1.1.1.205: IMP dehydrogenase

This is an abbreviated version, for detailed information about IMP dehydrogenase, go to the full flat file.

Reaction

IMP
+
NAD+
+
H2O
=
XMP
+
NADH
+
H+

Synonyms

dehydrogenase, inosinate, EC 1.2.1.14, guaB2, IMD2, IMD3, IMD4, IMP dehydrogenase, IMP DH, IMP oxidoreductase, IMP-DH, IMP:NAD oxidoreductase, IMP:NAD+ oxidoreductase, IMPD, IMPDH, IMPDH II, IMPDH-1, IMPDH-B, IMPDH-S, IMPDH1, IMPDH2, inosinate dehydrogenase, inosine 5' monophosphate dehydrogenase, inosine 5'-monophosphate dehydrogenase, inosine 5'-monophosphate dehydrogenase 2, inosine 5'-phosphate dehydrogenase, inosine 5-monophosphate dehydrogenase, inosine 5-monophosphate dehydrogenase type I, inosine 5 -monophosphate dehydrogenase, inosine monophosphate dehydrogenase, inosine monophosphate oxidoreductase, inosine-5'-monophosphate dehydrogenase, inosine-5'-phosphate dehydrogenase, inosinic acid 5-monophosphate dehydrogenase, inosinic acid dehydrogenase, mpaF, Raspberry protein, SOI12, Superoxide-inducible protein 12, type 1 inosine monophosphate, type 2 inosine monophosphate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.205 IMP dehydrogenase

General Information

General Information on EC 1.1.1.205 - IMP dehydrogenase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
isiform IMPDH2 undergoes time-dependent proteolysis with the protease-sensitive region mapping within the catalytic domain. Both IMPDH1 and IMPDH2 proteins show reduced proteolysis with pre-incubation of IMP. The presence of AMP results in significant protection of IMPDH2, via a mechanism involving conformational changes upon nucleotide binding to the Bateman domain without affecting catalytic activity; isoform IMPDH1 undergoes time-dependent proteolysis with the protease-sensitive region mapping within the catalytic domain. Both IMPDH1 and IMPDH2 proteins show reduced proteolysis with pre-incubation of IMP. The presence of ATP results in significant protection of IMPDH1, via a mechanism involving conformational changes upon nucleotide binding to the Bateman domain without affecting catalytic activity. Mutation R224P, responsible for retinitis pigmentosa, abolishes ATP binding and nucleotide protection and this correlates with an altered propensity to cluster
physiological function