Investigation of the role of conserved residues Ser13, Asn48 and Pro49 in the catalytic mechanism of the tau class glutathione transferase from Glycine max.
作者： Irene Axarli , Christiana Georgiadou , Prathusha Dhavala , Anastassios C. Papageorgiou , Nikolaos E. Labrou
DOI: 10.1016/J.BBAPAP.2009.10.016
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摘要: Abstract Plant glutathione transferases (GSTs) play a key role in the metabolism of various xenobiotics. In this report, catalytic mechanism tau class GSTU4-4 isoenzyme from Glycine max ( Gm GSTU4-4) was investigated by site-directed mutagenesis and steady-state kinetic analysis. The properties wild-type enzyme three mutants strictly conserved residues (Ser13Ala, Asn48Ala Pro49Ala) were studied 1-chloro-2,4-dinitrobenzene (CDNB) conjugation reaction. results showed that mutations significantly affect substrate binding specificity. effect Ser13Ala mutation on efficiency could be explained assuming direct involvement Ser13 to reaction chemistry correct positioning GSH CDNB ternary complex. Asn48 Pro49 found have structural integrity GSH-binding site (G-site). Moreover, may bring about secondary effects altering thermal stability activity k cat ) without affecting nature rate-limiting step
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