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Literature DB >> 6123317

The slow kinetic transients of arylsulphatase A.

C O'Fagain, U Bond, B A Orsi, T J Mantle.

Abstract

A simple model is described to account for the anomalous time course of arylsulphatase A. In the case of the ox liver and human placental enzymes the enzyme-nitrocatechol sulphate complex can, in addition to forming products, slowly break down to form an inactive species which can turn in slowly regenerate active enzyme. When the inactive form binds sulphate the rate of reactivation is enhanced, 218-fold in the case of the ox enzyme. Rat liver arylsulphatase A is refractory to reactivation by sulphate.

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Year: 1982 PMID： 6123317 PMCID： PMC1163649 DOI： 10.1042/bj2010345

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

21 in total

1. Uridine diphospho-N-acetylgalactosamine-4-sulfate sulfohydrolase activity of human arylsulfatase B and its deficiency in the Maroteaux-Lamy syndrome.

Authors: A L Fluharty; R L Stevens; D Fung; S Peak; H Kihara
Journal: Biochem Biophys Res Commun Date: 1975-01-02 Impact factor: 3.575

10. beta-elimination of beta-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction.

Authors: T S Soper; J M Manning
Journal: Biochemistry Date: 1978-08-08 Impact factor: 3.162

3 in total

The slow kinetic transients of arylsulphatase A.

1. Uridine diphospho-N-acetylgalactosamine-4-sulfate sulfohydrolase activity of human arylsulfatase B and its deficiency in the Maroteaux-Lamy syndrome.

2. The sulphatase of ox liver. XIX. On the nature of the polymeric forms of sulphatase A present in dilute solutions.

3. Suicide substrates for the alanine racemase of Escherichia coli B.

4. The determination of the initial velocity of enzyme-catalysed reactions.

5. Problems associated with the assay of arylsulphatases A and B of rat tissues.

6. Kinetic properties of the arylsulphatase A from human kidneys.

7. Kinetic properties of arylsulphatase A--theoretical treatment.

8. The sulphatase of ox liver. XI. The isoelectric focussing of a purified preparation of sulphatase B.

9. Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept.

10. beta-elimination of beta-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction.

1. The kinetics of substrate-induced inactivation.

Review 2. The anomalous kinetics of sulphatase A.

3. The effect of pH on the kinetics of arylsulphatases A and B.