Bacterial glyoxalase I enzymes: structural and biochemical investigations-Reference-Cited by-同舟云学术

Bacterial glyoxalase I enzymes: structural and biochemical investigations

Published:2014-03-20 Issue:2 Volume:42 Page:479-484
ISSN:0300-5127
Container-title:Biochemical Society Transactions
language:en
Short-container-title:

Author:

Honek John F.¹

Affiliation:

1. Department of Chemistry, University of Waterloo, 200 University Avenue West, Waterloo, Ontario, Canada, N2L 3G1

Abstract

A number of bacterial glyoxalase I enzymes are maximally activated by Ni2+ and Co2+ ions, but are inactive in the presence of Zn2+, yet these enzymes will also bind this metal ion. The structure–activity relationships between these two classes of glyoxalase I serve as important clues as to how the molecular structures of these proteins control metal-activation profiles.

Publisher

Portland Press Ltd.

Subject

Biochemistry

Link

https://portlandpress.com/biochemsoctrans/article-pdf/42/2/479/487006/bst0420479.pdf

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