1YY5

Crystal structure of Fms1, a polyamine oxidase from Yeast

1YY5 の概要

• エントリーDOI: 10.2210/pdb1yy5/pdb
• 関連するPDBエントリー: 1rsg 1xpq
• 分子名称: FMS1 protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: polyamine oxidase, fms1, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 118629.40

構造登録者

Huang, Q.,Liu, Q.,Hao, Q. (登録日: 2005-02-23, 公開日: 2005-03-08, 最終更新日: 2024-10-30)

主引用文献

Huang, Q.,Liu, Q.,Hao, Q.
Crystal Structures of Fms1 and its Complex with Spermine Reveal Substrate Specificity.
J.Mol.Biol., 348:951-959, 2005

PubMed Abstract: Fms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in yeast. Fms1 has polyamine oxidase (PAO) activity, which converts spermine into spermidine and 3-aminopropanal. The 3-aminopropanal is further oxidized to produce beta-alanine, which is necessary for the biosynthesis of pantothenic acid. The crystal structures of Fms1 and its complex with the substrate spermine have been determined using the single-wavelength anomalous diffraction (SAD) phasing method. Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain. The active site is a tunnel located at the interface of the two domains. The substrate spermine binds to the active site mainly via hydrogen bonds and hydrophobic interactions. In the complex, C11 but not C9 of spermine is close enough to the catalytic site (N5 of FAD) to be oxidized. Therefore, the products are spermidine and 3-aminopropanal, rather than 3-(aminopropyl) 4-aminobutyraldehyde and 1,3-diaminoprone.

PubMed: 15843025
DOI: 10.1016/j.jmb.2005.03.008

実験手法

X-RAY DIFFRACTION (2.3 Å)