Investigation of the Sulfuryl Transfer Stepfrom Substrate to Enzyme by Arylsulfatases

Authors

S. G. Gibby
J. M. Younker
Alvan C. Hengge, Utah State UniversityFollow

Document Type

Article

Journal/Book Title

Journal of Physical Organic Chemistry

Publication Date

2004

Volume

17

Issue

6

First Page

541

Last Page

547

Abstract

The reactions of the arylsulfatase A (ASA) from Helix pomatia and that from Aerobacter aerogenes with p‐nitrophenyl sulfate were examined by determination of the pH dependence of V_max/K_m and by measurement of kinetic isotope effects. Both enzymes exhibit bell‐shaped pH–rate dependences for V_max/K_m. The ASA from Helix pomatia exhibits a more acidic pH optimum (pH 4–5) than the ASA from Aerobacter aerogenes (pH ∼7). The sulfuryl transfer from substrate to enzyme is general acid‐assisted in both enzymes, but isotope effects indicate differences in the synchronicity of protonation with S^__O bond fission. In the reaction of the Helix pomatia enzyme, protonation is synchronous with bond fission and the leaving group is fully neutralized in the transition state. In the reaction catalyzed by the Aerobacter aerogenes ASA, protonation of the leaving group lags behind bond fission and the leaving group bears a partial negative charge in the transition state. Copyright © 2004 John Wiley & Sons, Ltd.

Recommended Citation

S. G. Gibby, J. M. Younker, and A. C. Hengge “An Investigation of the Sulfuryl Transfer Step from Substrate to Enzyme by Aryl Sulfatases.” Journal of Physical Organic Chemistry, 2004, 17 (6-7), 541-547; invited paper, special issue dedicated to William P. Jencks.