Evidence for essential histidine and dicarboxylic amino-acid residues in the active site of UDP-glucose : solasodine glucosyltransferase from eggplant leaves.

• Authors: Paulina Nawłoka , Małgorzata Kalinowska , Cezary Pączkowski , Zdzisław A Wojciechowski
• Languages of publication: EN

Abstracts

EN

Effects of several chemical probes selectively modifying various amino-acid residues on the activity of UDP-glucose : solasodine glucosyltransferase from eggplant leaves was studied. It was shown that diethylpyrocarbonate (DEPC), a specific modifier of histidine residues, was strongly inhibitory. However, in the presence of excessive amounts of the enzyme substrates, i.e. either UDP-glucose or solasodine, the inhibitory effect of DEPC was much weaker indicating that histidine (or histidines) are present in the active site of the enzyme. Our results suggest also that unmodified residues of glutamic (or aspartic) acid, lysine, cysteine, tyrosine and tryptophan are necessary for full activity of the enzyme. Reagents modifying serine and arginine residues have no effect on the enzyme activity.

Keywords

EN

solasodine; Solanum melongena; active site; glucosyltransferase; glycoalkaloids

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2003
• Volume: 50
• Issue: 2
• Pages: 567-572

Dates

published

2003

accepted

2002-06-02

received

2003-04-08

revised

2003-05-27

Contributors

author

Paulina Nawłoka

• Institute of Biochemistry, Warsaw University, Warszawa, Poland

author

Małgorzata Kalinowska

• Institute of Biochemistry, Warsaw University, Warszawa, Poland

author

Cezary Pączkowski

• Institute of Biochemistry, Warsaw University, Warszawa, Poland

author

Zdzisław A Wojciechowski

• Institute of Biochemistry, Warsaw University, Warszawa, Poland

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