1.1.1.205, the enzyme catalyzing the NAD+-dependent oxidation of IMP to xanthosine 5'-monophosphate (XMP). But GMPR and IMPDH are generally distinguished by the cystathionine beta-synthase (CBS) domain, which is well conserved in IMPDHs but absent in GMPRs
evolution
GMPR shows high similarities in amino acid sequence and structure to inosine 5'-monophosphate dehydrogenase (IMPDH), EC 1.1.1.205, the enzyme catalyzing the NAD+-dependent oxidation of IMP to xanthosine 5'-monophosphate (XMP). But GMPR and IMPDH are generally distinguished by the cystathionine beta-synthase (CBS) domain, which is well conserved in IMPDHs but absent in GMPRs
evolution
-
GMPR shows high similarities in amino acid sequence and structure to inosine 5'-monophosphate dehydrogenase (IMPDH), EC 1.1.1.205, the enzyme catalyzing the NAD+-dependent oxidation of IMP to xanthosine 5'-monophosphate (XMP). But GMPR and IMPDH are generally distinguished by the cystathionine beta-synthase (CBS) domain, which is well conserved in IMPDHs but absent in GMPRs
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malfunction
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expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of purine nucleotides, is downregulated in invasive stages of human melanoma. Overexpression of catalytically inactive mutant GMPRC186A at levels comparable to overexpression of wild-type GMPR does not affect invasion in of melanoma cells
malfunction
loss of the cystathionine-beta-synthase, CBS, domain may impair the catalytic activity of mutant lmgmprDELTACBS and/or cause a disruption of the protein structure
physiological function
-
GMPR downregulates the amounts of several GTP-bound (active) RHO-GTPases, and suppresses the ability of melanoma cells to form invadopodia, to degrade extracellular matrix and invade in vitro, and to grow as tumor xenografts in vivo. Enzyme GMPR partially depletes intracellular GTP pools. GMPR is a melanoma invasion suppressor, its enzymatic activity affects melanoma cell invasion and melanoma cell tumorigenicity. GMPR affects formation of invadopodia and matrix degradation. GMPR differentially regulates activity of several RHO-family GTPases, overview
physiological function
the cystathionine-beta-synthase domains on the guanosine 5-monophosphate reductase regulates the enzymatic activity in response to guanylate nucleotide levels. Recombinant enzyme LmGMPR complements the DELTAguaC mutation in Escherichia coli strain H1174 lacking bacterial GMPR
physiological function
enzyme GMPR modulates the concentration of intracellular guanosine in the pathogen
physiological function
-
enzyme GMPR modulates the concentration of intracellular guanosine in the pathogen
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additional information
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kinetics and dynamics of GMP, IMP, and NADP+ when bound to enzyme GMPR: IMP and GMP are in fast exchange with GMPR. Analysis of interactions of substrate and cofactors with GMPR, epitope mapping, overview. Dynamic properties of ternary complexes in hydride transfer and deamination
additional information
LmGMPR subunits may adopt conformations with Trp121 differentially exposed to the aqueous environment, binding of ATP resulted in an emission spectrum with a lambdamax centered at 350 nm indicative of a conformational change that position Trp121 into a more solvent exposed environment
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37382
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4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
37384
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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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
quaternary structure determination, LmGMPR subunits may adopt conformations with Trp121 differentially exposed to the aqueous environment
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C186A
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site-directed mutagenesis, a catalytically inactive mutant, overexpression of GMPRC186A mutant at levels comparable to overexpression of wild-type GMPR does not affect invasion in of melanoma cells
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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
recombinant GST-tagged enzyme from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, the tag is cleaved off by a commercial protease, followed by dialysis
recombinant untagged enzyme from Escherichia coli strain H1174 by affinity chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene LMJF_17_0725, DNA and amino acid sequence determination and analysis, , the gene has a 131 amino acid insertion encoding two tandem CBS domains, sequence comparisons, recombinant expression in Escherichia coli strain H1174
gene Tb927.5.2080, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene TCIL3000_5_1940, recombinant expression in Escherichia coli
transfection of HL-60 leukemia cells, expressed in COS-7 cells as His-tag fusion protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of purine nucleotides, is downregulated in invasive stages of human melanoma
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
the enzyme is a target for the design of trypanocidal agents, e.g. based on mycophenolic acid
drug development
-
the enzyme is a target for the design of trypanocidal agents, e.g. based on mycophenolic acid
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moffat, K.G.; Mackinnon, G.
Cloning of the Escherichia coli K-12 guaC gene following its transposition into the RP4:Mu cointegrate
Gene
40
141-143
1985
Escherichia coli
brenda
Stephens, R.W.; Whittaker, V.K.
Calf thymus GMP reductase: control by XMP
Biochem. Biophys. Res. Commun.
53
975-981
1973
Bos taurus
brenda
Endo, T.; Uratani, B.; Freese, E.
Purine salvage pathways of Bacillus subtilis and effect of guanine on growth of GMP reductase mutants
J. Bacteriol.
155
169-179
1983
Bacillus subtilis
brenda
Andrews, S.C.; Guest, J.R.
Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12
Biochem. J.
255
35-43
1988
Escherichia coli
brenda
Spector, T.; Jones, T.E.
Guanosine 5-monophosphate reductase from Leishmania donovani. A possible chemotherapeutic target
Biochem. Pharmacol.
31
3891-3897
1982
Leishmania donovani
brenda
Neuhard, J.; Nygaard, P.
Escherichia coli and Salmonella typhimurium cellular and molecular biology
American Society for Microbiology Washington (Neidhardt, F. C. , Ingraham, J. L. , Low, K. B. , Magasanik, B. , Schaechter, M. , Umbarger, E. , eds. )
1
445-473
1987
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Garber, B.B.; Jochimsen, B.U.; Gots, J.S.
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Mitchell, A.; Sin, I.L.; Finch, L.R.
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Spector, T.; Jones, T.E.; Miller, R.L.
Reaction mechanism and specificity of human GMP reductase. Substrates, inhibitors, activators, and inactivators
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Homo sapiens
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Renart, M.F.; Renart, J.; Sillero, M.A.G.; Sillero, A.
Guanosine monophosphate reductase from Artemia salina: Inhibition by xanthosine monophosphate and activation by diguanosine tetraphosphate
Biochemistry
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Artemia salina
brenda
Renart, M.F.; Sillero, A.
GMP reductase in Artemia salina
Biochim. Biophys. Acta
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Artemia salina
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Mackenzie, J.J.; Sorensen, L.B.
Guanosine 5-phosphate reductase of human erythrocytes
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Homo sapiens
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Brox, L.W.; Hampton, A.
Inactivation of guanosine 5-phosphate reductase by 6-chloro-, 6-mercapto-, and 2-amino-6-mercapto-9-beta-D-ribofuranosylpurine 5-phosphates
Biochemistry
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Klebsiella aerogenes
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Mager, J.; Magasanik, B.
Guanosine 5'-phosphate reductase and its role in the interconversion of purine nucleotides
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Escherichia coli, Klebsiella aerogenes, Salmonella enterica subsp. enterica serovar Typhimurium
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Salvatore, D.; Bartha, T.; Larsen, P.R.
The guanosine monophosphate reductase gene is conserved in rats and its expression increases rapidly in brown adipose tissue during cold exposure
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Rattus norvegicus (Q9Z244)
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Deng, Y.; Wang, Z.; Ying, K.; Gu, S.; Ji, C.; Huang, Y.; Gu, X.; Wang, Y.; Xu, Y.; Li, Y.; Xie, Y.; Mao, Y.
NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties
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Homo sapiens, Homo sapiens (Q9P2T1), no activity in Haemophilus influenzae, no activity in Methanocaldococcus jannaschii, no activity in Mycoplasma genitalium
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Ji, C.N.; Ying, G.; Deng, Y.F.; Chen, S.; Zhang, W.H.; Shu, G.; Xie, Y.; Mao, Y.M.
Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human
Acta Crystallogr. Sect. D
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Homo sapiens
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Zhang, J.; Zhang, W.; Zou, D.; Chen, G.; Wan, T.; Zhang, M.; Cao, X.
Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells
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Homo sapiens, Homo sapiens (Q9P2T1)
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Mohamed Fahmy Gad El-Rab, S.; Abdel-Fattah Shoreit, A.; Fukumori, Y.
Effects of cadmium stress on growth, morphology, and protein expression in Rhodobacter capsulatus B10
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70
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Rhodobacter capsulatus, Rhodobacter capsulatus B10
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Li, J.; Wei, Z.; Zheng, M.; Gu, X.; Deng, Y.; Qiu, R.; Chen, F.; Ji, C.; Gong, W.; Xie, Y.; Mao, Y.
Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP
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Homo sapiens
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Martinelli, L.K.; Ducati, R.G.; Rosado, L.A.; Breda, A.; Selbach, B.P.; Santos, D.S.; Basso, L.A.
Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation
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2011
Escherichia coli
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Wawrzyniak, J.A.; Bianchi-Smiraglia, A.; Bshara, W.; Mannava, S.; Ackroyd, J.; Bagati, A.; Omilian, A.R.; Im, M.; Fedtsova, N.; Miecznikowski, J.C.; Moparthy, K.C.; Zucker, S.N.; Zhu, Q.; Kozlova, N.I.; Berman, A.E.; Hoek, K.S.; Gudkov, A.V.; Shewach, D.S.; Morrison, C.D.; Nikiforov, M.A.
A purine nucleotide biosynthesis enzyme guanosine monophosphate reductase is a suppressor of melanoma invasion
Cell Rep.
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493-507
2013
Homo sapiens, Homo sapiens (P36959)
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Rosenberg, M.M.; Redfield, A.G.; Roberts, M.F.; Hedstrom, L.
Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry
J. Biol. Chem.
291
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2016
Homo sapiens (Q9P2T1)
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Smith, S.; Boitz, J.; Chidambaram, E.S.; Chatterjee, A.; Ait-Tihyaty, M.; Ullman, B.; Jardim, A.
The cystathionine-beta-synthase domains on the guanosine 5'-monophosphate reductase and inosine 5'-monophosphate dehydrogenase enzymes from Leishmania regulate enzymatic activity in response to guanylate and adenylate nucleotide levels
Mol. Microbiol.
100
824-840
2016
Leishmania major (Q4QEB3)
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Sarwono, A.E.Y.; Suganuma, K.; Mitsuhashi, S.; Okada, T.; Musinguzi, S.P.; Shigetomi, K.; Inoue, N.; Ubukata, M.
Identification and characterization of guanosine 5'-monophosphate reductase of Trypanosoma congolense as a drug target
Parasitol. Int.
66
537-544
2017
Trypanosoma congolense (G0UMT0), Trypanosoma congolense, Trypanosoma congolense IL3000 (G0UMT0)
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Bessho, T.; Okada, T.; Kimura, C.; Shinohara, T.; Tomiyama, A.; Imamura, A.; Kuwamura, M.; Nishimura, K.; Fujimori, K.; Shuto, S.; Ishibashi, O.; Kubata, B.K.; Inui, T.
Novel characteristics of Trypanosoma brucei guanosine 5-monophosphate reductase distinct from host animals
PLoS Negl. Trop. Dis.
10
e0004339
2016
Homo sapiens (P36959), Homo sapiens (Q9P2T1), Trypanosoma brucei brucei (Q57ZS7), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q57ZS7)
brenda
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