PMID: 3753455Jun 1, 1986Paper

Primary alkylsulphatase activities of the detergent-degrading bacterium Pseudomonas C12B. Purification and properties of the P1 enzyme

The Biochemical Journal
T J BatemanG F White

Abstract

The P1 primary alkylsulphatase of Pseudomonas C12B was purified 1500-fold to homogeneity by a combination of streptomycin sulphate precipitation of nucleic acids, (NH4)2SO4 fractionation and chromatography on columns of DEAE-cellulose, Sephacryl S-300 and butyl-agarose. The protein was tetrameric with an Mr of 181000-193000, and exhibited maximum activity at pH 6.1. Primary alkyl sulphates of carbon-chain length C1-C5 or above C14 were not substrates, but the intermediate homologues were shown to be substrates, either by direct assay (C6-C9 and C12) or by gel zymography (C10, C11, C13 and C14). Increasing the chain length from C6 to C12 led to diminishing Km. Values of delta G0' for binding substrates to enzyme were dependent linearly on chain length, indicating high dependence on hydrophobic interactions. Vmax./Km values increased with increasing chain length. Inhibition by alk-2-yl sulphates and alkane-sulphonates was competitive and showed a similar dependence on hydrophobic binding. The P1 enzyme was active towards several aryl sulphates, including o-, m- and p-chlorophenyl sulphates, 2,4-dichlorophenyl sulphate, o-, m- and p-methoxyphenyl sulphates, m- and p-hydroxyphenyl sulphates and p-nitrophenyl sulphate, but excluding...Continue Reading

Citations

Jan 1, 1993·Critical Reviews in Biotechnology·M G RoigJ F Kennedy
May 11, 2006·Proceedings of the National Academy of Sciences of the United States of America·Gregor HageluekenWolf-Dieter Schubert
Feb 15, 2011·Extremophiles : Life Under Extreme Conditions·Mengxian LongXun Xu
Jul 27, 2000·The Journal of Biological Chemistry·A Kahnert, M A Kertesz
Jan 5, 2002·Applied and Environmental Microbiology·Andrew J EllisGraham F White
Feb 1, 1996·Microbiology·Timothy P HigginsJ Colin Murrell

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