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一种植物糖基水解酶家族32蛋白的X射线衍射结构:菊苣的果聚糖1-外切水解酶IIa

X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus.

作者信息

Verhaest Maureen, Van den Ende Wim, Roy Katrien Le, De Ranter Camiel J, Laere André Van, Rabijns Anja

机构信息

Laboratorium voor Analytische Chemie en Medicinale Fysicochemie, Faculteit Farmaceutische Wetenschappen, K.U. Leuven, E. Van Evenstraat 4, B-3000 Leuven, Belgium.

出版信息

Plant J. 2005 Feb;41(3):400-11. doi: 10.1111/j.1365-313X.2004.02304.x.

Abstract

Fructan 1-exohydrolase, an enzyme involved in fructan degradation, belongs to the glycosyl hydrolase family 32. The structure of isoenzyme 1-FEH IIa from Cichorium intybus is described at a resolution of 2.35 A. The structure consists of an N-terminal fivefold beta-propeller domain connected to two C-terminal beta-sheets. The putative active site is located entirely in the beta-propeller domain and is formed by amino acids which are highly conserved within glycosyl hydrolase family 32. The fructan-binding site is thought to be in the cleft formed between the two domains. The 1-FEH IIa structure is compared with the structures of two homologous but functionally different enzymes: a levansucrase from Bacillus subtilis (glycosyl hydrolase family 68) and an invertase from Thermotoga maritima (glycosyl hydrolase family 32).

摘要

果聚糖1-外切水解酶是一种参与果聚糖降解的酶,属于糖基水解酶家族32。菊苣中1-FEH IIa同工酶的结构以2.35埃的分辨率进行了描述。该结构由一个与两个C端β折叠相连的N端五重β螺旋桨结构域组成。推测的活性位点完全位于β螺旋桨结构域中,由糖基水解酶家族32中高度保守的氨基酸形成。果聚糖结合位点被认为位于两个结构域之间形成的裂隙中。将1-FEH IIa的结构与两种同源但功能不同的酶的结构进行了比较:一种来自枯草芽孢杆菌的果聚糖蔗糖酶(糖基水解酶家族68)和一种来自海栖热袍菌的转化酶(糖基水解酶家族32)。

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