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Cited by 69Enzyme Structure and FunctionGarlic and Onion StudiesProtein Structure and Dynamics

Two Structures of Alliinase from Alliium sativum L.: Apo Form and Ternary Complex with Aminoacrylate Reaction Intermediate Covalently Bound to the PLP Cofactor

Shimon, Linda J.W., Rabinkov, Aharon, Shin, Irina, Miron, Talia, Mirelman, David, Wilchek, Meir, Frolow, Felix·2007·Journal of Molecular Biology
DOI 10.1016/j.jmb.2006.11.041
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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.

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  • Allinase enzyme, composed of pyridoxal phosphate (PLP), splits alliin and produces ammonium, pyruvate, and allyl sulfenic acid, which are highly reactive and unstable at room temperature, and two molecules combine to form allicin.

    “This enzyme composed of pyridoxal phosphate (PLP) which splits alliin and produces ammonium, pyruvate, and allyl sulfenic acid that are highly reactive and unstable at room temperature, where two molecules were combined to form allicin [37,39].”

    From Chemical Constituents and Pharmacological Activities of Garlic (Allium sativum L.): A Review (2020) · cites this paper as [39]

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Authors
Shimon, L. J. W., Rabinkov, A., Shin, I., Miron, T., Mirelman, D., Wilchek, M., & Frolow, F.
Affiliations
  • Weizmann Institute of Science (IL)
  • Tel Aviv University (IL)
Corresponding author
  • Shimon, Linda J.W.
  • Frolow, Felix
ORCID
Shimon, Linda J.W.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2007-02
Volume
366
Issue
2
Pages
611-625
ISSN
0022-2836 (ISSN-L)
DOI
10.1016/j.jmb.2006.11.041
OpenAlex
W1964099296
Cited by
69
References
70
Citations by year
2026: 5 · 2025: 2 · 2024: 2 · 2023: 5 · 2022: 6 · 2021: 6 · 2020: 3 · 2019: 2 · 2017: 1 · 2015: 2 · 2014: 6 · 2013: 2 · 2012: 4
FWCI
3.06
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
European Synchrotron Radiation Facility
Topics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Garlic and Onion Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
alliinase, garlic, ternary complex, apoenzyme structure, N-glycans, hexasaccharide, trisaccharides, active site, alliin, enzyme crystal structure
MeSH terms
Apoenzymes, Binding Sites, Garlic, Glycosylation, Models, Chemical, Models, Molecular, Molecular Sequence Data, Plants, Medicinal, Structure-Activity Relationship, Carbon-Sulfur Lyases, Protein Structure, Tertiary, Dimerization

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