大豆种皮过氧化物酶的共价结构

Covalent structure of soybean seed coat peroxidase.

作者信息

Welinder Karen G, Larsen Yvonne B

机构信息

Department of Protein Chemistry, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark.

出版信息

Biochim Biophys Acta. 2004 Apr 8;1698(1):121-6. doi: 10.1016/j.bbapap.2003.11.005.

DOI:10.1016/j.bbapap.2003.11.005

PMID:15063322

Abstract

Peroxidase from soybean seed coat (SBP) is very stable at high temperature, extremes of pH, and in organic solvent. At the same time, it is highly reactive towards both organic and inorganic substrates, similar to horseradish peroxidase. SBP has a wide range of potential applications, and its structure is of particular interest for engineering purposes and as a model for stable heme peroxidases. The covalent structure of SBP has been determined by Edman sequencing and MALDI-TOF MS. SBP is a highly heterogeneous glycoprotein with MS determined masses from 39 to 41 kDa. The mature protein consists of 306 residues starting with pyrrolidone carboxylic acid. Seven glycosylation sites have been observed, although some sites were only partially glycosylated. No putative plant peroxidases were orthologous to SBP. However, SBP showed greater than 70% amino acid sequence identity to peroxidases from other legumes recruited in various defense responses.

摘要

来自大豆种皮的过氧化物酶（SBP）在高温、极端pH值和有机溶剂中非常稳定。同时，它对有机和无机底物都具有高反应活性，类似于辣根过氧化物酶。SBP具有广泛的潜在应用，其结构对于工程目的以及作为稳定血红素过氧化物酶的模型特别受关注。SBP的共价结构已通过埃德曼测序和基质辅助激光解吸电离飞行时间质谱（MALDI-TOF MS）确定。SBP是一种高度异质的糖蛋白，质谱测定的质量为39至41 kDa。成熟蛋白由306个残基组成，起始于吡咯烷酮羧酸。已观察到七个糖基化位点，尽管有些位点仅部分糖基化。没有推定的植物过氧化物酶与SBP直系同源。然而，SBP与参与各种防御反应的其他豆科植物的过氧化物酶显示出超过70%的氨基酸序列同一性。