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Arylsulfotransferase from Clostridium innocuum —A new enzyme catalyst for sulfation of phenol‐containing compounds
Author(s) -
Mozhaev Vadim V.,
Khmelnitsky Yuri L.,
SanchezRiera Fernando,
MaurinaBrunker Julie,
Rosson Reinhardt A.,
Grund Alan D.
Publication year - 2002
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10229
Subject(s) - chemistry , sulfation , phenols , phenol , organic chemistry , biocatalysis , solvent , toluene , catalysis , enzyme , substrate (aquarium) , chloroform , methanol , lipase , ether , reaction mechanism , biochemistry , oceanography , geology
Abstract Arylsulfotransferase (AST, EC 2.8.2.22), an enzyme capable of sulfating a wide range of phenol‐containing compounds was purified from a Clostridium innocuum isolate (strain 554). The enzyme has a molecular weight of 320 kDa and is composed of four subunits. Unlike many mammalian and plant arylsulfotransferases, AST from Clostridium utilizes arylsulfates, including p ‐nitrophenyl sulfate, as sulfate donors, and is not reactive with 3‐phosphoadenosine‐5′‐phosphosulfate (PAPS). The enzyme possesses broad substrate specificity and is active with a variety of phenols, quinones and flavonoids, but does not utilize primary and secondary alcohols and sugars as substrates. Arylsulfotransferase tolerates the presence of 10 vol% of polar cosolvents (dimethyl formamide, acetonitrile, methanol), but loses significant activity at higher solvent concentrations of 30–40 vol%. The enzyme retains high arylsulfotransferase activity in biphasic systems composed of water and nonpolar solvents, such as cyclohexane, toluene and chloroform, while in biphasic systems with more polar solvents (ethyl acetate, 2‐pentanone, methyl tert ‐butyl ether, and butyl acetate) the enzyme activity is completely lost. High yields of AST‐catalyzed sulfation were achieved in reactions with several phenols and tyrosine‐containing peptides. Overall, AST studied in this work is a promising biocatalyst in organic synthesis to afford efficient sulfation of phenolic compounds under mild reaction conditions. © 2002 Wiley Periodicals, Inc. Biotechnol Bioeng 78: 567–575, 2002.