Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase.
Deacetoxycephalosporin C synthase from Streptomyces clavuligerus catalyses the conversion of the five-membered penicillin ring to the unsaturated six-membered cephem ring of deacetoxycephalosporin C. The effects on enzyme activity of the penicillin substrate sidechain and various cofactors were inve...
المؤلفون الرئيسيون: | Dubus, A, Lloyd, MD, Lee, H, Schofield, C, Baldwin, J, Frere, J |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2001
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مواد مشابهة
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Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase. The role of arginine 258.
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Active site mutations of recombinant deacetoxycephalosporin C synthase.
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Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase.
حسب: Lloyd, MD, وآخرون
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The effect of cysteine mutations on recombinant deacetoxycephalosporin C synthase from S. clavuligerus.
حسب: Lee, H, وآخرون
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Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS).
حسب: Lee, H, وآخرون
منشور في: (2001)