2W8S

CRYSTAL STRUCTURE OF A catalytically promiscuous PHOSPHONATE MONOESTER HYDROLASE FROM Burkholderia caryophylli

2W8S の概要

• エントリーDOI: 10.2210/pdb2w8s/pdb
• 分子名称: PHOSPHONATE MONOESTER HYDROLASE, ZINC ION, FE (III) ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, formylglycine, phosphodiesterase, alkaline phosphatase superfamily, catalytic promiscuity, phosphonate monoester hydrolase
• 由来する生物種: BURKHOLDERIA CARYOPHYLLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 246407.00

構造登録者

Jonas, S.,van Loo, B.,Hyvonen, M.,Hollfelder, F. (登録日: 2009-01-19, 公開日: 2010-02-23, 最終更新日: 2023-12-13)

主引用文献

Van Loo, B.,Jonas, S.,Babtie, A.C.,Benjdia, A.,Berteau, O.,Hyvonen, M.,Hollfelder, F.
An Efficient, Multiply Promiscuous Hydrolase in the Alkaline Phosphatase Superfamily.
Proc.Natl.Acad.Sci.USA, 107:2740-, 2010

PubMed Abstract: We report a catalytically promiscuous enzyme able to efficiently promote the hydrolysis of six different substrate classes. Originally assigned as a phosphonate monoester hydrolase (PMH) this enzyme exhibits substantial second-order rate accelerations ((k(cat)/K(M))/k(w)), ranging from 10(7) to as high as 10(19), for the hydrolyses of phosphate mono-, di-, and triesters, phosphonate monoesters, sulfate monoesters, and sulfonate monoesters. This substrate collection encompasses a range of substrate charges between 0 and -2, transition states of a different nature, and involves attack at two different reaction centers (P and S). Intrinsic reactivities (half-lives) range from 200 days to 10(5) years under near neutrality. The substantial rate accelerations for a set of relatively difficult reactions suggest that efficient catalysis is not necessarily limited to efficient stabilization of just one transition state. The crystal structure of PMH identifies it as a member of the alkaline phosphatase superfamily. PMH encompasses four of the native activities previously observed in this superfamily and extends its repertoire by two further activities, one of which, sulfonate monoesterase, has not been observed previously for a natural enzyme. PMH is thus one of the most promiscuous hydrolases described to date. The functional links between superfamily activities can be presumed to have played a role in functional evolution by gene duplication.

PubMed: 20133613
DOI: 10.1073/PNAS.0903951107

実験手法

X-RAY DIFFRACTION (2.4 Å)