GMP reductase
Class of enzymes / From Wikipedia, the free encyclopedia
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GMP reductase EC 1.7.1.7 (Guanosine 5'-monophosphate oxidoreductase ) is an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination of GMP into IMP.[1]
guanosine monophosphate reductase | |||||||
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Identifiers | |||||||
Symbol | GMPR | ||||||
NCBI gene | 2766 | ||||||
HGNC | 4376 | ||||||
OMIM | 139265 | ||||||
RefSeq | NM_006877 | ||||||
UniProt | P36959 | ||||||
Other data | |||||||
EC number | 1.7.1.7 | ||||||
Locus | Chr. 6 p23 | ||||||
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guanosine monophosphate reductase 2 | |||||||
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Identifiers | |||||||
Symbol | GMPR2 | ||||||
NCBI gene | 51292 | ||||||
HGNC | 4377 | ||||||
OMIM | 610781 | ||||||
RefSeq | NM_016576 | ||||||
UniProt | Q9P2T1 | ||||||
Other data | |||||||
Locus | Chr. 14 q11.2 | ||||||
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NADPH + guanosine 5-phosphate = NADP+ + inosine 5-phosphate + NH3
By converting guanosine nucleotides to inosine nucleotides, which serve as precursors to both adenosine (A) and G nucleotides, it helps maintains intracellular balance of A and G nucleotides.[2] GMP can be broken down (catabolized) by other enzymes, but GMPR catalyzes the only recognized route for converting GMP to AMP (indirectly, through the IMP intermediate).[3] Whereas the conversion of GMP to IMP involves a single enzyme, GMPR, the conversion of IMP to GMP involves two enzymes. First, inosine monophosphate dehydrogenase (IMPDH) catalyzes the conversion of IMP to XMP; then GMP synthetase (GMPS) catalyzes the conversion of XMP to GMP. These two pathways are inversely regulated, with conditions favoring IMPDH expression decreasing GMPR expression.[3] In melanocytic cells, GMP reductase gene expression may be regulated by MITF.[4] It is activated by GTP and inhibited by xanthosine 5'-monophosphate (XMP).[5]
The amino acid sequence that makes up the GMP reductase is similar across organisms. In humans, there are hGMPR1 and hGMPR2, 2 GMP reductases that are different in their amino acid sequence (90% of the sequence is conserved) but has the same function overall. Although hGMPR1 and hGMPR2 do not have an identical amino acid sequence, they have similar kinetic properties and they both use NADPH as a coenzyme for their catalyzed reaction.[6] Aside from human erythrocytes, GMPR has been isolated from E.coli as well as rodents.[7]