5-Aminolevulinic-Acid Synthetase of Rhodopseudomonas spheroides Y. Purification and Some Properties
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چکیده
منابع مشابه
Control of 5-aminolaevulinate synthetase activity in Rhodopseudomonas spheroides.
Rhodopseudomonas spheroides can grow in a defined medium with either light or oxygen as an energy source. Cells grown anaerobically or at very low oxygen tensions are rich in the photosynthetic pigment bacteriochlorophyll, whereas this pigment is virtually absent in cells grown under high oxygen tensions. Aminolaevulinate synthetase, the first enzyme on the pathway to bacteriochlorophyll, appea...
متن کاملA partial reaction of delta-aminolaevulinate synthetase from Rhodopseudomonas spheroides.
microsomal fraction. The properties of the microsomal phosphorylcholinetransferase enzyme are similar to those reported for that from spinach leaves (Devor & Mudd, 1971), except that exogenous diglyceride was necessary for maximal rates, presumably because the activity of endogenous lipases was not high enough to generate a sufficient amount. These results indicate that, whereas the CDP-base pa...
متن کاملControl of 5-aminolaevulinate synthetase activity in Rhodopseudomonas spheroides. Binding of pyridoxal phosphate to 5-aminolaevulinate synthetase.
1. Pyridoxal 5'-phosphate is a cofactor essential for the enzymic activity of aminolaevulinate synthetase from Rhodopseudomonas spheroides. It also aids activation of the low-activity enzyme by trisulphides such as cystine trisulphide, whereas inactivation of enzyme is facilitated by its absence. 2. The fluorescence spectrum of purified high-activity enzyme is that expected for a pyridoxal phos...
متن کاملPurification and properties of solubilized mitochondrial -aminolevulinic acid synthetase and comparison with the cytosol enzyme.
&Aminolevulinic acid synthetase extracted from porphyric liver mitochondria by sonication or freeze-drying was found to be excluded from Sephadex G-ZOO, and other studies revealed that activity was associated with a large aggregate. In contrast, aminoacetone synthetase behaved as a soluble enzyme with a molecular weight of 64,000. By treating the aggregate with both sodium chloride and dithioer...
متن کاملIsolation, purification, and some properties of reduced nicotinamide adenine dinucleotide phosphate-cytochrome C2 reductase from Rhodopseudomonas spheroides.
A method has been described for the isolation and purification of NADPH-cytochrome cZ reductase from light-grown Rhodopseudomonas spheroides. The enzyme is a nonmetalloflavoprotein with flavin adenine dinucleotide as the prosthetic group, and it catalyzes the reduction of R. spheroides cytochrome c2, 2,6dichloroindophenol, and K,Fe(CN), with NADPH as the electron donor. It does not reduce R. sp...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1973
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1973.tb03163.x