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D-octopine dehydrogenase
Octopine dehydrogenase (N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase, OcDH, ODH) is a dehydrogenase enzyme in the opine dehydrogenase family that helps maintain redox balance under anaerobic conditions. It is found largely in aquatic invertebrates, especially mollusks, sipunculids, and coelenterates, and plays a role analogous to lactate dehydrogenase (found largely in vertebrates)
. In the presence of NADH, OcDH catalyzes the reductive condensation of an α-keto acid with an amino acid to form N-carboxyalkyl-amino acids (opines).〔 The purpose of this reaction is to reoxidize glycolytically formed NADH to NAD+, replenishing this important reductant used in glycolysis and allowing for the continued production of ATP in the absence of oxygen.
:L-arginine + pyruvate + NADH + H+ D-octopine + NAD+ + H2O
== Structure ==
OcDH is a monomer with a molecular weight of 38kD made of two functionally distinct subunits. The first, Domain I, is composed of 199 amino acids and contains a Rossmann fold. Domain II is composed of 204 amino acids and is connected to the Rossmann fold of Domain I via its N-terminus.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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