메뉴 건너뛰기




Volumn 27, Issue 7, 2000, Pages 467-474

Carboxyl group modification significantly altered the kinetic properties of purified carboxymethylcellulase from Aspergillus niger

Author keywords

4 glucanase; Charge neutralization and reversal by chemical modification; Endo 1; Purification and kinetic properties; Thermodynamics of carboxymethylcellulose hydrolysis; Transition state theory; Water soluble carbodiimide

Indexed keywords

CHEMICAL MODIFICATION; ENTROPY; REACTION KINETICS;

EID: 0034307643     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(00)00254-4     Document Type: Article
Times cited : (52)

References (30)
  • 1
    • 0010288910 scopus 로고
    • Carboxymethylcellulase from Sclerotum rolfsii
    • W.A. Wood, & S.T. Kellogg. New York: Academic Press
    • Lindner W.A. Carboxymethylcellulase from Sclerotum rolfsii. Wood W.A., Kellogg S.T. Methods enzymol. 1988;376-382 Academic Press, New York.
    • (1988) Methods Enzymol , pp. 376-382
    • Lindner, W.A.1
  • 2
    • 0032532639 scopus 로고    scopus 로고
    • Crystal structure of the family 7 endoglucanase 1 (Cel7 B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate
    • Mackenzie L.F., Sulzenbacher G., Divne C., et al. Crystal structure of the family 7 endoglucanase 1 (Cel7 B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate. Biochem J. 335:1998;409-416.
    • (1998) Biochem J , vol.335 , pp. 409-416
    • Mackenzie, L.F.1    Sulzenbacher, G.2    Divne, C.3
  • 3
    • 0033609450 scopus 로고    scopus 로고
    • Mechanistic studies of active site mutants of Themomonospora fusca endocellulase E2
    • Wolfgang D.E., Wilson D.B. Mechanistic studies of active site mutants of Themomonospora fusca endocellulase E2. Biochemistry. 38:1999;9746-9751.
    • (1999) Biochemistry , vol.38 , pp. 9746-9751
    • Wolfgang, D.E.1    Wilson, D.B.2
  • 4
    • 0021865554 scopus 로고
    • The role of carboxyl groups in the function of endo-β-1,4-glucanase from Schizophyllum commune
    • Clarke A.J., Yaguchi M. The role of carboxyl groups in the function of endo-β-1,4-glucanase from Schizophyllum commune. Eur J Biochem. 149:1985;233-238.
    • (1985) Eur J Biochem , vol.149 , pp. 233-238
    • Clarke, A.J.1    Yaguchi, M.2
  • 5
    • 0017668198 scopus 로고
    • Chemical modification of a cellulase from Aspergillus niger
    • Hurst P.L., Sullivan P.A., Shepherd M.G. Chemical modification of a cellulase from Aspergillus niger. Biochem J. 167:1977;549-556.
    • (1977) Biochem J , vol.167 , pp. 549-556
    • Hurst, P.L.1    Sullivan, P.A.2    Shepherd, M.G.3
  • 6
    • 0027259408 scopus 로고
    • Disulphide arrangement and chemical modification of β-1,4- endoglucanase-E2 from Thermomonospora-fusca
    • Mcginnis K., Wilson D.B. Disulphide arrangement and chemical modification of β-1,4- endoglucanase-E2 from Thermomonospora-fusca. Biochemistry. 32:1993;8151-8156.
    • (1993) Biochemistry , vol.32 , pp. 8151-8156
    • McGinnis, K.1    Wilson, D.B.2
  • 7
    • 0343472021 scopus 로고    scopus 로고
    • Surface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2
    • Zhang S., Wilson D.B. Surface residue mutations which change the substrate specificity of Thermomonospora fusca endoglucanase E2. J Biotechnol. 57:1997;101-113.
    • (1997) J Biotechnol , vol.57 , pp. 101-113
    • Zhang, S.1    Wilson, D.B.2
  • 8
    • 0033981570 scopus 로고    scopus 로고
    • Effect of noncatalytic residue mutations on substrate specificity and ligand binding of Thermobifida fusca endocellulase ce16A
    • Zhang S., Barr B.K., Wilson D.B. Effect of noncatalytic residue mutations on substrate specificity and ligand binding of Thermobifida fusca endocellulase ce16A. Eur J Biochem. 267:2000;244-252.
    • (2000) Eur J Biochem , vol.267 , pp. 244-252
    • Zhang, S.1    Barr, B.K.2    Wilson, D.B.3
  • 9
    • 0014216749 scopus 로고
    • A method for the quantitative modification and estimation of carboxylic acid groups in proteins
    • Hoare D.G., Koshland D.E. A method for the quantitative modification and estimation of carboxylic acid groups in proteins. J Biol Chem. 242:1967;2447-2453.
    • (1967) J Biol Chem , vol.242 , pp. 2447-2453
    • Hoare, D.G.1    Koshland, D.E.2
  • 10
    • 0030895303 scopus 로고    scopus 로고
    • Thermostabilization of carboxymethylcellulase from Aspergillus niger by carboxyl group modification
    • Siddiqui K.S., Najmus Saqib A.A., Rashid M.H., Rajoka M.I. Thermostabilization of carboxymethylcellulase from Aspergillus niger by carboxyl group modification. Biotechnol Lett. 19:1997;325-329.
    • (1997) Biotechnol Lett , vol.19 , pp. 325-329
    • Siddiqui, K.S.1    Najmus Saqib, A.A.2    Rashid, M.H.3    Rajoka, M.I.4
  • 11
    • 0032919227 scopus 로고    scopus 로고
    • Partial and complete alteration of surface charges of carboxymethylcellulase by chemical modification: Thermostabilization in water-miscible organic solvent
    • Siddiqui K.S., Shemsi A.M., Anwar M.A., Rashid M.H., Rajoka M.I. Partial and complete alteration of surface charges of carboxymethylcellulase by chemical modification thermostabilization in water-miscible organic solvent . Enzyme Microbial Technol. 24:1999;599-608.
    • (1999) Enzyme Microbial Technol , vol.24 , pp. 599-608
    • Siddiqui, K.S.1    Shemsi, A.M.2    Anwar, M.A.3    Rashid, M.H.4    Rajoka, M.I.5
  • 12
    • 17544374998 scopus 로고    scopus 로고
    • Activity and thermostability of carboxymethylcellulase from Aspergillus niger is strongly influenced by non-covalently attached polysaccharides
    • Siddiqui K.S., Azhar M.J., Rashid M.H., Rajoka M.I. Activity and thermostability of carboxymethylcellulase from Aspergillus niger is strongly influenced by non-covalently attached polysaccharides. World J Microbiol Biotechnol. 12:1996;213-216.
    • (1996) World J Microbiol Biotechnol , vol.12 , pp. 213-216
    • Siddiqui, K.S.1    Azhar, M.J.2    Rashid, M.H.3    Rajoka, M.I.4
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72:1976;248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0009290576 scopus 로고
    • Guide to protein purification
    • Academic Press, San Diego
    • Deutscher MP. Guide to protein purification, Methods enzymol. Academic Press, San Diego 1990;182.
    • (1990) Methods Enzymol. , pp. 182
    • Deutscher, M.P.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0027772708 scopus 로고
    • Arthrobacter D-xylose isomerase: Chemical modification of carboxy groups and protein engineering of pH optimum
    • Siddiqui K.S., Loviny-Anderton T., Rangarajan M., Hartely B.S. Arthrobacter D-xylose isomerase chemical modification of carboxy groups and protein engineering of pH optimum . Biochem J. 296:1993;685-691.
    • (1993) Biochem J , vol.296 , pp. 685-691
    • Siddiqui, K.S.1    Loviny-Anderton, T.2    Rangarajan, M.3    Hartely, B.S.4
  • 17
    • 0000346442 scopus 로고
    • The application of the theory of absolute reaction rates to proteins
    • Eyring H., Stearn A.E. The application of the theory of absolute reaction rates to proteins. Chem Rev. 24:1939;253-270.
    • (1939) Chem Rev , vol.24 , pp. 253-270
    • Eyring, H.1    Stearn, A.E.2
  • 18
    • 0009478466 scopus 로고
    • Enzyme-substrate complementarity and the use of binding energy in catalysis
    • W.H. Freeman and Company, New York
    • Fersht A. Enzyme-substrate complementarity and the use of binding energy in catalysis. In: Enzyme Structure and Mechanism. W.H. Freeman and Company, New York, 1985:311-346.
    • (1985) In: Enzyme Structure and Mechanism , pp. 311-346
    • Fersht, A.1
  • 19
    • 0018707566 scopus 로고
    • Effect of pH on enzymes
    • D.L. Purich. San Diego: Academic Press
    • Tipton K.F., Dixon H.B.F. Effect of pH on enzymes. Purich D.L. Enzyme kinetics and mechanism. 1979;183-234 Academic Press, San Diego.
    • (1979) Enzyme Kinetics and Mechanism , pp. 183-234
    • Tipton, K.F.1    Dixon, H.B.F.2
  • 20
    • 0023962320 scopus 로고
    • Extracellular cellulytic enzyme system of Aspergillus japonicus: 3. Isolation, purification and characterization of multiple forms of endoglucanase
    • Kundu R.K., Dube S., Dube D.K. Extracellular cellulytic enzyme system of Aspergillus japonicus 3. Isolation, purification and characterization of multiple forms of endoglucanase . Enzyme Microb Technol. 10:1988;100-109.
    • (1988) Enzyme Microb Technol , vol.10 , pp. 100-109
    • Kundu, R.K.1    Dube, S.2    Dube, D.K.3
  • 21
    • 0028946812 scopus 로고
    • Purification and characterization of a protease-resistant cellulase from Aspergillus niger
    • Akiba S., Kimura Y., Yamamoto K., Kumagai H. Purification and characterization of a protease-resistant cellulase from Aspergillus niger. J Ferment Bioengg. 79:1995;125-130.
    • (1995) J Ferment Bioengg , vol.79 , pp. 125-130
    • Akiba, S.1    Kimura, Y.2    Yamamoto, K.3    Kumagai, H.4
  • 22
    • 0030899644 scopus 로고    scopus 로고
    • Native enzyme mobility shift assay (NEMSA) a new method for monitoring the carboxyl group modification of carboxymethylcellulase from Aspergillus niger
    • Rashid M.H., Najmus Saqib A.A., Rajoka M.I., Siddiqui K.S. Native enzyme mobility shift assay (NEMSA) a new method for monitoring the carboxyl group modification of carboxymethylcellulase from Aspergillus niger . Biotechnol Techniques. 11:1997;245-247.
    • (1997) Biotechnol Techniques , vol.11 , pp. 245-247
    • Rashid, M.H.1    Najmus Saqib, A.A.2    Rajoka, M.I.3    Siddiqui, K.S.4
  • 23
    • 0009882512 scopus 로고
    • β-glucosidase, β-glucanases and xylanases: Their mechanism of catalysis
    • A. Esen. Washington, DC: American Chemical Society
    • Clarke A.J., Bray M.R., Starting H. β-glucosidase, β-glucanases and xylanases their mechanism of catalysis . Esen A. β-glucosidase, biochemistry and molecular biology. 1993;27-41 American Chemical Society, Washington, DC.
    • (1993) β-Glucosidase, Biochemistry and Molecular Biology , pp. 27-41
    • Clarke, A.J.1    Bray, M.R.2    Starting, H.3
  • 24
    • 0031587296 scopus 로고    scopus 로고
    • The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution and a comparison with related enzymes
    • Kleywegt G.J., Zou J.-Y., Divne C., et al. The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution and a comparison with related enzymes. J Mol Biol. 272:1997;383-397.
    • (1997) J Mol Biol , vol.272 , pp. 383-397
    • Kleywegt, G.J.1    Zou, J.-Y.2    Divne, C.3
  • 25
    • 0031298093 scopus 로고    scopus 로고
    • Stability and identification of active-site residues of carboxymethylcellulases from Aspergillus niger and Cellulomonas biazotea
    • Siddiqui K.S., Azhar M.J., Rashid M.H., Rajoka M.I. Stability and identification of active-site residues of carboxymethylcellulases from Aspergillus niger and Cellulomonas biazotea. Folia Microbiol. 42:1997;312-318.
    • (1997) Folia Microbiol , vol.42 , pp. 312-318
    • Siddiqui, K.S.1    Azhar, M.J.2    Rashid, M.H.3    Rajoka, M.I.4
  • 26
    • 0030952232 scopus 로고    scopus 로고
    • Circular dichroism studies on conformation of cellobiohydrolase and endoglucanase from Trichoderma pseudokiningii S-38: Effects of pH and ligand binding
    • Xu Y.B., Quing S.Y. Circular dichroism studies on conformation of cellobiohydrolase and endoglucanase from Trichoderma pseudokiningii S-38 effects of pH and ligand binding . J Protein Chemistry. 16:1997;107-111.
    • (1997) J Protein Chemistry , vol.16 , pp. 107-111
    • Xu, Y.B.1    Quing, S.Y.2
  • 27
    • 0028364450 scopus 로고
    • The cellulose-binding domain of endoglucanase a (CENA) from Cellulomonas fimi: Evidence for the involvement of tryptophan residues in binding
    • Din N., Forsythe I.J., Burtnick L.D., et al. The cellulose-binding domain of endoglucanase a (CENA) from Cellulomonas fimi evidence for the involvement of tryptophan residues in binding . Mol Microbiol. 11:1994;747-755.
    • (1994) Mol Microbiol , vol.11 , pp. 747-755
    • Din, N.1    Forsythe, I.J.2    Burtnick, L.D.3
  • 28
    • 0029993491 scopus 로고    scopus 로고
    • The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism
    • Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M. The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J Mol Biol. 257:1996;1042-1051.
    • (1996) J Mol Biol , vol.257 , pp. 1042-1051
    • Dominguez, R.1    Souchon, H.2    Lascombe, M.-B.3    Alzari, P.M.4
  • 29
    • 0032566284 scopus 로고    scopus 로고
    • Snapshots along an enzymatic reaction coordinate: Analysis of a retaining beta-glycoside hydrolase
    • Davies G.J., Mackenzie L., Varrot A., et al. Snapshots along an enzymatic reaction coordinate analysis of a retaining beta-glycoside hydrolase . Biochemistry. 37:1998;11707-11713.
    • (1998) Biochemistry , vol.37 , pp. 11707-11713
    • Davies, G.J.1    Mackenzie, L.2    Varrot, A.3
  • 30
    • 0015924871 scopus 로고
    • Enzymatic catalysis and transition state theory
    • Lienhard G.E. Enzymatic catalysis and transition state theory. Science. 180:1973;149-154.
    • (1973) Science , vol.180 , pp. 149-154
    • Lienhard, G.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.