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Literature DB >> 23663086

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

Carlos Huerta¹, Nick V Grishin, Hong Zhang.

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.

Entities: CellLine Chemical Disease Gene Mutation Species

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Year: 2013 PMID： 23663086 PMCID： PMC3795796 DOI： 10.1021/bi400454w

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

15 in total

1. Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins.

Authors: Enza M Torchetti; Francesco Bonomi; Michele Galluccio; Elisabetta Gianazza; Teresa A Giancaspero; Stefania Iametti; Cesare Indiveri; Maria Barile
Journal: FEBS J Date: 2011-10-20 Impact factor: 5.542

Review 2. Biosynthesis of flavocoenzymes.

Authors: Markus Fischer; Adelbert Bacher
Journal: Nat Prod Rep Date: 2005-04-21 Impact factor: 13.423

Review 3. Flavoenzymes.

Authors: Vivi Joosten; Willem J H van Berkel
Journal: Curr Opin Chem Biol Date: 2007-02-01 Impact factor: 8.822

4. Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.

Authors: Justin Chartron; Kate S Carroll; Carrie Shiau; Hong Gao; Julie A Leary; Carolyn R Bertozzi; C David Stout
Journal: J Mol Biol Date: 2006-09-01 Impact factor: 5.469

5. A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.

Authors: P Bork; E V Koonin
Journal: Proteins Date: 1994-12

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

1. Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins.

Review 2. Biosynthesis of flavocoenzymes.

Review 3. Flavoenzymes.

4. Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.

5. A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.

Review 6. Sequence-structure analysis of FAD-containing proteins.

7. Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver.

8. Purification, properties, and function of flavokinase from rat intestinal mucosa.

9. Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.

10. Effect of riboflavin status on hepatic activities of flavin-metabolizing enzymes in rats.

Review 1. Production of riboflavin and related cofactors by biotechnological processes.

2. Insights into the FMNAT Active Site of FAD Synthase: Aromaticity is Essential for Flavin Binding and Catalysis.

3. Mutation of Aspartate 238 in FAD Synthase Isoform 6 Increases the Specific Activity by Weakening the FAD Binding.