Biochemical Characterization and Crystal Structure of a Novel NAD⁺-Dependent Isocitrate Dehydrogenase from Phaeodactylum tricornutum.

ABSTRACT: The marine diatom Phaeodactylum tricornutum originated from a series of secondary symbiotic events and has been used as a model organism for studying diatom biology. A novel type II homodimeric isocitrate dehydrogenase from P. tricornutum (PtIDH1) was expressed, purified, and identified in detail through enzymatic characterization. Kinetic analysis showed that PtIDH1 is NAD⁺-dependent and has no detectable activity with NADP⁺. The catalytic efficiency of PtIDH1 for NAD⁺ is 0.16 μM^-1·s^-1 and 0.09 μM^-1·s^-1 in the presence of Mn²⁺ and Mg²⁺, respectively. Unlike other bacterial homodimeric NAD-IDHs, PtIDH1 activity was allosterically regulated by the isocitrate. Furthermore, the dim

SUBMITTER: Huang SP 

PROVIDER: S-EPMC7460673 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature