PURIFICATION, PROPERTIES AND CELLULAR LOCALIZATION OF STEREOSPECIFIC CS2 SECONDARY ALKYLSULFOHYDROLASE OF COMAMONAS-TERRIGENA
PURIFICATION, PROPERTIES AND CELLULAR LOCALIZATION OF STEREOSPECIFIC CS2 SECONDARY ALKYLSULFOHYDROLASE OF COMAMONAS-TERRIGENA
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DOI：
10.1042/bj1670723
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发表时间：
1977-01-01
影响因子：
4.1
通讯作者：
FITZGERALD, JW
中科院分区：
文献类型：
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作者：
MATCHAM, GWJ;DODGSON, KS;FITZGERALD, JW
L-和d -辛烷-2-酰基硫酸盐钾盐均质样品的可用性使得从terrigena细胞提取物中分离出具有光学立体特异性的CS1和CS2次烷基磺酸水解酶成为可能。将CS2酶纯化至均匀性，初步研究其一般性质、特异性、细胞定位及其与CS1酶的关系。CS2酶的分子量为。apprx。250,000，亚单位大小约为。58000，表明这个分子是一个四聚体。在实验条件下，该酶似乎对C-2上的硫酸盐基团且链长至少为6 c的(+)-硫酸烷基酯具有特异性。酶对外消旋C-2硫酸盐的活性随着链长增加而增加，直至C10，并且有一些间接证据表明，当超过该链长时，活性下降。其他间接证据证实CS1酶具有类似的特异性，除了只有(-)-异构体可以作为底物。这两种酶都存在于肉汤培养的terrigena静止期细胞中，数量大致相等。
The availability of homogeneous samples of the potassium salts of L- and D-octan-2-yl sulfate enabled the separation of the optically stereospecific CS1 and CS2 secondary alkylsulfohydrolases from extracts of cells of C. 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 MW of .apprx. 250,000 and a subunit size of .apprx. 58,000, indicating that the molecule is a tetramer. Under the experimental conditions used the enzyme appears to be specific for (+)-secondary alkyl sulfate esters with the sulfate group at C-2 and with a chain length of at least 6 C. Enzyme activity towards racemic C-2 sulfates 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.