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The eukaryotic enzyme Bds1 is an alkyl but not an aryl sulfohydrolase.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2017 Sep 16; Vol. 491 (2), pp. 382-387. Date of Electronic Publication: 2017 Jul 15. - Publication Year :
- 2017
-
Abstract
- The eukaryotic enzyme Bds1 in Saccharomyces cerevisiae is a metallo-β-lactamase-related enzyme evolutionarily originating from bacterial horizontal gene transfer that serves an unknown biological role. Previously, Bds1 was reported to be an alkyl and aryl sulfatase. However, we demonstrate here that Bds1 acts on primary alkyl sulfates (of 6-12 carbon atoms) but not the aryl sulfates p-nitrophenyl sulfate and p-nitrocatechol sulfate. The apparent catalytic rate constant for hydrolysis of the substrate 1-hexyl sulfate by Bds1 is over 100 times lower than that of the reaction catalyzed by its bacterial homolog SdsA1. We show that Bds1 shares a catalytic mechanism with SdsA1 in which the carbon atom of the sulfate ester is the subject of nucleophilic attack, rather than the sulfur atom, resulting in C-O bond lysis. In contrast to SdsA1 and another bacterial homolog with selectivity for secondary alkyl sulfates named Pisa1, Bds1 does not show any substantial activity towards secondary alkyl sulfates. Neither Bds1 nor SdsA1 have any significant activity towards a branched primary alkyl sulfate, primary and secondary steroid sulfates, or phosphate diesters. Therefore, the enzymes homologous to SdsA1 that have been identified and characterized thus far vary in their selectivity towards primary and secondary alkyl sulfates but do not exhibit aryl sulfatase activity.<br /> (Copyright © 2017 Elsevier Inc. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Biocatalysis
Cloning, Molecular
Escherichia coli genetics
Gene Expression
Gene Transfer, Horizontal
Kinetics
Recombinant Proteins genetics
Recombinant Proteins metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae Proteins genetics
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Sulfatases genetics
beta-Lactamases genetics
Escherichia coli enzymology
Saccharomyces cerevisiae enzymology
Saccharomyces cerevisiae Proteins metabolism
Sulfatases metabolism
Sulfuric Acid Esters metabolism
beta-Lactamases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 491
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 28720494
- Full Text :
- https://doi.org/10.1016/j.bbrc.2017.07.092