TY - JOUR
T1 - Direct demonstration by 1H N.M.R. spectrometry of the stereoselectivity of yeast glyoxalase I towards the diastereomeric forms of the α-ketoaldehyde-glutathione hemithioacetal
AU - Brown, Charles
AU - Douglas, Kenneth T.
AU - Ghobt-Sharif, J.
PY - 1981
Y1 - 1981
N2 - Addition of yeast glyoxalase I at pD 4.4 leads to selective disappearance of one of the diastereotopic methine proton signals of the phenylglyoxal- glutathione hemithioacetal, the diastereomer with the lower field signal reacting preferentially with the enzyme, which directly establishes asymmetric binding of the hemithioacetal carbon region as the origin of the stereospecificity of the glyoxalase I reaction to form (S)-D-mandeloyl- glutathione.
AB - Addition of yeast glyoxalase I at pD 4.4 leads to selective disappearance of one of the diastereotopic methine proton signals of the phenylglyoxal- glutathione hemithioacetal, the diastereomer with the lower field signal reacting preferentially with the enzyme, which directly establishes asymmetric binding of the hemithioacetal carbon region as the origin of the stereospecificity of the glyoxalase I reaction to form (S)-D-mandeloyl- glutathione.
UR - http://www.scopus.com/inward/record.url?scp=37049095604&partnerID=8YFLogxK
U2 - 10.1039/C39810000944
DO - 10.1039/C39810000944
M3 - Article
AN - SCOPUS:37049095604
SN - 0022-4936
SP - 944
EP - 946
JO - Journal of the Chemical Society, Chemical Communications
JF - Journal of the Chemical Society, Chemical Communications
IS - 18
ER -