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The "super mutant" of yeast FMN adenylyltransferase enhances the enzyme turnover rate by attenuating product inhibition.

ABSTRACT: FMN adenylyltransferase (FMNAT) is an essential enzyme catalyzing the last step of a two-step pathway converting riboflavin (vitamin B2) to FAD, the ubiquitous flavocoenzyme. A structure-based mutagenesis and steady-state kinetic analysis of yeast FMNAT unexpectedly revealed that mutant D181A had a much faster turnover rate than the wild-type enzyme. Product inhibition analysis showed that wild-type FMNAT is strongly inhibited by FAD, whereas the D181A mutant has an attenuated product inhibition. These results provide a structural basis for the product inhibition of the enzyme and suggest that product release may be the rate-limiting step of the reaction.

SUBMITTER: Huerta C

PROVIDER: S-EPMC3795796 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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The "super mutant" of yeast FMN adenylyltransferase enhances the enzyme turnover rate by attenuating product inhibition.

Huerta Carlos C Grishin Nick V NV Zhang Hong H

Biochemistry 20130515 21

FMN adenylyltransferase (FMNAT) is an essential enzyme catalyzing the last step of a two-step pathway converting riboflavin (vitamin B2) to FAD, the ubiquitous flavocoenzyme. A structure-based mutagenesis and steady-state kinetic analysis of yeast FMNAT unexpectedly revealed that mutant D181A had a much faster turnover rate than the wild-type enzyme. Product inhibition analysis showed that wild-type FMNAT is strongly inhibited by FAD, whereas the D181A mutant has an attenuated product inhibition ...[more]

PMID: 23663086

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