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The Catalytic Intermediate Stabilized by a “Down” Active Site Loop for Diaminopimelate Decarboxylase from Helicobacter pylori: ENZYMATIC CHARACTERIZATION WITH CRYSTAL STRUCTURE ANALYSIS
The meso-diaminopimelate decarboxylase (DAPDC, EC 4.1.1.20) catalyzes the final step of l-lysine biosynthesis in bacteria and is regarded as a target for the discovery of antibiotics. Here we report the 2.3Å crystal structure of DAPDC from Helicobacter pylori (HpDAPDC). The structure, in which the p...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Biochemistry and Molecular Biology
2008
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3258949/ https://ncbi.nlm.nih.gov/pubmed/18508763 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M801823200 |
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