Reaction of COTC with Glutathione: Structure of the Putative Glyoxalase I Inhibitor
- 14 September 2000
- journal article
- letter
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 2 (20) , 3143-3144
- https://doi.org/10.1021/ol006341z
Abstract
The structure of the active glyoxalase I inhibitor derived from the Streptomyces griseosporeus metabolite COTC 1 has been conclusively identified by means of total synthesis as 2c. Human glyoxalase I is competitively inhibited by 2c (Ki = 183 ± 6 μM) but is not inhibited by 1 itself.Keywords
This publication has 7 references indexed in Scilit:
- Reaction Mechanism of Glyoxalase I Explored by an X-ray Crystallographic Analysis of the Human Enzyme in Complex with a Transition State AnalogueBiochemistry, 1999
- Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy.Journal of Biological Chemistry, 1992
- Synthesis of glycosyl phosphonates and related compoundsHeteroatom Chemistry, 1991
- Enantioselective total synthesis of Glyoxalase I inhibitor using asymmetric Diels-Alder reaction of a new chiral dienophile, ()S-3-(3-triflouromethylpyrid-2-ylsulfinyl)acrylate.Tetrahedron Letters, 1986
- Synthesis of a Glyoxalase I Inhibitor from Streptomyces griseosporeus NIIDAet OGASAWARAHelvetica Chimica Acta, 1985
- A glyoxalase I inhibitor of a new structural type produced by Streptomyces.The Journal of Antibiotics, 1975
- [205] Thiol-disulfide transhydrogenase (Yeast)Published by Elsevier ,1971