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KINETIC-STUDIES OF THE POLYGALACTURONASE ENZYME FROM COLLETOTRICHUM-LINDEMUTHIANUM

WAKSMAN, G; TURNER, G; WALMSLEY, AR; (1992) KINETIC-STUDIES OF THE POLYGALACTURONASE ENZYME FROM COLLETOTRICHUM-LINDEMUTHIANUM. BIOCHEM J , 285 551 - 556.

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Abstract

The intrinsic protein fluorescence of the polygalacturonase from Colletotrichium lindemuthianum was exploited in stopped-flow experiments aimed at elucidating the kinetic mechanism for this enzyme. Binding of the polymeric substrate polygalacturonic acid (PGA) essentially produced a triphasic fluorescence profile. There was an initial rapid quench in fluorescence, consistent with the rapid formation of the enzyme-substrate complex, with an equilibrium constant of about 8 x 10(-4)% (w/v) PGA (about 0.27-mu-M). There then followed a near-constant fluorescence phase, attributable to turnover of the enzyme-substrate complex as a steady-state intermediate. As the concentration of the steady-state intermediate became depleted, towards the end of the reaction, there was a partial return of the fluorescence intensity. This phase is attributed to a final, single turnover of the enzyme at the end of the reaction. The fluorescence intensity does not return to its original level due to product remaining bound at the end of the reaction.

Type: Article
Title: KINETIC-STUDIES OF THE POLYGALACTURONASE ENZYME FROM COLLETOTRICHUM-LINDEMUTHIANUM
Keywords: ASPERGILLUS-NIDULANS, GENE, ENDOPOLYGALACTURONASES, TRANSFORMATION, FUNGI, NIGER
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/73818
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