4KKV

Crystal structure of candida glabrata FMN adenylyltransferase D181A Mutant

4KKV の概要

• エントリーDOI: 10.2210/pdb4kkv/pdb
• 関連するPDBエントリー: 3FWK 3G59 3G5A 3G6K
• 分子名称: Similar to uniprot|P38913 Saccharomyces cerevisiae YDL045c FAD synthetase, beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta protein, rossmann-like fold, transferase, fad biosynthesis
• 由来する生物種: Candida glabrata (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36157.32

構造登録者

Huerta, C.,Zhang, H. (登録日: 2013-05-06, 公開日: 2013-05-29, 最終更新日: 2023-09-20)

主引用文献

Huerta, C.,Grishin, N.V.,Zhang, H.
The "Super Mutant" of Yeast FMN Adenylyltransferase Enhances the Enzyme Turnover Rate by Attenuating Product Inhibition.
Biochemistry, 52:3615-3617, 2013

PubMed 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.

PubMed: 23663086
DOI: 10.1021/bi400454w

実験手法

X-RAY DIFFRACTION (1.74 Å)