Ferrous Ion-Dependent l -Serine Dehydratase from Clostridium acidiurici
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چکیده
منابع مشابه
Phosphotransacetylase from Clostridium acidiurici.
The phosphotransacetylase from Clostridium acidiurici has two properties not observed for this enzyme in other bacteria: (i) it requires a divalent metal for activity, and (ii) it is not subject to uncoupling by arsenate. The enzyme has been obtained in highly purified form, with a specific activity 500-fold higher than crude extracts. Ferrous or manganous ions are required for maximal activity...
متن کاملA novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae.
YGL196W of Saccharomyces cerevisiae encodes a putative protein that is unidentified but is predicted to have a motif similar to that of the N-terminal domain of the bacterial alanine racemase. In the present study we found that YGL196W encodes a novel D-serine dehydratase, which belongs to a different protein family from that of the known bacterial enzyme. The yeast D-serine dehydratase purifie...
متن کاملRegulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat.
1. The activities of l-serine dehydratase and l-serine-pyruvate aminotransferase were determined in rat liver during foetal and neonatal development. 2. l-Serine-pyruvate aminotransferase activity begins to develop in late-foetal liver, increases rapidly at birth to a peak during suckling and then decreases at weaning to the adult value. 3. l-Serine dehydratase activity is very low prenatally, ...
متن کاملL-serine specific dehydrase from Clostridium acidi-urici.
Formation of serine and pyruvate as intermediates in uric acid fermentation by Clostridium acidi-urici was suggested by Radin and Barker (1953), Sagers and Beck (1956), and Rabinowitz and B3arker (1956) to account for the labeling of acetate formed from C14-labele(d purines, and from the ability of cell suspensions and extracts to deaminate serine to pyruvate and ammonia. The present communicat...
متن کاملInduction of L-serine dehydratase in Aeromonas punctata.
L-Serine dehydratase (SD) was produced to the extent of only 0·04 international unit (iu) per mg dry weight by Aeromollas pUllctata NRRL B-928 when grown on a chemically defined medium. Addition of 2% (w/v) L-serine to this medium increased SD ten-fold or more, indicating a significant inductive effect. o-Serine was toxic to the organism, making weights and enzyme titres uncertain, but DL-serin...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1972
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.109.2.757-763.1972