Structure and-function of bovine pancreatic deoxyribonuclease I

被引：17

作者：

Chen, Wei-Jung

Liao, Ta-Hsiu

机构：

[1] Natl Ilan Univ, Coll Bioresources, Inst Biotechnol, Ilan 260, Taiwan

[2] Natl Taiwan Univ, Coll Med, Inst Biochem & Mol Biol, Ilan 260, Taiwan

来源：

PROTEIN AND PEPTIDE LETTERS | 2006年 / 13卷 / 05期

关键词：

deoxyribonuclease; calcium; disulfide; protein folding; chemical modification; site-directed mutagenesis; enzyme mechanism;

D O I：

10.2174/092986606776819475

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：

Bovine pancreatic deoxyribonuclehse I (bpDNase), the first DNase discovered, is the best characterized among various types of DNase, A catalytic mechanism has been suggested based on the X-ray structure of the bpDNase-octamer complex. In this review, we will focus on three aspects: 1) the distinctive functions of the two structural calcium atoms; 2) the biological functions of the two disulfides; and 3) the involvement of the N- and C-terminal fragments in the enzyme folding for activity.

引用

页码：447 / 453

页数：7

共 69 条

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