HUMAN GLYOXALASE I COMPLEXED WITH S-(N-HYDROXY-N-P-IODOPHENYLCARBAMOYL) GLUTATHIONE

Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue.

AEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDI
PKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGL
AFIQDPDGYWIEILNPNKMATLM

PROTEIN WAS CRYSTALLISED BY EQILLABRATION AGAINST PEG 2000 MONOMETHLY ETHER, 50 MM MES PH 5.8, 0.1M NACL. HIPC-GSH WAS PRESENT IN THE PROTEIN SOLUTION

THE REFERENCE FOR THE SEQUENCE: M.RIDDERSTROM, B.MANNERVIK, BIOCHEM J. 314, 463-467, 1996.

LYASE, LACTOYLGLUTATHIONE LYASE, GLYOXALASE I

HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.

BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.

BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.