水稻蔗糖合成酶催化反應機制與蛋白質結構之探討

黃玉嬌

doi:10.6342/NTU.2015.00909

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水稻蔗糖合成酶催化反應機制與蛋白質結構之探討

Studies on the catalytic mechanism and the structure of rice sucrose synthase

黃玉嬌 , Ph.D　　Advisor：王愛玉　　

繁體中文 DOI： 10.6342/NTU.2015.00909

蔗糖合成酶；反應機制；蛋白質結構；定位點突變；同源模擬； sucrose synthase ； catalytic mechanism ； protein structure ； site-directed mutagenesis ； homology modeling

Abstract │ Reference (119) │ Altmetrics

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Sucrose synthase (SuS, EC 2.4.1.13) catalyzes the reversible conversion of sucrose and UDP into fructose and UDP-glucose. The enzyme is encoded by at least seven RSus genes in rice. The amino acid sequences of different RSuS are highly similar. 
The objective of this study is to elucidate the structure-function relationships of RSuS. The results of substrate binding assay shown that UDP and fructose are the leading substrate of sucrose cleavage and sucrose synthesis direction, respectively. Different approaches including small angle X-ray scattering, protein crystallography and homology modeling, have been attempted to obtain the structure information of RSuS. The theoretical structure of partial RSuS, which was built with the structure of Arabidopsis sucrose synthase 1 as template, revealed that Gln307 and E-X7-E motif of RSuS was involved in fructose binding. Changing the Gln307 to Asn or Ser resulted in completely loss of enzyme activity. Substrate binding assays revealed that the mutant RSuS1(Q307N) retained the capability of fructose binding while RSuS1(Q307S) did not. The E-X7-E motif is conserved in members of glycosyltransferase family 4 (GT4) and other two GT families. The results of enzyme activity assay showed that the mutants E686D and F680Y retained partial enzyme activity and the mutants E678D, E678Q, F680S and E686Q were inactive; however, the tetrameric conformation was maintained in these mutant proteins. The results of substrate binding assays revealed that the mutants E6786D, E686Q, F680S and E686Q could bind UDP but lost the capability of sucrose binding and fructose binding. The kinetic parameters of RSuS3, F680Y and E686D indicated that the residues in E-X7-E motif are important in UDP-glucose binding and enzyme activity.

Reference ( 119 ) 〈TOP〉

Absmanner, B., Schmeiser, V., Kampf, M. and Lehle, L. (2010) Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. Biochem J 426: 205-217.
連結：
Amor, Y., Haigler, C.H., Johnson, S., Wainscott, M. and Delmer, D.P. (1995) A membrane-associated form of sucrose synthase and its potential role in synthesis of cellulose and callose in plants. Proc Natl Acad Sci USA 92: 9353-9357.
連結：
Anguenot, R., Yelle, S. and Nguyen-Quoc, B. (1999) Purification of tomato sucrose synthase phosphorylated isoforms by Fe(III)-immobilized metal affinity chromatography. Arch Biochem Biophys 365: 163-169.
連結：
Baroja-Fernandez, E., Munoz, F.J., Li, J., Bahaji, A., Almagro, G., Montero, M., et al. (2012) Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production. Proc Natl Acad Sci USA 109: 321-326.
連結：
Baroja-Fernandez, E., Munoz, F.J., Montero, M., Etxeberria, E., Sesma, M.T., Ovecka, M., et al. (2009) Enhancing sucrose synthase activity in transgenic potato (Solanum tuberosum L.) tubers results in increased levels of starch, ADPglucose and UDPglucose and total yield. Plant Cell Physiol 50: 1651-1662.
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