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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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Библиографические подробности
Опубликовано в::J Bacteriol
Главные авторы: Allam, A M, Hassan, M M, Elzainy, T A
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Microbiology (ASM) 1975
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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