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Article

The active-site residue tyr-175 in human glyoxalase II contributes to binding of glutathione derivatives.

Biochimica et biophysica acta - 29 Sept 2000

Ridderström M, Jemth P, Cameron A D, Mannervik B

Abstract excerpt

Tyrosine-175 located in the active site of human glyoxalase II was replaced by phenylalanine in order to study the contribution of this residue to catalysis. The mutation had a marginal effect on the k(cat) value determined using S-D-lactoylglutathione as substrate. However, the Y175F mutant had an 8-fold higher K(m) value than the wild-type enzyme. The competitive inhibitor...

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PMID: 11018726
DOI: 10.1016/s0167-4838(00)00178-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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