Functional identification of the 4-deoxy-L-erythro-5-hexoseulose uronate reductase from a brown alga, Saccharina japonica.


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
19 03 2021
Historique:
received: 10 12 2020
accepted: 25 01 2021
pubmed: 7 2 2021
medline: 11 5 2021
entrez: 6 2 2021
Statut: ppublish

Résumé

We previously reported the alginate lyase, SjAly, from a brown alga, Saccharina japonica, providing the first experimental evidence for a functional alginate-degradation enzyme in brown algae. 4-deoxy-L-erythro-5-hexoseulose uronate (DEHU), derived from an unsaturated monosaccharide, was identified as the minimum degradation product produced by SjAly-mediated lysis of alginate. DEHU was hitherto reported to be reduced to 2-keto-3-deoxy-gluconate (KDG) by a DEHU-specific reductase with NAD(P)H in alginate-assimilating organisms and its metabolism in alginate-producing organisms is unknown. Here, we report the functional identification of a DEHU reductase, SjRed, in S. japonica. Among the 14 tested compounds, only DEHU was used as a substrate and was converted to KDG in the presence of NADPH. Optimum temperature, pH, and KCl concentration required for SjRed activity were determined to be 25 °C, 7.2, and 100 mM, respectively. SjRed consists of 341 amino acid residues and is proposed to be a member of the aldo-keto reductase superfamily. Sequencing of SjRed revealed that it is composed of at least three exons. These results indicate the existence of an enzyme that reduces DEHU to KDG in S. japonica. This is the first report on the functional identification of a DEHU-reductase in alginate-producing organisms.

Identifiants

pubmed: 33548623
pii: S0006-291X(21)00155-8
doi: 10.1016/j.bbrc.2021.01.090
pii:
doi:

Substances chimiques

Algal Proteins 0
Alginates 0
Deoxy Sugars 0
Hexuronic Acids 0
Recombinant Proteins 0
Aldo-Keto Reductases EC 1.1.1.-
Polysaccharide-Lyases EC 4.2.2.-
poly(beta-D-mannuronate) lyase EC 4.2.2.3

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

112-118

Informations de copyright

Copyright © 2021 Elsevier Inc. All rights reserved.

Auteurs

Akira Inoue (A)

Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, 041-8611, Japan. Electronic address: inouea21@fish.hokudai.ac.jp.

Takao Ojima (T)

Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, 041-8611, Japan.

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Classifications MeSH