Covalent structure of soybean seed coat peroxidase

被引：27

作者：

Welinder, KG

Larsen, YB

机构：

[1] Univ Aalborg, Inst Biotechnol, Dept Life Sci, DK-9000 Aalborg, Denmark

[2] Univ Copenhagen, Inst Mol Biol, Dept Prot Chem, DK-1353 Copenhagen, Denmark

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2004年 / 1698卷 / 01期

关键词：

Edman sequencing; glycoprotein; MALDI-TOF MS; propeptide; protein modification; pyrrolidone carboxylyl;

D O I：

10.1016/j.bbapap.2003.11.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Elsevier B.V. All rights reserved.

引用

页码：121 / 126

页数：6

共 19 条

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