The Three-dimensional Structure of Alliinase from Garlic
[ALLN1_ALLSA] Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.
Publication Abstract from PubMed
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 A 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 pyridoxal-5'-phosphate-dependent enzymes.
The active principle of garlic at atomic resolution.,Kuettner EB, Hilgenfeld R, Weiss MS J Biol Chem. 2002 Nov 29;277(48):46402-7. Epub 2002 Sep 15. PMID:12235163
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.