1lk9
From Proteopedia
|
The Three-dimensional Structure of Alliinase from Garlic
Overview
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.
About this Structure
1LK9 is a Single protein structure of sequence from Allium sativum with , , , and as ligands. Active as Alliin lyase, with EC number 4.4.1.4 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:45:41 2008
Categories: Alliin lyase | Allium sativum | Single protein | Hilgenfeld, R. | Kuettner, E B. | Weiss, M S. | CL | DHA | EPE | PLP | SO4 | Chloride binding | Egf-like domain | Plp type 1
