Sulfate-activating Enzymes of Penicillium chrysogenum
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چکیده
منابع مشابه
Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile).
ATP sulfurylases from Penicillium chrysogenum (a mesophile) and from Penicillium duponti (a thermophile) had a native molecular weight of about 440,000 and a subunit molecular weight of about 69,000. (The P. duponti subunit appeared to be a little smaller than the P. chrysogenum subunit.) The P. duponti enzyme was about 100 times more heat stable than the P. chrysogenum enzyme; k inact (the fir...
متن کاملSulfate utilization by penicillin-producing mutants of Penicillium chrysogenum.
A great deal of work has been directed toward increasing the yield of penicillin in fermentations with Penicillium chrysogenum. The spectacular increase in yield which has been achieved has resulted, in the main, from two approaches. In the first approach, mutant strains of P. chrysogenum produced by spontaneous variation or by the action of mutagenic agents such as nitrogen mustard or ultravio...
متن کاملAccumulation of intracellular inorganic sulfate by Penicillium chrysogenum.
The cell membranes of microorganisms appear to be rather complex, metabolically active entities, equipped with many specific active transport mechanisms which mediate the uptake and accumulation of a variety of compounds. Bacteria have been shown to accumulate amino acids (Cohen and Rickenberg, 1956; Gale, 1947; 1953), carbohydrates (Cohen and Monod, 1957; Rickenberg et al., 1956), and inorgani...
متن کاملPenicillin acyltransferase in Penicillium chrysogenum.
Isotopic exchange of (35)S between penicillins and 6-amino-penicillanic acid (6-APA) was observed in cell-free extracts of Penicillium chrysogenum. Sulfhydryl-containing compounds were required for activity. Dithiothreitol, dithioerythritol, mercaptoethanol, and glutathione served as activators. The acyltransferase was purified threefold by adsorption on calcium phosphate gel at pH 6 and elutio...
متن کاملThe lactic dehydrogenase of Penicillium chrysogenum.
A soluble, cytochrome linked flavoprotein which oxidizes lactic acid to pyruvic acid has been isolated from Penicillium chrysogenum, strain NRRL 1951 -B25. The reduction of cytochrome c by a flavin enzyme has precedence in the work of Horecker and Heppel (1949) and Mlorell (1952) who have shown that xanthine oxidase can reduce cytochrome c. Morell reported the enzyme to be inhibited strongly by...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)60550-2