| RRC ID |
88931
|
| 著者 |
Nakamichi Y, Shimada N, Watanabe M, Fujii T, Yaoi K, Matsuzawa T.
|
| タイトル |
Structural insights into substrate recognition of tri-modular xyloglucanase from Aspergillus oryzae.
|
| ジャーナル |
J Struct Biol
|
| Abstract |
Xeg5A from Aspergillus oryzae belongs to glycoside hydrolase family 5 subfamily 4. This enzyme has been characterized as a xyloglucan-specific endo-β-1,4-glucanase (xyloglucanase) that cleaves the main chain of xyloglucan at both unbranched and xylosylated glucosyl residues in an endo-processive mode of action. X-ray crystallography revealed that Xeg5A is a tri-modular enzyme composed of a catalytic, an Ig-like, and a C-terminal CBM46-like domains. Xeg5A structures complexed with branched xyloglucan oligosaccharides at subsites -4 to +4 showed that the recognition of xyloglucan side-chain moieties is important for Xeg5A activity. The crystal structure also provided structural insights into the role of the CBM46-like domain in contributing to regiospecificity and, possibly, processivity.
|
| 巻・号 |
217(2)
|
| ページ |
108213
|
| 公開日 |
2025-6-1
|
| DOI |
10.1016/j.jsb.2025.108213
|
| PII |
S1047-8477(25)00048-6
|
| PMID |
40414580
|
| MeSH |
Aspergillus oryzae* / enzymology
Catalytic Domain
Crystallography, X-Ray
Fungal Proteins* / chemistry
Fungal Proteins* / metabolism
Glucans* / chemistry
Glucans* / metabolism
Glycoside Hydrolases* / chemistry
Glycoside Hydrolases* / metabolism
Models, Molecular
Substrate Specificity
Xylans* / chemistry
Xylans* / metabolism
|
| リソース情報 |
| 一般微生物 |
JCM22676 |
