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Volumn 377, Issue 1, 2004, Pages 225-232

Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: Identification of family 36 glycosyltransferase in Vibrio

Author keywords

Cellobiose phosphorylase; Chitobiose phosphorylase; Glycosyltransferase family 36; Phosphorolytic reaction; Synthetic reaction; Vibrio

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; CLONING; GENES;

EID: 1642494584     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031171     Document Type: Article
Times cited : (46)

References (31)
  • 1
    • 0031749615 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of cellobiose phosphorylase gene from Cellvibrio gilvus
    • Liu, A., Tomita, H., Li, H., Miyaki, H., Aoyagi, C., Kaneko, S. and Hayashi, K. (1998) Cloning, sequencing and expression of cellobiose phosphorylase gene from Cellvibrio gilvus. J. Ferment. Bioeng. 85, 511-513
    • (1998) J. Ferment. Bioeng. , vol.85 , pp. 511-513
    • Liu, A.1    Tomita, H.2    Li, H.3    Miyaki, H.4    Aoyagi, C.5    Kaneko, S.6    Hayashi, K.7
  • 2
    • 0036685627 scopus 로고    scopus 로고
    • Kinetic studies of a recombinant cellobiose phosphorylase (CBP) of the Clostridium thermocellum YM4 strain expressed in Escherichia coli
    • Tokyo
    • Kim, Y. K., Kitaoka, M., Krishnareddy, M., Mori, Y. and Hayashi, K. (2002) Kinetic studies of a recombinant cellobiose phosphorylase (CBP) of the Clostridium thermocellum YM4 strain expressed in Escherichia coli. J. Biochem. (Tokyo) 132, 197-203
    • (2002) J. Biochem. , vol.132 , pp. 197-203
    • Kim, Y.K.1    Kitaoka, M.2    Krishnareddy, M.3    Mori, Y.4    Hayashi, K.5
  • 3
    • 0042201948 scopus 로고    scopus 로고
    • Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8
    • Rajashekhara, E., Kitaoka, M., Kim, Y. K. and Hayashi, K. (2002) Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8. Biosci. Biotechnol. Biochem. 66, 2578-2586
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2578-2586
    • Rajashekhara, E.1    Kitaoka, M.2    Kim, Y.K.3    Hayashi, K.4
  • 4
    • 0010018536 scopus 로고    scopus 로고
    • Cellodextrin phosphorylase from Clostridium thermocellum YM4 strain expressed in Escherichia coli
    • Krishnareddy, M., Kim, Y. K., Kitaoka, M., Mori, Y. and Hayashi, K. (2002) Cellodextrin phosphorylase from Clostridium thermocellum YM4 strain expressed in Escherichia coli. J. Appl. Glycosci. 49, 1-8
    • (2002) J. Appl. Glycosci. , vol.49 , pp. 1-8
    • Krishnareddy, M.1    Kim, Y.K.2    Kitaoka, M.3    Mori, Y.4    Hayashi, K.5
  • 5
    • 0001547692 scopus 로고    scopus 로고
    • Chitin catabolism in the marine bacterium Vibrio furnissil. Identification, molecular cloning, and characterization of a N, N′-diacetylchitobiose phosphorylase
    • Park, J. K., Keyhani, N. O. and Roseman, S. (2000) Chitin catabolism in the marine bacterium Vibrio furnissil. Identification, molecular cloning, and characterization of a N, N′-diacetylchitobiose phosphorylase. J. Biol. Chem. 275, 33077-33083
    • (2000) J. Biol. Chem. , vol.275 , pp. 33077-33083
    • Park, J.K.1    Keyhani, N.O.2    Roseman, S.3
  • 6
  • 9
    • 0034664940 scopus 로고    scopus 로고
    • Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus
    • Zhang, Z. Z., Nirasawa, S., Nakajima, Y., Yoshida, M. and Hayashi, K. (2000) Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus. Biochem. J. 350, 671-676
    • (2000) Biochem. J. , vol.350 , pp. 671-676
    • Zhang, Z.Z.1    Nirasawa, S.2    Nakajima, Y.3    Yoshida, M.4    Hayashi, K.5
  • 10
    • 0000642542 scopus 로고
    • A facile synthesis of 2-methyl-(3,4,6-tri-0-acetyl-1,2-dideoxy-α-D- glucopyrano)-[2,1-d]-2-oxazoline
    • Srivastava, V. K. (1982) A facile synthesis of 2-methyl-(3,4,6-tri-0- acetyl-1,2-dideoxy-α-D-glucopyrano)-[2,1-d]-2-oxazoline. Carbohydr. Res. 103, 286-292
    • (1982) Carbohydr. Res. , vol.103 , pp. 286-292
    • Srivastava, V.K.1
  • 12
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu, Y. G. and Whittier, R. F. (1995) Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25, 674-681
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 13
    • 0029360727 scopus 로고
    • Efficient isolation and mapping of Arabidopsis thaliana T-DNA insert junctions by thermal asymmetric interlaced PCR
    • Liu, Y. G., Mitsukawa, N., Oosumi, T. and Whittier, R. F. (1995) Efficient isolation and mapping of Arabidopsis thaliana T-DNA insert junctions by thermal asymmetric interlaced PCR. Plant J. 8, 457-463
    • (1995) Plant J. , vol.8 , pp. 457-463
    • Liu, Y.G.1    Mitsukawa, N.2    Oosumi, T.3    Whittier, R.F.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 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
  • 16
    • 0000807711 scopus 로고
    • The determination of inorganic phosphate in the presence of labile phosphate esters
    • Lowry, O. H. and Lopez, J. A. (1946) The determination of inorganic phosphate in the presence of labile phosphate esters. J. Biol. Chem. 162, 421-428
    • (1946) J. Biol. Chem. , vol.162 , pp. 421-428
    • Lowry, O.H.1    Lopez, J.A.2
  • 17
    • 0033810985 scopus 로고    scopus 로고
    • Cloning and characterization of the glucooligosaccharide catabolic pathway β-glucan glucohydrolase and cellobiose phosphorylase in the marine hyperthermophile Thermotoga neapolitana
    • Yernool, D. A., McCarthy, J. K., Eveleigh, D. E. and Bok, J. D. (2000) Cloning and characterization of the glucooligosaccharide catabolic pathway β-glucan glucohydrolase and cellobiose phosphorylase in the marine hyperthermophile Thermotoga neapolitana. J. Bacteriol. 182, 5172-5179
    • (2000) J. Bacteriol. , vol.182 , pp. 5172-5179
    • Yernool, D.A.1    McCarthy, J.K.2    Eveleigh, D.E.3    Bok, J.D.4
  • 19
    • 0030609809 scopus 로고    scopus 로고
    • Purification and properties of a cellobiose phosphorylase (CepA) and a cellodextrin phosphorylase (CepB) from the cellulolytic thermophile Clostridium stercorarium
    • Reichenbecher, M., Lottspeich, F. and Bronnenmeier, K. (1997) Purification and properties of a cellobiose phosphorylase (CepA) and a cellodextrin phosphorylase (CepB) from the cellulolytic thermophile Clostridium stercorarium. Eur. J. Biochem. 247, 262-267
    • (1997) Eur. J. Biochem. , vol.247 , pp. 262-267
    • Reichenbecher, M.1    Lottspeich, F.2    Bronnenmeier, K.3
  • 20
    • 0028931975 scopus 로고
    • Purification and properties of cellobiose phosphorylase from Clostridium thermocellum
    • Tanaka, K., Kawaguchi, T., Imada, Y., Ooi, T. and Arai, M. (1995) Purification and properties of cellobiose phosphorylase from Clostridium thermocellum. J. Ferment. Bioeng. 79, 212-216
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 212-216
    • Tanaka, K.1    Kawaguchi, T.2    Imada, Y.3    Ooi, T.4    Arai, M.5
  • 21
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. Biochim. Biophys. Acta 67, 104-137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 23
    • 0020532570 scopus 로고
    • Purification and properties of Cellvibrio gilvus cellobiose phosphorylase
    • Sasaki, T., Tanaka, T., Nakagawa, S. and Kainuma, K. (1983) Purification and properties of Cellvibrio gilvus cellobiose phosphorylase. Biochem. J. 209, 803-807
    • (1983) Biochem. J. , vol.209 , pp. 803-807
    • Sasaki, T.1    Tanaka, T.2    Nakagawa, S.3    Kainuma, K.4
  • 24
    • 0014409336 scopus 로고
    • Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum
    • Alexander, J. K. (1968) Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum. J. Biol. Chem. 243, 2899-2904
    • (1968) J. Biol. Chem. , vol.243 , pp. 2899-2904
    • Alexander, J.K.1
  • 25
    • 0001599359 scopus 로고
    • Phosphorolysis and synthesis of cellobiose by cell extracts from Ruminococcus flavefaciens
    • Ayers, W. A. (1959) Phosphorolysis and synthesis of cellobiose by cell extracts from Ruminococcus flavefaciens. J. Biol. Chem. 234, 2819-2822
    • (1959) J. Biol. Chem. , vol.234 , pp. 2819-2822
    • Ayers, W.A.1
  • 26
    • 0001117576 scopus 로고
    • Cellobiose phosphorylase (EC 2.4.1.20) of Cellulomonas: Occurrence, induction, and its role in cellobiose metabolism
    • Schimz, K. L., Broll, B. and Jhon, B. (1983) Cellobiose phosphorylase (EC 2.4.1.20) of Cellulomonas: occurrence, induction, and its role in cellobiose metabolism. Arch. Microbiol. 135, 241-249
    • (1983) Arch. Microbiol. , vol.135 , pp. 241-249
    • Schimz, K.L.1    Broll, B.2    Jhon, B.3
  • 27
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase
    • Mark, B. L., Vocadlo, D. J., Knapp, S., Triggs-Raine, B. L., Withers, S. G. and James, M. N. (2001) Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase. J. Biol. Chem. 276, 10330-10337
    • (2001) J. Biol. Chem. , vol.276 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 28
    • 0000613964 scopus 로고
    • Phosphorolytic reaction of Cellvibrio gilvus cellobiose phosphorylase
    • Kitaoka, M., Sasaki, T. and Taniguchi, H. (1992) Phosphorolytic reaction of Cellvibrio gilvus cellobiose phosphorylase. Biosci. Biotechnol. Biochem. 56, 652-655
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 652-655
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 29
    • 0034329594 scopus 로고    scopus 로고
    • Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda
    • Nidetzky, B., Eis, C. and Albert, M. (2000) Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda. Biochem. J. 351, 649-659
    • (2000) Biochem. J. , vol.351 , pp. 649-659
    • Nidetzky, B.1    Eis, C.2    Albert, M.3
  • 30
    • 0026637250 scopus 로고
    • Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase
    • Tokyo
    • Kitaoka, M., Sasaki, T. and Taniguchi, H. (1992) Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase. J. Biochem. (Tokyo) 112, 40-44
    • (1992) J. Biochem. , vol.112 , pp. 40-44
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 31
    • 0027222134 scopus 로고
    • Purification and properties of laminaribiose phosphorylase (EC 2.4 1.31) from Euglena gracilis Z
    • Kitaoka, M., Sasaki, T. and Taniguchi, H. (1993) Purification and properties of laminaribiose phosphorylase (EC 2.4 1.31) from Euglena gracilis Z. Arch. Biochem. Biophys. 304, 508-514
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 508-514
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3


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