Formation and cleavage of 2-keto-3-deoxygluconate by 2-keto-3-deoxygluconate aldolase of Aspergillus niger.
2-Keto-3-deoxygluconate aldolase of Aspergillus niger, an enzyme that has not been reported previously, was purified 468-fold. Maximal activity was obtained at pH 8.0 and 50 C. The enzyme exhibited relative stereochemical specificity with respect to glyceraldehyde. The Km values for 2-keto-3-deoxygl...
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| Опубликовано в:: | J Bacteriol |
|---|---|
| Главные авторы: | , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Microbiology (ASM)
1975
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC236016/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/358/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.124.3.1128-1131.1975 |
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