EC Number   |
General Information |
Reference |
|---|
    1.7.1.7 | 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 |
-, 743568 |
| 1.7.1.7 | 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 |
764517 |
| 1.7.1.7 | malfunction |
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 |
742245 |
| 1.7.1.7 | 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 |
743300 |
| 1.7.1.7 | metabolism |
the enzyme activity establishes a link between guanosine metabolism and RHOGTPase-dependent melanoma cell invasion |
742245 |
| 1.7.1.7 | more |
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 |
742897 |
| 1.7.1.7 | more |
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 |
743300 |
| 1.7.1.7 | physiological function |
enzyme GMPR modulates the concentration of intracellular guanosine in the pathogen |
-, 743397 |
| 1.7.1.7 | 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 |
742245 |
| 1.7.1.7 | 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 |
743300 |
