2HOX

alliinase from allium sativum (garlic)

2HOX の概要

• エントリーDOI: 10.2210/pdb2hox/pdb
• 関連するPDBエントリー: 2HOR
• 分子名称: Alliin lyase 1, beta-D-xylopyranose-(1-2)-[beta-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: cysteine sulphoxide lyase, alliinase, lyase
• 由来する生物種: Allium sativum (garlic)
• 細胞内の位置: Vacuole: Q01594
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 202532.77

構造登録者

Shimon, L.J.W.,Rabinkov, A.,Wilcheck, M.,Mirelman, D.,Frolow, F. (登録日: 2006-07-17, 公開日: 2007-02-06, 最終更新日: 2024-10-30)

主引用文献

Shimon, L.J.,Rabinkov, A.,Shin, I.,Miron, T.,Mirelman, D.,Wilchek, M.,Frolow, F.
Two Structures of Alliinase from Alliium sativum L.: Apo Form and Ternary Complex with Aminoacrylate Reaction Intermediate Covalently Bound to the PLP Cofactor.
J.Mol.Biol., 366:611-625, 2007

PubMed Abstract: Alliinase (alliin lyase EC 4.4.1.4), a PLP-dependent alpha, beta-eliminating lyase, constitutes one of the major protein components of garlic (Alliium sativum L.) bulbs. The enzyme is a homodimeric glycoprotein and catalyzes the conversion of a specific non-protein sulfur-containing amino acid alliin ((+S)-allyl-L-cysteine sulfoxide) to allicin (diallyl thiosulfinate, the well known biologically active component of freshly crushed garlic), pyruvate and ammonia. The enzyme was crystallized in the presence of (+S)-allyl-L-cysteine, forming dendrite-like monoclinic crystals. In addition, intentionally produced apo-enzyme was crystallized in tetragonal form. These structures of alliinase with associated glycans were resolved to 1.4 A and 1.61 A by molecular replacement. Branched hexasaccharide chains N-linked to Asn146 and trisaccharide chains N-linked to Asn328 are seen. The structure of hexasaccharide was found similar to "short chain complex vacuole type" oligosaccharide most commonly seen in plant glycoproteins. An unexpected state of the enzyme active site has been observed in the present structure. The electron density in the region of the cofactor made it possible to identify the cofactor moiety as aminoacrylate intermediate covalently bound to the PLP cofactor. It was found in the present structure to be stabilized by large number of interactions with surrounding protein residues. Moreover, the existence of the expected internal aldimine bond between the epsilon-amino group of Lys251 and the aldehyde of the PLP is ruled out on the basis of a distinct separation of electron density of Lys251. The structure of the active site cavity in the apo-form is nearly identical to that seen in the holo-form, with two sulfate ions, an acetate and several water molecules from crystallization conditions that replace and mimic the PLP cofactor.

PubMed: 17174334
DOI: 10.1016/j.jmb.2006.11.041

実験手法

X-RAY DIFFRACTION (1.4 Å)