Crystal structure and substrate recognition mechanism of Aspergillus oryzae isoprimeverose-producing enzyme.

Aspergillus oryzae / enzymology Catalytic Domain Crystallography, X-Ray Disaccharides / biosynthesis Glucans / metabolism Glycoside Hydrolases / chemistry Substrate Specificity Xylans / metabolism
Aspergillus oryzae Glycoside hydrolase family 3 Hemicellulose Isoprimeverose Xyloglucan

Journal

Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206

Informations de publication

Date de publication:
01 01 2019
Historique:
received: 14 08 2018
revised: 30 10 2018
accepted: 12 11 2018
pubmed: 18 11 2018
medline: 28 4 2020
entrez: 17 11 2018
Statut: ppublish

Résumé

Isoprimeverose-producing enzymes (IPases) release isoprimeverose (α-d-xylopyranosyl-(1 → 6)-d-glucopyranose) from the non-reducing end of xyloglucan oligosaccharides. Aspergillus oryzae IPase (IpeA) is classified as a member of the glycoside hydrolase family 3 (GH3); however, it has unusual substrate specificity compared with other GH3 enzymes. Xylopyranosyl branching at the non-reducing ends of xyloglucan oligosaccharides is vital for IpeA activity. We solved the crystal structure of IpeA with isoprimeverose at 2.4 Å resolution, showing that the structure of IpeA formed a dimer and was composed of three domains: an N-terminal (β/α)

Identifiants

DOI: 10.1016/j.jsb.2018.11.005 PMID: 30445155
pubmed: 30445155
pii: S1047-8477(18)30288-0
doi: 10.1016/j.jsb.2018.11.005
pii:
doi:

Substances chimiques

Disaccharides 0
Glucans 0
Xylans 0
xyloglucan 37294-28-3
isoprimeverose 534-98-5
Glycoside Hydrolases EC 3.2.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

84-90

Informations de copyright

Copyright © 2018 Elsevier Inc. All rights reserved.

Auteurs

Tomohiko Matsuzawa (T)

Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.

Masahiro Watanabe (M)

Research Institute for Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), 3-11-32, Kagamiyama, HigashiHiroshima, Hiroshima 739-0046, Japan.

Yusuke Nakamichi (Y)

Research Institute for Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), 3-11-32, Kagamiyama, HigashiHiroshima, Hiroshima 739-0046, Japan.

Zui Fujimoto (Z)

Advanced Analysis Center, National Agriculture and Food Research Organization (NARO), 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.

Katsuro Yaoi (K)

Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan. Electronic address: k-yaoi@aist.go.jp.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Champignons › Deuteromycota › Aspergillus › Aspergillus oryzae › Crystal structure and substrate recognition...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Éléments structuraux des protéines › Domaine catalytique › Crystal structure and substrate recognition...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Cristallographie aux rayons X › Crystal structure and substrate recognition...
questionsmedicales.fr › Glucides › Sucres › Diholoside › Crystal structure and substrate recognition...
questionsmedicales.fr › Glucides › Polyosides › Glucanes › Crystal structure and substrate recognition...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Glycosidases › Crystal structure and substrate recognition...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › Crystal structure and substrate recognition...
questionsmedicales.fr › Glucides › Polyosides › Xylanes › Crystal structure and substrate recognition...