The effect of cysteine mutations on recombinant deacetoxycephalosporin C synthase from S. clavuligerus.
Cysteines 100, 155, and 197 of recombinant deacetoxycephalosporin C synthase were mutated to alanine residues. The C100A mutant had properties similar to those of the wild-type enzyme, but mutation of Cys-155 and Cys-197 reduced enzyme activity with penicillin N and penicillin G to different extents...
المؤلفون الرئيسيون: | Lee, H, Lloyd, MD, Harlos, K, Schofield, C |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2000
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مواد مشابهة
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Active site mutations of recombinant deacetoxycephalosporin C synthase.
حسب: Lee, H, وآخرون
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Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS).
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Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase.
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Studies on the active site of deacetoxycephalosporin C synthase.
حسب: Lloyd, MD, وآخرون
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Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase. The role of arginine 258.
حسب: Lee, H, وآخرون
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