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Literature summary for 1.7.1.7 extracted from

  • Rosenberg, M.M.; Redfield, A.G.; Roberts, M.F.; Hedstrom, L.
    Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry (2016), J. Biol. Chem., 291, 22988-22998 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GMP + NADPH + H+ Homo sapiens
-
IMP + NH3 + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9P2T1
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GMP + NADPH + H+
-
Homo sapiens IMP + NH3 + NADP+
-
?

Synonyms

Synonyms Comment Organism
GMPR
-
Homo sapiens
GMPR2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Homo sapiens

General Information

General Information Comment Organism
additional information 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 Homo sapiens