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Improving the Activity and Stability of GL-7-ACA Acylase CA130 by Site-Directed Mutagenesis
In the present study, glutaryl-7-amino cephalosporanic acid acylase from Pseudomonas sp. strain 130 (CA130) was mutated to improve its enzymatic activity and stability. Based on the crystal structure of CA130, two series of amino acid residues, one from those directly involved in catalytic function...
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| Hoofdauteurs: | , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology
2005
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1214626/ https://ncbi.nlm.nih.gov/pubmed/16151116 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.71.9.5290-5296.2005 |
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