메뉴 건너뛰기




Volumn 21, Issue 4, 2011, Pages 503-511

Elucidation of exo-βd-glucosaminidase activity of a family 9 glycoside hydrolase (PBPRA0520) from Photobacterium profundum SS9

Author keywords

chitin; exo d glucosaminidase; GH family 9; Photobacterium; Vibrio

Indexed keywords

4 NITROPHENOL; 4 NITROPHENYL BETA DEXTRO GLUCOSAMINIDE; 9 GLYCOSIDE HYDROLASE; CELLOBIOSE; CHITOBIOSE; EXO BETA DEXTRO GLUCOSAMINIDASE; GLUCOSAMINE DERIVATIVE; GLUCOSAMINIDASE; HYDROLASE; UNCLASSIFIED DRUG;

EID: 79952551796     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwq191     Document Type: Article
Times cited : (12)

References (40)
  • 2
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • DOI 10.1002/prot.1168
    • Bates PA, Kelley LA, MacCallum RM, Sternberg MJ. 2001. Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAWand 3D-PSSM. Proteins Suppl. 5:39-46. (Pubitemid 34113166)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 5
    • 33645010330 scopus 로고    scopus 로고
    • Two exo-p-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases
    • Cote N, Fleury A, Dumont-Blanchette E, Fukamizo T, Mitsutomi M, Brzezinski R. 2006. Two exo-p-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem J. 394:675-686.
    • (2006) Biochem J , vol.394 , pp. 675-686
    • Cote, N.1    Fleury, A.2    Dumont-Blanchette, E.3    Fukamizo, T.4    Mitsutomi, M.5    Brzezinski, R.6
  • 6
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases [1]
    • Davies GJ, Wilson KS, Henrissat B. 1997. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J. 321:557-559. (Pubitemid 27056509)
    • (1997) Biochemical Journal , vol.321 , Issue.2 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 9
    • 1642494584 scopus 로고    scopus 로고
    • Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: Identification of family 36 glycosyltransferase in Vibrio
    • DOI 10.1042/BJ20031171
    • Honda Y, Kitaoka M, Hayashi K 2004. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: Identification offamily 36 glyco-syltransferase in Vibrio. Biochem J. 377:225-232. (Pubitemid 38114449)
    • (2004) Biochemical Journal , vol.377 , Issue.1 , pp. 225-232
    • Honda, Y.1    Kitaoka, M.2    Hayashi, K.3
  • 10
  • 11
    • 33748996180 scopus 로고    scopus 로고
    • Cloning and heterologous expression of the exo-β-D-glucosaminidase- encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7
    • DOI 10.1007/s00253-006-0320-y
    • Ike M, Isami K, Tanabe Y, Nogawa M, Ogasawara W, Okada H, Morikawa Y 2006. Cloning and heterologous expression of the exo-p-D-glucosamini-dase- encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7. Appl Microbiol Biotechnol. 72:687-695. (Pubitemid 44454928)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.4 , pp. 687-695
    • Ike, M.1    Isami, K.2    Tanabe, Y.3    Nogawa, M.4    Ogasawara, W.5    Okada, H.6    Morikawa, Y.7
  • 12
    • 19544381690 scopus 로고
    • Simple activity measurement of lysozyme
    • Imoto T, Yagishita K. 1971. Simple activity measurement of lysozyme. Agric BiolChem. 35:1154-1156.
    • (1971) Agric BiolChem , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 13
    • 0032714186 scopus 로고    scopus 로고
    • Physiological aspects of chitin catabolism in marine bacteria
    • Keyhani NO, Roseman S. 1999. Physiological aspects of chitin catabolism in marine bacteria. Biochim Biophys Acta. 1473:108-122.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 108-122
    • Keyhani, N.O.1    Roseman, S.2
  • 14
    • 0030478209 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Characterization of an N, A-diacetyl-chitobiose transport system
    • Keyhani NO, Wang LX, Lee YC, Roseman S. 1996. The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Characterization of an N, A-diacetyl-chitobiose transport system. J Biol Chem. 271:33409-33413.
    • (1996) J Biol Chem , vol.271 , pp. 33409-33413
    • Keyhani, N.O.1    Wang, L.X.2    Lee, Y.C.3    Roseman, S.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0345743697 scopus 로고    scopus 로고
    • The chitinolytic cascade in Vibrios is regulated by chitin oligosaccharides and a two-component chitin catabolic sensor/kinase
    • DOI 10.1073/pnas.0307645100
    • Li X, Roseman S. 2004. The chitinolytic cascade in Vibrios is regulated by chitin oligosaccharides and a two-component chitin catabolic sensor/ kinase. Proc Natl Acad Sci USA. 101:627-631. (Pubitemid 38084687)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.2 , pp. 627-631
    • Li, X.1    Roseman, S.2
  • 18
    • 65449187856 scopus 로고    scopus 로고
    • Expression, purification, and characterization of exo-p-D-glucosaminidase of Aspergillus sp. CJ22-326 from Escherichia coli
    • Li S, Wang C, Xia W. 2009. Expression, purification, and characterization of exo-p-D-glucosaminidase of Aspergillus sp. CJ22-326 from Escherichia coli. Carbohydr Res. 344:1046-1049.
    • (2009) Carbohydr Res , vol.344 , pp. 1046-1049
    • Li, S.1    Wang, C.2    Xia, W.3
  • 19
    • 33748582281 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a thermostable exo-β-D-glucosaminidase from the hyperthermophilic archaeon Pyrococcus horikoshii
    • DOI 10.1007/s10529-006-9137-0
    • Liu B, Li Z, Hong Y, Ni J, Sheng D, Shen Y 2006. Cloning, expression and characterization of a thermostable exo-p-D-glucosaminidase from the hyperthermophilic archaeon Pyrococcus horikoshii. Biotechnol Lett. 28:1655-1660. (Pubitemid 44369329)
    • (2006) Biotechnology Letters , vol.28 , Issue.20 , pp. 1655-1660
    • Liu, B.1    Li, Z.2    Hong, Y.3    Ni, J.4    Sheng, D.5    Shen, Y.6
  • 21
    • 0037478772 scopus 로고    scopus 로고
    • X-ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides
    • DOI 10.1128/JB.185.14.4127-4135.2003
    • Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R. 2003. X-ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides. JBacteriol. 185:4127-4135. (Pubitemid 36835252)
    • (2003) Journal of Bacteriology , vol.185 , Issue.14 , pp. 4127-4135
    • Mandelman, D.1    Belaich, A.2    Belaich, J.P.3    Aghajari, N.4    Driguez, H.5    Haser, R.6
  • 23
    • 0025329913 scopus 로고
    • Purification and characterization of an exo-p-D-glucosaminidase, a novel type of enzyme, from Nocardia orientals
    • Nanjo F, Katsumi R, Sakai K. 1990. Purification and characterization of an exo-p-D-glucosaminidase, a novel type of enzyme, from Nocardia orientals. J Biol Chem. 265:10088-10094.
    • (1990) J Biol Chem , vol.265 , pp. 10088-10094
    • Nanjo, F.1    Katsumi, R.2    Sakai, K.3
  • 24
    • 0000674033 scopus 로고
    • A photometric adaptation of the somogyi method for the determination of glucose
    • Nelson N. 1944. A photometric adaptation of the somogyi method for the determination of glucose. J Biol Chem. 153:375-380.
    • (1944) J Biol Chem , vol.153 , pp. 375-380
    • Nelson, N.1
  • 25
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, 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
  • 26
    • 0001547692 scopus 로고    scopus 로고
    • Chitin catabolism in the marine bacterium Vibrio furnissii: Identification, molecular cloning, and characterization of a W^V'-diacetylchitobiose phosphorylase
    • Park JK, Keyhani NO, Roseman S. 2000. Chitin catabolism in the marine bacterium Vibrio furnissii: Identification, molecular cloning, and characterization of a W^V'-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
  • 27
    • 0037119381 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a unique β-glucosidase from Vibrio cholerae
    • DOI 10.1074/jbc.M202978200
    • Park JK, Wang LX, Patel HV, Roseman S. 2002a. Molecular cloning and characterization of a unique p-glucosidase from Vibrio cholerae. J Biol Chem. 277:29555-29560. (Pubitemid 41079243)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.33 , pp. 29555-29560
    • Park, J.K.1    Wang, L.-X.2    Patel, H.V.3    Roseman, S.4
  • 28
    • 0037013321 scopus 로고    scopus 로고
    • Isolation of a glucosamine-specific kinase, a unique enzyme of Vibrio cholerae
    • DOI 10.1074/jbc.M107953200
    • Park JK, Wang LX, Roseman S. 2002b. Isolation of a glucosamine-specific kinase, a unique enzyme of Vibrio cholerae. J Biol Chem. 277:15573-15578. (Pubitemid 34967826)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15573-15578
    • Park, J.K.1    Wang, L.-X.2    Roseman, S.3
  • 29
    • 0037125924 scopus 로고    scopus 로고
    • Crystal structure of the cellulase Ce19M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases
    • DOI 10.1021/bi025816m
    • Parsiegla G, Belaich A, Belaich JP, Haser R. 2002. Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases. Biochemistry. 41:11134-11142. (Pubitemid 35034015)
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11134-11142
    • Parsiegla, G.1    Belaich, A.2    Belaich, J.P.3    Haser, R.4
  • 31
    • 40449132569 scopus 로고    scopus 로고
    • Cel9D, an atypical 1,4-β-D-glucan glucohydrolase from Fibrobacter succinogenes: Characteristics, catalytic residues, and synergistic interactions with other cellulases
    • DOI 10.1128/JB.01667-07
    • Qi M, Jun HS, Forsberg CW. 2008. Cel9D, an atypical 1,4-p-D-glucan gluco-hydrolase from Fibrobacter succinogenes: Characteristics, catalytic residues, and synergistic interactions with other cellulases. J Bacteriol. 190:1976-1984. (Pubitemid 351355320)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 1976-1984
    • Qi, M.1    Jun, H.-S.2    Forsberg, C.W.3
  • 33
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • DOI 10.1038/nsb1097-810
    • Sakon J, Irwin D, Wilson DB, Karplus PA. 1997. Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nat Struct Biol. 4:810-818. (Pubitemid 27435346)
    • (1997) Nature Structural Biology , vol.4 , Issue.10 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Andrew Karplus, P.4
  • 35
    • 0842327141 scopus 로고    scopus 로고
    • Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from Clostridium thermocellum
    • DOI 10.1021/bi030202i
    • Schubot FD, Kataeva IA, Chang J, Shah AK, Ljungdahl LG, Rose JP, Wang BC. 2004. Structural basis for the exocellulase activity of the cellobiohydro-lase CbhA from Clostridium thermocellum. Biochemistry. 43:1163-1170. (Pubitemid 38176514)
    • (2004) Biochemistry , vol.43 , Issue.5 , pp. 1163-1170
    • Schubot, F.D.1    Kataeva, I.A.2    Chang, J.3    Shah, A.K.4    Ljungdahl, L.G.5    Rose, J.P.6    Wang, B.-C.7
  • 36
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • Somogyi M. 1952. Notes on sugar determination. J Biol Chem. 195:19-23.
    • (1952) J Biol Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 37
    • 0042890412 scopus 로고    scopus 로고
    • Characterization of an exo-β-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • DOI 10.1128/JB.185.17.5175-5181.2003
    • Tanaka T, Fukui T, Atomi H, Imanaka T. 2003. Characterization of an exo-p-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Bacteriol. 185:5175-5181. (Pubitemid 37021979)
    • (2003) Journal of Bacteriology , vol.185 , Issue.17 , pp. 5175-5181
    • Tanaka, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 38
    • 57749191947 scopus 로고    scopus 로고
    • The structural basis of substrate recognition in an exo-p-D- glucosaminidase involved in chitosan hydrolysis
    • Van Bueren AL, Ghinet MG, Gregg K, Fleury A, Brzezinski R, Boraston AB. 2009. The structural basis of substrate recognition in an exo-p-D- glucosaminidase involved in chitosan hydrolysis. J Mol Biol. 385:131-139.
    • (2009) J Mol Biol , vol.385 , pp. 131-139
    • Van Bueren, A.L.1    Ghinet, M.G.2    Gregg, K.3    Fleury, A.4    Brzezinski, R.5    Boraston, A.B.6
  • 40
    • 0001681096 scopus 로고
    • The occurrence and characteristics of chiti-noclastic bacteria in the sea
    • Zobell CE, Rittenberg SC. 1938. The occurrence and characteristics of chiti-noclastic bacteria in the sea. J Bacteriol. 35:275-287.
    • (1938) J Bacteriol , vol.35 , pp. 275-287
    • Zobell, C.E.1    Rittenberg, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.