|
IMP dehydrogenase (Inosine-5'-monophosphate dehydrogenase) (Inosinic acid dehydrogenaseis) (IMPDH) an enzyme that converts inosine monophosphate to xanthosine monophosphate: :inosine 5'-phosphate + NAD+ + H2O xanthosine 5'-phosphate + NADH + H+ It catalyzes the rate-limiting reaction of ''de novo'' GTP biosynthesis. IMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it. The structure of this enzyme is composed of a TIM barrel domain with two CBS domains inserted within a loop.〔〔 It is inhibited by Mycophenolic acid, ribavirin, and 6TGMP (6-thioguanine monophosphate). 6TGMP inhibition prevents purine interconversion and thus the synthesis of purine nucleotides. == Examples == Humans express the following two IMP dehydrogenase isozymes: 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「IMP dehydrogenase」の詳細全文を読む スポンサード リンク
|