Replacement of the catalytic nucleophile aspartyl residue of dextran glucosidase by cysteine sulfinate enhances transglycosylation activity.
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Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidaseGlycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases.α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.
P2860
Replacement of the catalytic nucleophile aspartyl residue of dextran glucosidase by cysteine sulfinate enhances transglycosylation activity.
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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2013年论文
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name
Replacement of the catalytic n ...... s transglycosylation activity.
@en
Replacement of the catalytic n ...... s transglycosylation activity.
@nl
type
label
Replacement of the catalytic n ...... s transglycosylation activity.
@en
Replacement of the catalytic n ...... s transglycosylation activity.
@nl
prefLabel
Replacement of the catalytic n ...... s transglycosylation activity.
@en
Replacement of the catalytic n ...... s transglycosylation activity.
@nl
P2093
P2860
P356
P1476
Replacement of the catalytic n ...... s transglycosylation activity.
@en
P2093
Atsuo Kimura
Haruhide Mori
Masayuki Okuyama
Momoko Kobayashi
P2860
P304
31670-31677
P356
10.1074/JBC.M113.491449
P407
P577
2013-09-19T00:00:00Z