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ABSTRACT:
SUBMITTER: Inagaki E
PROVIDER: S-EPMC2335078 | biostudies-literature | 2007 Jun
REPOSITORIES: biostudies-literature
Inagaki Eiji E Ohshima Noriyasu N Sakamoto Keiko K Babayeva Nigar D ND Kato Hiroaki H Yokoyama Shigeyuki S Tahirov Tahir H TH
Acta crystallographica. Section F, Structural biology and crystallization communications 20070505 Pt 6
Delta(1)-Pyrroline-5-carboxylate dehydrogenase (P5CDh) is known to preferentially use NAD(+) as a coenzyme. The k(cat) value of Thermus thermophilus P5CDh (TtP5CDh) is four times lower for NADP(+) than for NAD(+). The crystal structure of NADP(+)-bound TtP5CDh was solved in order to study the structure-activity relationships for the coenzymes. The binding mode of NADP(+) is essentially identical to that in the previously solved NAD(+)-bound form, except for the regions around the additional 2'-p ...[more]