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Volumn 14, Issue 5, 2002, Pages 1033-1052

Structural basis for broad substrate specificity in higher plant β-D-glucan glucohydrolases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; HYDROGEN BONDS; SUBSTRATES; X RAY CRYSTALLOGRAPHY;

EID: 0036016436     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.010442     Document Type: Article
Times cited : (88)

References (77)
  • 7
    • 0000230693 scopus 로고
    • Host-pathogen interactions. XVI. Purification and characterization of a glucosyl hydrolase/transferase present in the walls of soybean cells
    • (1981) Plant Physiol. , vol.68 , pp. 207-220
    • Cline, K.1    Albersheim, P.2
  • 10
    • 0032125968 scopus 로고    scopus 로고
    • A xyloglucan oligosacchadde-active, transglycosylating β-D-glucosidase from the cotyledons of nasturtium (Tropaeolum majus L) seedlings: Purification, properties and characterization of a cDNA clone
    • (1998) Plant J , vol.15 , pp. 27-38
    • Crombie, H.J.1    Chengappa, S.2    Hellyer, A.3    Reid, J.S.G.4
  • 19
    • 0031972297 scopus 로고    scopus 로고
    • Plant α-glucosidases of the glycoside hydrolase family 31: Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
    • (1998) Plant Mol. Biol. , vol.37 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 23
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 24
    • 0014943898 scopus 로고
    • Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions: Evaluation of subsite affinities of exo-enzyme
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1-6
    • Hiromi, K.1
  • 25
    • 0027439791 scopus 로고
    • Purification and properties of three (1→3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • (1993) Biochem. J. , vol.289 , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 28
    • 0029039918 scopus 로고
    • Subsite affinities and disposition of catalytic amino acids in the substrate-binding region of barley 1,3-β-D-glucanases: Implications in plant-pathogen interactions
    • (1995) J. Biol. Chem. , vol.270 , pp. 14556-14563
    • Hrmova, M.1    Garrett, T.P.J.2    Fincher, G.B.3
  • 48
    • 0030694040 scopus 로고    scopus 로고
    • Mechanism of Bacillus 1,3:1,4-β-D-glucan 4-glucanohydrolases: Kinetic and pH studies with 4-methylumbelliferyl β-D-oligosaccharides
    • (1997) Biochemistry , vol.36 , pp. 13838-13848
    • Malet, C.1    Planas, A.2
  • 49
    • 0032573586 scopus 로고    scopus 로고
    • From β-glucanase to β-glucansynthase: Glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile
    • (1998) FEBS Lett , vol.440 , pp. 208-212
    • Malet, C.1    Planas, A.2
  • 51
    • 0028971418 scopus 로고
    • Mechanism of Agrobacterium β-glucosidase: Kinetic analysis of the role of noncovalent enzyme/substrate interactions
    • (1995) Biochemistry , vol.34 , pp. 16194-16202
    • Namchuk, M.N.1    Withers, S.G.2
  • 59
    • 0023774901 scopus 로고
    • EZ-FIT: A practical curve-fitting microcomputer program for the analysis of the enzyme kinetic data on IBM-PC compatible computers
    • (1988) Anal. Biochem. , vol.174 , pp. 437-447
    • Perella, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.