Purification, properties and cellular localization of the stereospecific CS2 secondary alkylsulphohydrolase of Comamonas terrigena.
The availability of homogeneous samples of the potassium salts of L- and D-octan-2-yl sulphate has enabled the separation of the optically stereospecific CS1 and CS2 secondary alkysulphohydrolases from extracts of cells of Comamonas terrigena. The CS2 enzyme was purified to homogeneity, and an initial study was made of its general properties, specificity, cellular localization and relationship to the CS1 enzyme. The CS2 enzyme has a molecular weight of approx. 250000 and a subunit size of approx. 58000, indicating that the molecule is a tetramer. Under the experimental conditions used the enzyme appears to be specific for (+)-secondary alkyl sulphate esters with the sulphate group at C-2 and with a chain length of at least six carbons. Enzyme activity towards racemic C-2 sulphates increases with increasing chain length up to C10, and there is some indirect evidence to suggest that activity declines when that chain length is exceeded. Other indirect evidence confirms that the CS1 enzyme exhibits similar specificity, except that only (-)-isomers can serve as substrates. Both enzymes are present in broth-grown stationary-phase cells of C. terrigena in approximately equal amounts.
D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013237:Stereoisomerism; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013429:Sulfatases / Q000302:isolation & purification / Q000378:metabolism*; D013463:Sulfuric Acid Esters / Q000378:metabolism
D013463:Sulfuric Acid Esters; D013429:Sulfatases