메뉴 건너뛰기




Volumn 133, Issue 2, 2003, Pages 253-258

Kinetic studies on the hydrolysis of N-acetylated and N-deacetylated derivatives of 4-methylumbelliferyl chitobioside by the family 18 chitinases ChiA and ChiB from Serratia marcescens

Author keywords

Chitinase; Fluorogenic chitobioside; Serratia marcescens; Steady state kinetics

Indexed keywords

4 METHYLUMBELLIFERYL CHITOBIOSIDE; CHITIN DERIVATIVE; CHITINASE; CHITINASE CHIA; CHITINASE CHIB; UNCLASSIFIED DRUG;

EID: 0037302229     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg031     Document Type: Article
Times cited : (19)

References (24)
  • 1
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Bairoch, A. (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316, 695-696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 2
    • 0001616015 scopus 로고
    • Comparative biochemistry of chitinase-Anomeric form of the reaction products
    • Fukamizo, T., Daizo, K., and Goto, S. (1995) Comparative biochemistry of chitinase-Anomeric form of the reaction products. Biosci. Biotechnol. Biochem. 59, 311-313
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 311-313
    • Fukamizo, T.1    Daizo, K.2    Goto, S.3
  • 4
    • 0035644196 scopus 로고    scopus 로고
    • Dissection of nucleophilic and acid-base catalysis in glycosidases
    • Zechel, D.L. and Withers, S.G. (2001) Dissection of nucleophilic and acid-base catalysis in glycosidases. Curr. Opin. Chem. Biol. 5, 643-649
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 643-649
    • Zechel, D.L.1    Withers, S.G.2
  • 5
    • 0033974048 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Asp280 suggests substrate-assisted catalysis of chitinase A1 from Bacillus circulans WL-12
    • Hashimoto, M., Honda, Y., Nikaidou, N., Fukamizo, T., and Watanabe, T. (2000) Site-directed mutagenesis of Asp280 suggests substrate-assisted catalysis of chitinase A1 from Bacillus circulans WL-12. J. Biosci. Bioeng. 89, 100-102
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 100-102
    • Hashimoto, M.1    Honda, Y.2    Nikaidou, N.3    Fukamizo, T.4    Watanabe, T.5
  • 6
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • Terwisscha van Scheltinga, A.C., Armand, S., Kalk, K.H., Isogai, A., Henrissat, B., and Dijkstra, B.W. (1995) Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry 34, 15619-15623
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 8
    • 0029947945 scopus 로고    scopus 로고
    • NAG-thiazoline, An N-Acetyl-β-hexosaminidase inhibitor that implicates acetamido participation
    • Knapp, S., Vocadlo, D., Gao, Z., Kirk, B., Lou, J., and Withers, S.G. (1996) NAG-thiazoline, An N-Acetyl- β-hexosaminidase inhibitor that implicates acetamido participation. J. Am. Chem. Soc. 118, 6804-6805
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6804-6805
    • Knapp, S.1    Vocadlo, D.2    Gao, Z.3    Kirk, B.4    Lou, J.5    Withers, S.G.6
  • 10
    • 0029270304 scopus 로고
    • The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan
    • Mitsutomi, M., Kidoh, H., Tomita, H., and Watanabe, T. (1995) The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan. Biosci. Biotechnol. Biochem. 59, 529-531
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 529-531
    • Mitsutomi, M.1    Kidoh, H.2    Tomita, H.3    Watanabe, T.4
  • 11
    • 0025407307 scopus 로고
    • Action pattern of Aeromonas hydrophila chitinase on partially N-acetylated chitosan
    • Mitsutomi, M., Ohtakara, A., Fukamizo, T., and Goto, S. (1990) Action pattern of Aeromonas hydrophila chitinase on partially N-acetylated chitosan. Agric. Biol. Chem. 54, 871-877
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 871-877
    • Mitsutomi, M.1    Ohtakara, A.2    Fukamizo, T.3    Goto, S.4
  • 12
    • 0025656279 scopus 로고
    • Action pattern of Streptomyces griseus chitinase on partially N-acetylated chitosan
    • Ohtakara, A., Matsunaga, H., and Mitsutomi, M. (1990) Action pattern of Streptomyces griseus chitinase on partially N-acetylated chitosan. Agric. Biol. Chem. 54, 3191-3199
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 3191-3199
    • Ohtakara, A.1    Matsunaga, H.2    Mitsutomi, M.3
  • 13
    • 0034678642 scopus 로고    scopus 로고
    • Chemo- and enzymatic synthesis of partially and fully N-deacetylated 4- methy-lumbelliferyl chitobiosides: Fluorogenic substrates for chitinase
    • Honda, Y., Tanimori, S., Kirihata, M., Kaneko, S., Tokuyasu, K., Hashimoto, M., and Watanabe, T. (2000) Chemo- and enzymatic synthesis of partially and fully N-deacetylated 4-methy-lumbelliferyl chitobiosides: fluorogenic substrates for chitinase. Bioorg. Med. Chem. Lett. 10, 827-829
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 827-829
    • Honda, Y.1    Tanimori, S.2    Kirihata, M.3    Kaneko, S.4    Tokuyasu, K.5    Hashimoto, M.6    Watanabe, T.7
  • 14
    • 0034617366 scopus 로고    scopus 로고
    • Kinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N-deacetylated 4-methylumbelliferyl chitobiosides
    • Honda, Y., Tanimori, S., Kirihata, M., Kaneko, S., Tokuyasu, K., Hashimoto, M., Watanabe, T., and Fukamizo, T. (2000) Kinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N-deacetylated 4-methylumbelliferyl chitobiosides. FEBS Lett. 476, 194-197
    • (2000) FEBS Lett. , vol.476 , pp. 194-197
    • Honda, Y.1    Tanimori, S.2    Kirihata, M.3    Kaneko, S.4    Tokuyasu, K.5    Hashimoto, M.6    Watanabe, T.7    Fukamizo, T.8
  • 15
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis
    • Papanikolau, Y., Prag, G., Tavlas, G., Vorgias, C.E., Oppenheim, A.B., and Petratos, K. (2001) High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry 40, 11338-11343
    • (2001) Biochemistry , vol.40 , pp. 11338-11343
    • Papanikolau, Y.1    Prag, G.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6
  • 18
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 19
    • 0035957051 scopus 로고    scopus 로고
    • Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis
    • Fukamizo, T., Sasaki, C., Schelp, E., Bortone, K., and Robertus, J.D. (2001) Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis. Biochemistry 40, 2448-2454
    • (2001) Biochemistry , vol.40 , pp. 2448-2454
    • Fukamizo, T.1    Sasaki, C.2    Schelp, E.3    Bortone, K.4    Robertus, J.D.5
  • 20
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases A and B from Serratia marcescens
    • Brurberg, M.B., Nes, I.F., and Eijsink, V.G. (1996) Comparative studies of chitinases A and B from Serratia marcescens. Microbiology 142, 1581-1589
    • (1996) Microbiology , vol.142 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.3
  • 21
    • 0026637250 scopus 로고
    • Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase
    • Kitaoka, M., Sasaki, T., and Taniguchi, H. (1992) Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase. J. Biochem. (Tokyo) 112, 40-44
    • (1992) J. Biochem. (Tokyo) , vol.112 , pp. 40-44
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 22
    • 0021799919 scopus 로고
    • On porcine pancreatic α-amylase action: Kinetic evidence for the binding of two maltooligosaccharide molecules (maltose, maltotriose and o-nitrophenylmaltoside) by inhibition studies. Correlation with the five-subsite energy profile
    • Seigner, C., Prodanov, E., and Marchis-Mouren, G. (1985) On porcine pancreatic α-amylase action: kinetic evidence for the binding of two maltooligosaccharide molecules (maltose, maltotriose and o-nitrophenylmaltoside) by inhibition studies. Correlation with the five-subsite energy profile. Eur. J. Biochem. 148, 161-168
    • (1985) Eur. J. Biochem. , vol.148 , pp. 161-168
    • Seigner, C.1    Prodanov, E.2    Marchis-Mouren, G.3
  • 23
    • 0030694040 scopus 로고    scopus 로고
    • Mechanism of Bacillus 1, 3-1, 4-β-D-glucan 4-glucanohydrolases: Kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides
    • Malet, C. and Planas, A. (1997) Mechanism of Bacillus 1, 3-1, 4-β-D-glucan 4-glucanohydrolases: kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides. Biochemistry 36, 13838-13848
    • (1997) Biochemistry , vol.36 , pp. 13838-13848
    • Malet, C.1    Planas, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.