The active principle of garlic at atomic resolution

被引:58
作者
Kuettner, EB [1 ]
Hilgenfeld, R [1 ]
Weiss, MS [1 ]
机构
[1] Inst Mol Biotechnol, Dept Struct Biol & Crystallog, D-07745 Jena, Germany
关键词
D O I
10.1074/jbc.M208669200
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
Despite the fact that many cultures around the world value and utilize garlic as a fundamental component of their cuisine as well as of their medicine cabinets, relatively little is known about the plant's protein configuration that is responsible for the specific properties of garlic. Here, we report the three-dimensional structure of the garlic enzyme alliinase at 1.5 Angstrom resolution. Alliinase constitutes the major protein component in garlic bulbs, and it is able to cleave carbon-sulfur bonds. The active enzyme is a pyridoxal-5'-phosphate-dependent homodimeric glycoprotein and belongs to the class I family of pyridoxal-5'-phosphate-dependent enzymes. In addition, it contains a novel epidermal growth factor-like domain that makes it unique among all pyridoxal5'-phosphate-dependent enzymes.
引用
收藏
页码:46402 / 46407
页数:6
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