1.7.1.7: GMP reductase
This is an abbreviated version!
For detailed information about GMP reductase, go to the full flat file.
Word Map on EC 1.7.1.7
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1.7.1.7
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purine
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imp
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salvage
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hypoxanthine
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impdhs
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hypoxanthine-guanine
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adenylosuccinate
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medicine
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drug development
- 1.7.1.7
- purine
- imp
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salvage
- hypoxanthine
- impdhs
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hypoxanthine-guanine
- adenylosuccinate
- medicine
- drug development
Reaction
Synonyms
EC 1.6.6.8, GMPR, GMPR-I, GMPR-II, GMPR2, guaC, Guanosine 5'-monophosphate oxidoreductase, guanosine 5'-monophosphate reductase, guanosine monophosphate reductase, guanosine monophosphate reductase 2, guanosine-5'-monophosphate reductase, guanylate reductase, HsGMPR1, HsGMPR2, LmGMPR, Lmj17.0725, LMJF_17_0725, NADPH:GMP oxidoreductase (deaminating), reductase, guanylate, Tb927.5.2080, TbGMPR, TcGMPR, TCIL3000_5_1940
ECTree
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General Information
General Information on EC 1.7.1.7 - GMP reductase
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evolution
malfunction
metabolism
the enzyme activity establishes a link between guanosine metabolism and RHOGTPase-dependent melanoma cell invasion
physiological function
additional information
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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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
malfunction
an enzyme mutation causes aberrant splicing, decreased enzyme protein levels in skeletal muscle of patient with autosomal dominant progressive external ophthalmoplegia, proliferating and quiescent cells, and is associated with subtle changes in nucleotide homeostasis protein levels and evidence of disturbed mitochondrial DNA maintenance in skeletal muscle
enzyme GMPR modulates the concentration of intracellular guanosine in the pathogen
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
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enzyme GMPR modulates the concentration of intracellular guanosine in the pathogen
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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