An efficient arabinoxylan-debranching α-L-arabinofuranosidase of family GH62 from Aspergillus nidulans contains a secondary carbohydrate binding site.
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Structure of the Catalytic Domain of α-L-Arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, Provides Insights into Structure-Function Relationships in Glycoside Hydrolase Family 62Using Carbohydrate Interaction Assays to Reveal Novel Binding Sites in Carbohydrate Active Enzymes.Two Distinct α-l-Arabinofuranosidases in Caldicellulosiruptor Species Drive Degradation of Arabinose-Based Polysaccharides.Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.
P2860
An efficient arabinoxylan-debranching α-L-arabinofuranosidase of family GH62 from Aspergillus nidulans contains a secondary carbohydrate binding site.
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2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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name
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@en
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@nl
type
label
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@en
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@nl
prefLabel
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@en
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@nl
P2093
P2860
P50
P1476
An efficient arabinoxylan-debr ...... ary carbohydrate binding site.
@en
P2093
Barry McCleary
Bent O Petersen
Darrell Cockburn
Hiroyuki Nakai
Johnny Birch
Maher Abou Hachem
Ole Hindsgaul
Paul Dupree
Susan Andersen
P2860
P2888
P304
P356
10.1007/S00253-016-7417-8
P407
P577
2016-03-05T00:00:00Z