Essential role of a family-32 carbohydrate-binding module in substrate recognition by Clostridium thermocellum mannanase CtMan5A
• An essential role of a CBM in substrate recognition by mannanase CtMan5A is reported. • A catalytic domain and a CBM collectively form a substrate-binding site. • The CBM directly participates in substrate recognition for catalytic action. • CtMan5A and its derivative without the CBM yielded diffe...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Mizutani, Kimiya [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Umfang: |
5 |
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| Übergeordnetes Werk: |
Enthalten in: Mitigating the environmental impacts of milk production via anaerobic digestion of manure: Case study of a dairy farm in the Po Valley - Battini, F. ELSEVIER, 2014, for the rapid publication of short reports in biochemistry, biophysics, and molecular biology, Chichester |
|---|---|
| Übergeordnetes Werk: |
volume:588 ; year:2014 ; number:9 ; day:2 ; month:05 ; pages:1726-1730 ; extent:5 |
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| DOI / URN: |
10.1016/j.febslet.2014.03.022 |
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Essential role of a family-32 carbohydrate-binding module in substrate recognition by Clostridium thermocellum mannanase CtMan5A |
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• An essential role of a CBM in substrate recognition by mannanase CtMan5A is reported. • A catalytic domain and a CBM collectively form a substrate-binding site. • The CBM directly participates in substrate recognition for catalytic action. • CtMan5A and its derivative without the CBM yielded different hydrolysis products. • Substrate binding modes of CtMan5A and the truncated derivative are different. |
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• An essential role of a CBM in substrate recognition by mannanase CtMan5A is reported. • A catalytic domain and a CBM collectively form a substrate-binding site. • The CBM directly participates in substrate recognition for catalytic action. • CtMan5A and its derivative without the CBM yielded different hydrolysis products. • Substrate binding modes of CtMan5A and the truncated derivative are different. |
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• An essential role of a CBM in substrate recognition by mannanase CtMan5A is reported. • A catalytic domain and a CBM collectively form a substrate-binding site. • The CBM directly participates in substrate recognition for catalytic action. • CtMan5A and its derivative without the CBM yielded different hydrolysis products. • Substrate binding modes of CtMan5A and the truncated derivative are different. |
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