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Guanosine monophosphate reductase

GMP Reductase, guanosine monophosphate reductase, GMPR
This gene encodes an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP. The protein also functions in the re-utilization of free intracellular bases and purine nucleosides.[provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: ACID, IMPDH, CAN, HAD, STEP
Papers on GMP Reductase
Novel Characteristics of Trypanosoma brucei Guanosine 5'-monophosphate Reductase Distinct from Host Animals.
New
Inui et al., Sakai, Japan. In Plos Negl Trop Dis, Jan 2016
Guanosine 5'-monophosphate reductase (GMPR), which catalyzes the deamination of guanosine 5'-monophosphate (GMP) to inosine 5'-monophosphate (IMP), plays an important role in the interconversion of purine nucleotides to maintain the intracellular balance of their concentration.
Characterizing and optimizing human anticancer drug targets based on topological properties in the context of biological pathways.
New
Li et al., Daqing, China. In J Biomed Inform, Apr 2015
Furthermore, the performance for mercaptopurine was significant: 6 known targets (ADSL, GMPR2, GMPR, HPRT1, AMPD3, AMPD2) were ranked in the top 15 and other four out of the top 15 (MAT2A, CDKN1A, AREG, JUN) have the potentialities to become new targets for cancer therapy.
Identification of Pathogenicity-Related Genes in Biofilm-Defective Acidovorax citrulli by Transposon Tn5 Mutagenesis.
Sun et al., Shanghai, China. In Int J Mol Sci, 2014
Furthermore, sequence analysis indicated that the obtained 22 mutants were due to the insertion of Tn5 into eight genes, including Aave 4244 (cation diffusion facilitator family transporter), Aave 4286 (hypothetical protein), Aave 4189 (alpha/beta hydrolase fold), Aave 1911 (IMP dehydrogenase/GMP reductase domain), Aave 4383 (bacterial export proteins, family 1), Aave 4256 (Hsp70 protein), Aave 0003 (histidine kinase, DNA gyrase B, and HSP90-like ATPase), and Aave 2428 (pyridoxal-phosphate dependent enzyme).
A purine nucleotide biosynthesis enzyme guanosine monophosphate reductase is a suppressor of melanoma invasion.
Nikiforov et al., Buffalo, United States. In Cell Rep, 2013
Here, we report that expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of purine nucleotides, was downregulated in the invasive stages of human melanoma.
6p22.3 deletion: report of a patient with autism, severe intellectual disability and electroencephalographic anomalies.
Fichera et al., Serbia and Montenegro. In Mol Cytogenet, 2012
This deletion includes ATXN1, DTNBP1, JARID2 and MYLIP genes, known to play an important role in the brain, and the GMPR gene whose function in the nervous system is unknown.
The dynamic determinants of reaction specificity in the IMPDH/GMPR family of (β/α)(8) barrel enzymes.
Review
Hedstrom, Waltham, United States. In Crit Rev Biochem Mol Biol, 2012
The inosine monophosphate dehydrogenase (IMPDH)/guanosine monophosphate reductase (GMPR) family of (β/α)(8) enzymes presents an excellent opportunity to investigate how subtle changes in enzyme structure change reaction specificity.
Modulation of guanosine nucleotides biosynthetic pathways enhanced GDP-L-fucose production in recombinant Escherichia coli.
Seo et al., Seoul, South Korea. In Appl Microbiol Biotechnol, 2012
The effects of overexpression of inosine 5'-monophosphate (IMP) dehydrogenase, guanosine 5'-monophosphate (GMP) synthetase (GuaB and GuaA), GMP reductase (GuaC) and guanosine-inosine kinase (Gsk) on GDP-L-fucose production were investigated in a series of fed-batch fermentations.
Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes.
Hedstrom et al., Waltham, United States. In Nat Chem Biol, 2011
Inosine monophosphate dehydrogenase (IMPDH) and guanosine monophosphate reductase (GMPR) belong to the same structural family, share a common set of catalytic residues and bind the same ligands.
Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation.
Basso et al., Porto Alegre, Brazil. In Mol Biosyst, 2011
GMP reductase plays an important role in the conversion of nucleoside and nucleotide derivatives of guanine to adenine nucleotides.
Genetic variants influencing circulating lipid levels and risk of coronary artery disease.
Sandhu et al., King of Prussia, United States. In Arterioscler Thromb Vasc Biol, 2010
These include a potentially functional SNP in the SLC39A8 gene for HDL-C, an SNP near the MYLIP/GMPR and PPP1R3B genes for LDL-C, and at the AFF1 gene for triglycerides.
Identification and characterization of inosine 5-monophosphate dehydrogenase in Streptococcus suis type 2.
Lu et al., Nanjing, China. In Microb Pathog, 2009
A 957-bp gene, impdh, was identified in the virulent S. suis serotype 2 (SS2), and analysis of the predicted IMPDH sequence revealed IMP dehydrogenase/GMP reductase domain.
Isolation and molecular characterization of a cax gene from Capsella bursa-pastoris.
Tang et al., Shanghai, China. In Biocell, 2008
The predicted CbCAX51 contained an IMP dehydrogenase/GMP reductase domain, two Na+/Ca2+ exchanger protein domains.
The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover.
Markham et al., Philadelphia, United States. In Mol Microbiol, 2008
The activities of IMPDH, adenylosuccinate synthetase and GMP reductase were two to threefold lower in MP101 crude extracts compared with the BW25113 wild-type strain.
Use of pathway analysis and genome context methods for functional genomics of Mycoplasma pneumoniae nucleotide metabolism.
Schuster et al., Jena, Germany. In Gene, 2007
For the case that M. pneumoniae does not require adenine as a substrate, we suggest adenylosuccinate synthetase (EC 6.3.4.4), adenylosuccinate lyase (EC 4.3.2.2) and GMP reductase (EC 1.7.1.7)
Intervarietal differences in some metabolic functions associated with protein accumulation in rice grains.
Bhatia et al., Mumbai, India. In Theor Appl Genet, 1976
Total nitrogen, amino nitrogen, glutamic acid dehydrogenase (GDH) activity and incorporation of (3)H-uridine and (14)C-amino acids into RNA and proteins, respectively, were compared in the developing grains of three high-protein stocks (IR-480-5-9, GMPR-51 and Erythroceros) and a high-yielding, medium-protein cultivar IR-8.
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