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Enzyme Nomenclature
Information on EC 1.7.1.7 - GMP reductase
for references in articles please use BRENDA:EC1.7.1.7
Word Map on EC 1.7.1.7
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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
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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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
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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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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
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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
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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
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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
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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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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
-
-
-
-
?
additional information
?
-
enzyme nucleotide bindng analysis, nucleotide binding alters the quarternary structure of the enzyme, overview
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-
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GMP + NADPH + H+
IMP + NH3 + NADP+
reductive deamination of GMP, the back conversion of IMP to GMP is highly unfavorable
-
-
?
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
-
-
-
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
-
-
-
?
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
-
-
-
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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
-
-
-
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
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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
-
-
-
-
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
-
specific for GMP
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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
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?
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
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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 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
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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
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
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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
KCl
highly activating, best monovalent cation, amino acid sequences of putative K+-binding sites of TbGMPR, overview
NaCl
additional information
additional information
-
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
-
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
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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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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
-
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
-
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
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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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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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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
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of Trypanosoma brucei bloodstream forms
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constitutive expression of TcGMPR in glycosomes at all of the parasite's developmental stages
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constitutive expression of TcGMPR in glycosomes at all of the parasite's developmental stages
-
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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
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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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C186A
-
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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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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