Conserved Cys residue influences catalytic properties of potato endo-[1-3]-beta-glucanase GLUB20-2

• Autorzy: Witek A. I. , Witek K. , Hennig J.
• Języki publikacji: EN

Abstrakty

EN

The synthesis and degradation of (1->3)-β-glycosidic bonds between glucose moieties are essential metabolic processes in plant cell architecture and function. We have found that a unique, conserved cysteine residue, positioned outside the catalytic centre of potato endo-(1->3)-β-glucanase — product of the gluB20-2 gene, participates in determining the substrate specificity of the enzyme. The same residue is largely responsible for endo-(1->3)-β-glucanase inhibition by mercury ions. Our results confirm that the spatial adjustment between an enzyme and its substrate is one of the essential factors contributing to the specificity and accuracy of enzymatic reactions.

Słowa kluczowe

EN

[1-3]-beta-glucanase; gluB20-2 gene; catalytic property; substrate specificity; inhibition; structure-function relationship; potato; Solanum tuberosum; plant cell; cellular function; enzymatic reaction

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2008
• Tom: 55
• Numer: 4
• Opis fizyczny: p.791-797,fig.,ref.

Twórcy

autor

Witek A. I.

• Institute of Biochemistry and Biophysics Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland

autor

Witek K.

autor

Hennig J.

Bibliografia

• Barabasz A (2005) Functional analysis of the 1,3-β-glucanase, product of gluB20-2 gene in potato. Ph.D. Thesis, Institute of Biochemistry and Biophysics PAS, Warsaw (in Polish).
• Barone LM, He Mu H, Shih CJ, Kashlan KB, Wasserman BP (1998) Distinct biochemical and topological properties of the 31- and 27-kilodalton plasma membrane intrinsic protein subgroups from red beet. Plant Physiol 118:315-322.
• Chen L, Garrett TPJ, Fincher GB, Hoj PB (1995) A tetrad of ionizable amino acids is important for catalysis in barley β-glucanases. J Biol Chem 270:8093-8101.
• Cobbett C, Goldsbrough P (2002) Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis. Annu Rev Plant Biol 53:159-182.
• Cornish-Bowden A (2004) Fundamentals of Enzyme Kinetics. Portland Press, London.
• Davies G, Henrissat B (1995) Structure and mechanisms of glycosyl hydrolases. Structure 3:853-859.
• DeLano WL (2002) The PyMOL molecular graphics system. DeLano Scientific, Palo Alto, CA.
• Denault LJ, Allen WG, Boyer EW, Collins D, Kramme D, Spradlin JE (1978) A simple reducing sugar assay for measuring β-glucanase activity in malt, and various microbial enzyme preparations. J Am Soc Brew Chem 36:18-23.
• Dixon M, Webb EC (1964) Enzymes. Longman Group Ltd., London.
• Felix G, Meins F Jr (1985) Purification, immunoassay and characterization of an abundant, cytokinin-regulated polypeptide in cultured tobacco tissues. Planta 164:423-428.
• Henrissat B, Davies GJ (2000) Glycoside hydrolases and glycosyltransferases. Families, modules, and implications for genomics. Plant Physiol 124:1515-1519.
• Ho SN, Hunt HD, Horton M, Pullen JK, Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
• Hoj PB, Fincher GB (1995) Molecular evolution of plant β-glucan endohydrolases. Plant J 7: 367-379.
• Hoj PB, Slade AM, Wettenhall REH, Fincher GB (1988) Isolation and characterization of a (1-->3)-β-glucan endohydrolase from germinating barley (Hordeum vulgare): amino acid sequence similarity with barley (1-->3, 1-->4)-β-glucanases. FEBS Lett 230:67-71.
• Hrmova M, Fincher GB (2001) Structure-function relationships of β-d-glucan endo- and exohydrolases from higher plants. Plant Mol Biol 47:73-91.
• Hrmova M, Imai T, Rutten SJ, Fairweather JK, Pelosi L, Bulone V, Drigues H, Fincher GB (2002) Mutated barley (1-->3)-β-d-glucan endohydrolases synthesize crystalline (1-->3)-β-d-glucans. J Biol Chem 277:30102-30111.
• Koshland DE (1958) Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA 44:98-104.
• Lever M (1972) A new reaction for colorimetric determination of carbohydrates. Anal Biochem 47:273-279.
• MacGregor JT, Clarkson TW (1974) Distribution, tissue binding and toxicity of mercurials. In Protein-metal interactions, Friedman M, ed, pp 463-503. Plenum Press, New York.
• Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-428.
• Moore AE, Stone BA (1972) A β-1,3-glucan hydrolase from Nicotiana glutinosa II. Specificity, action pattern and inhibitor studies. Biochim Biophys Acta 258:248-264.
• Preston GM, Jung JS, Guggino WB, Agre P (1993) The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J Biol Chem 268:17-20.
• Receveur-Brechot V, Czjzek M, Barre A, Roussel A, Peumans WJ, Van Damme EJ, Rouge P (2006) Crystal structure at 1.45-A resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome. Proteins 63:235-242.
• Sambrook JE, Fritsch F, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
• Sorensen I, Pettolino FA, Wilson SM, Doblin MS, Johansen B, Bacic A, Willats WGT (2008) Mixed-linkage (1-->3),(1-->4)-β-d-glucan is not unique to the Poales and is abundant component of Equisetum arvensecell walls. Plant J 54:510-521.
• Stone BA, Clarke AE (1992) Chemistry and biology of (1-->3)-β-glucans. La Trobe University Press, Victoria.
• Varghese JN, Garrett TPJ, Colman, PM, Chen L, Hoj PB, Fincher GB (1994) Three-dimensional structures of two plant β-glucan endohydrolases with distinct substrate specificities. Proc Natl Acad Sci USA 91:2785-2789.
• Wong Y, Maclachlan GA (1979) 1,3-β-d-Glucanases from Pisum sativum seedlings. II. Substrate specificities and enzymic action patterns. Biochim Biophys Acta 571:256-269.
• Yamamoto M, Ezure T, Watanabe T, Tanaka H, Aono R (1998) C-Terminal domain of β-1,3-glucanase H in Bacillus circulans IAM1165 has a role in binding to insoluble β-1,3-glucan. FEBS Lett 433:41-43