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Crystal Structure and Promiscuous Partitioning of a Covalent Intermediate Common in the Pentein Superfamily
Many enzymes in the pentein superfamily use a transient covalent intermediate in their catalytic mechanisms. Here, we use a mutant (H162G) dimethylarginine dimethylaminohydrolase from Pseudomonas aeruginosa and an alternative substrate, S-methyl-L-thiocitrulline, to trap, crystallize and determine t...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2008
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2601531/ https://ncbi.nlm.nih.gov/pubmed/18482699 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.chembiol.2008.03.012 |
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