Title : Kinetic and Binding Studies of Streptococcus pneumoniae Type 2 Isopentenyl Diphosphate:Dimethylallyl Diphosphate Isomerase.

Pub. Date : 2016 Apr 19

PMID : 27003727






2 Functional Relationships(s)
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1 For IDI-2 from the pathogenic bacterium Streptococcus pneumoniae, the flavin can be treated kinetically as a dissociable cosubstrate in incubations with IPP and excess NADH. 4,6-dinitro-o-cresol isopentenyl-diphosphate delta isomerase 2 Homo sapiens
2 Dithionite reduction of FMN in the IDI-2 FMN and IPP mixture was biphasic with k(red)(IDI-2 FMN IPP (fast)) = 326 s(-1) and k(red)(IDI-2 FMN IPP (slow)) = 6.9 s(-1) The pseudo-first-order rate constant for the slow component was similar to those for NADH reduction of the flavin in the IDI-2 FMN and IPP mixture and may reflect a rate-limiting conformational change in the enzyme. 4,6-dinitro-o-cresol isopentenyl-diphosphate delta isomerase 2 Homo sapiens