Structural insights into the substrate specificity and activity of a novel mannose 2-epimerase from Runella slithyformis.

Mannose / metabolism Racemases and Epimerases Substrate Specificity Carbohydrate Epimerases / chemistry
Runella slithyformis crystal structure enzyme mechanism mannose 2-epimerase substrate specificity

Journal

Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043

Informations de publication

Date de publication:
01 Jul 2023
Historique:
received: 01 12 2022
accepted: 02 05 2023
medline: 30 6 2023
pubmed: 14 6 2023
entrez: 14 6 2023
Statut: ppublish

Résumé

Mannose 2-epimerase (ME), a member of the acylglucosamine 2-epimerase (AGE) superfamily that catalyzes epimerization of D-mannose and D-glucose, has recently been characterized to have potential for D-mannose production. However, the substrate-recognition and catalytic mechanism of ME remains unknown. In this study, structures of Runella slithyformis ME (RsME) and its D254A mutant [RsME(D254A)] were determined in their apo forms and as intermediate-analog complexes [RsME-D-glucitol and RsME(D254A)-D-glucitol]. RsME possesses the (α/α)

Identifiants

DOI: 10.1107/S205979832300390X PMID: 37314406
pubmed: 37314406
pii: S205979832300390X
doi: 10.1107/S205979832300390X
doi:

Substances chimiques

Mannose PHA4727WTP
Racemases and Epimerases EC 5.1.-
Carbohydrate Epimerases EC 5.1.3.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

585-595

Subventions

Organisme : Japan Society for the Promotion of Science
ID : 18K05382
Organisme : Japan Society for the Promotion of Science
ID : 21K05388
Organisme : Japan Society for the Promotion of Science
ID : 21H01754
Organisme : Japan Agency for Medical Research and Development
ID : JP18am0101071 (0058)
Organisme : Japan Agency for Medical Research and Development
ID : JP19am0101083

Auteurs

Hang Wang (H)

Faculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo 060-0810, Japan.
ORCID: 0000-0001-7706-0536

Xiaomei Sun (X)

Faculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo 060-0810, Japan.

Wataru Saburi (W)

Research Faculty of Agriculture, Hokkaido University, Kita 9, Nishi 9, Kita-ku, Sapporo 060-8589, Japan.
ORCID: 0000-0002-2015-7086

Saki Hashiguchi (S)

Research Faculty of Agriculture, Hokkaido University, Kita 9, Nishi 9, Kita-ku, Sapporo 060-8589, Japan.

Jian Yu (J)

Faculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo 060-0810, Japan.

Toyoyuki Ose (T)

Faculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo 060-0810, Japan.

Haruhide Mori (H)

Research Faculty of Agriculture, Hokkaido University, Kita 9, Nishi 9, Kita-ku, Sapporo 060-8589, Japan.

Min Yao (M)

Faculty of Advanced Life Science, Hokkaido University, Kita 10, Nishi 8, Kita-ku, Sapporo 060-0810, Japan.
ORCID: 0000-0003-1687-5904

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Classifications MeSH

questionsmedicales.fr › Glucides › Sucres › Oses › Hexose › Mannose › Structural insights into the substrate...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Racémases et épimérases › Structural insights into the substrate...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › Structural insights into the substrate...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Racémases et épimérases › Carbohydrate epimerases › Structural insights into the substrate...