Studies on the Arylsulphatase and phenol sulphotransferase activities of Aspergillus oryzae

Author:

Burns G R J.1,Wynn C H1

Affiliation:

1. Department of Biological Chemistry, University of Manchester, Manchester M13 9PL, U.K.

Abstract

1. Crude extracts of Aspergillus oryzae grown under conditions of sulphur limitation possess high arylsulphatase activity. 2. This activity can be greatly enhanced by the inclusion of tyramine or a number of other phenols in the assay medium. 3. The arylsulphatase activity of these extracts can be resolved into three distinct fractions by chromatography on DEAE-cellulose. 4. The effect of tyramine is restricted to one of these fractions only. 5. Evidence is presented which indicates that this effect is the consequence of a phenol sulphotransferase activity, which shows no requirement for 3'-phosphoadenosine 5'-phosphate as a cofactor, and which will not transfer sulphate from 3'-phosphoadenosine 5'-sulphatophosphate to potential phenolic acceptors. 6. The three enzymes differ also in their molecular weights and substrate specificities.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 27 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Microbial Sulfatases;Moscow University Chemistry Bulletin;2018-07

2. Enrichment of Cheeses Manufactured from Cow's and Sheep's Milk Blends with Sheep-like Species-Related Alkylphenols;Journal of Agricultural and Food Chemistry;2005-02-05

3. The stereochemical course of sulphuryl transfer catalysed by arylsulphatase II from Aspergillus oryzae;Biochemical Journal;1992-11-01

4. Mechanisms of sulphate activation and transfer;Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences;1991-05-29

5. Partial characterization of the steroidsulfatases in Peptococcus niger H4;Applied and Environmental Microbiology;1991-01

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