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, appears to play an important role in the control of bacteriochlorophyll synthesis. Thus, the enzyme has a high activity in extracts of pigmented cells and a low activity in extracts of non-pigmented cells. Further, oxygenation of a pigmented culture causes immediate cessation of pigment synthesis and produces a rapid fall in the activity of aminolaevulinate synthetase. This loss of activity appears to be due to the loss of an endogenous activator of the enzyme. Thus, pigmented cells contain cystine trisulphide, which at muM concentrations is an activator of aminolaevulinate synthetase, while oxygenation causes a rapid fall in the cellular content of this trisulphide. Cystathionase (EC 4.2.1.15) extracted from pigmented cells can catalyse the formation of cystine trisulphide from cystine, while rhodanese (EC 2.8.1.1) extracted from the same cells can catalyse the degradation of cystine trisulphide in the presence of sulphite to form cystine and thiosulphate. It is proposed that the cellular content of cystine trisulphide is controlled by changes in the levels of substrates for cystathionase and possibly rhodanese rather than changes in the amounts of these enzymes. Cystine trisulphide controls the activity of aminolaevulinate synthetase by converting a low-activity form of the enzyme (b-form) into a high-activity form (a-form). The fall in aminolaevulinate synthetase activity on oxygenation appears to be the result of cessation of conversion of b-form into a-form, along with a conversion of a-form into b-form. Factors affecting the equilibrium between the forms and the possible mechanisms for their interconversion are discussed.
D000624:5-Aminolevulinate Synthetase / Q000378:metabolism*; D001429:Bacteriochlorophylls / Q000096:biosynthesis; D013437:Carbon-Sulfur Lyases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003553:Cystine / Q000031:analogs & derivatives / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism*; D008027:Light; D008190:Lyases / Q000378:metabolism*; D010100:Oxygen; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D013440:Sulfides / Q000378:metabolism; D013466:Sulfurtransferases / Q000378:metabolism*; D013884:Thiosulfate Sulfurtransferase / Q000378:metabolism*
D001429:Bacteriochlorophylls; D007527:Isoenzymes; D013440:Sulfides; D003553:Cystine; D000624:5-Aminolevulinate Synthetase; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase; D008190:Lyases; D013437:Carbon-Sulfur Lyases; D010100:Oxygen