Literature summary for 1.1.1.205 extracted from

Thomas, E.C.; Gunter, J.H.; Webster, J.A.; Schieber, N.L.; Oorschot, V.; Parton, R.G.; Whitehead, J.P.
Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms (2012), PLoS ONE, 7, e51096.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in HeLa cell and CHO cell	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P12268	isoform IMPDH2	-
Homo sapiens	P20839	isoform IMPDH1	-

Synonyms

Synonyms	Comment	Organism
IMPDH1	-	Homo sapiens
IMPDH2	-	Homo sapiens

General Information

General Information	Comment	Organism
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	Homo sapiens
metabolism	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	Homo sapiens

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Release 2023.1 (January 2023)