Purification and characterization of 3-deoxy-D-manno-octulosonate 8-phosphate synthetase from Escherichia coli.
3-Deoxy-D-manno-octulosonate (KDO)-8-phosphate synthetase has been purified 450-fold from frozen Escherichia coli B cells. The purified enzyme catalyzed the stoichiometric formation of KDO-8-phosphate and Pi from phosphoenolpyruvate (PEP) and D-arabinose-5-phosphate. The enzyme showed no metal requi...
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| Udgivet i: | J Bacteriol |
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| Hovedforfatter: | |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Microbiology (ASM)
1980
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC293669/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6988389/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.141.2.635-644.1980 |
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