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Chemical Communications

Volumn , Issue 12, 2006, Pages 1298-1300

Enzyme stabilizer DTT catalyzes nitrilase analogue hydrolysis of nitriles

(3) Winkler, Margit a Glieder, Anton a Klempier, Norbert a

a GRAZ UNIVERSITY OF TECHNOLOGY (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

DITHIOTHREITOL; NITRILASE; NITRILE;

ARTICLE; BIOTRANSFORMATION; CATALYSIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; ENZYME MECHANISM; ENZYME RELEASE; ENZYME STABILITY; ENZYME STRUCTURE; PROTEIN HYDROLYSIS; REACTION ANALYSIS; STRUCTURE ANALYSIS;

EID: 33644908013 PISSN: 13597345 EISSN: None Source Type: Journal
DOI: 10.1039/b516937b Document Type: Article

Times cited : (17)

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- -1 (30/70 from 0-2 min, 80/20 from 10-15 min and 30/70 from 15-23 min). The values are calculated from the UV response at 254 nm as area normalization percentage and averaged over 2 to 5 measurements
- -1 (30/70 from 0-2 min, 80/20 from 10-15 min and 30/70 from 15-23 min). The values are calculated from the UV response at 254 nm as area normalization percentage and averaged over 2 to 5 measurements

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- It should be stressed at this point that a radical mechanism cannot be ruled out. Such a mechanism would comprise a single electron transfer from a sulfhydryl-group to the nitrile, which is subsequently quenched by water to give the amide
- It should be stressed at this point that a radical mechanism cannot be ruled out. Such a mechanism would comprise a single electron transfer from a sulfhydryl-group to the nitrile, which is subsequently quenched by water to give the amide

22
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- -1 (5/95 from 0-10 min, 50/50 from 15-20 min and 5/95 from 20-25 min). The values are calculated from the UV response at 225 nm using external calibration and averaged over 2 measurements
- -1 (5/95 from 0-10 min, 50/50 from 15-20 min and 5/95 from 20-25 min). The values are calculated from the UV response at 225 nm using external calibration and averaged over 2 measurements

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- Data not presented
- Data not presented

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