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An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles

Nitrilase from Rhodococcus rhodochrous ATCC 33278 hydrolyses both aliphatic and aromatic nitriles. Replacing Tyr-142 in the wild-type enzyme with the aromatic amino acid phenylalanine did not alter specificity for either substrate. However, the mutants containing non-polar aliphatic amino acids (ala...

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Detaylı Bibliyografya
Asıl Yazarlar: Yeom, Soo-Jin, Kim, Hye-Jung, Lee, Jung-Kul, Kim, Dong-Eun, Oh, Deok-Kun
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Portland Press Ltd. 2008
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2570083/
https://ncbi.nlm.nih.gov/pubmed/18412544
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20080440
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