메뉴 건너뛰기




Volumn 89, Issue 12, 2007, Pages 1489-1497

Biochemical characterization of a novel β-1-3, 1-4 glucan 4-glucanohydrolase from Thermomonospora sp. having a single active site for lichenan and xylan

Author keywords

1 3, 1 4 glucan 4 glucanohydrolase; Bifunctional; O phthalaldehyde; Single active site; Thermomonospora sp.; Xylanase

Indexed keywords

GLUCAN; HYDROLASE; LICHENAN; LICHENASE; UNCLASSIFIED DRUG; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 36248944069     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.06.010     Document Type: Article
Times cited : (8)

References (29)
  • 2
    • 0027772710 scopus 로고
    • Stereochemical copurse and structure of the products of the enzymic action of endo-1,3-1,4-β-d-glucan-4-glucanohydrolase from Bacillus licheniformis
    • Malet C., Jimenez-Barbero J., Berbabe M., et al. Stereochemical copurse and structure of the products of the enzymic action of endo-1,3-1,4-β-d-glucan-4-glucanohydrolase from Bacillus licheniformis. Biochem. J. 296 (1993) 753-758
    • (1993) Biochem. J. , vol.296 , pp. 753-758
    • Malet, C.1    Jimenez-Barbero, J.2    Berbabe, M.3
  • 3
    • 1642446551 scopus 로고    scopus 로고
    • Medium optimization of thermal stable β-glucanase by Bacillus subtilis ZJF - 1A5 using response surface methodology
    • Tang X., He G., Chen Q., Zhang X., and Ali M.A.M. Medium optimization of thermal stable β-glucanase by Bacillus subtilis ZJF - 1A5 using response surface methodology. Biosour. Technol. 93 (2004) 175-181
    • (2004) Biosour. Technol. , vol.93 , pp. 175-181
    • Tang, X.1    He, G.2    Chen, Q.3    Zhang, X.4    Ali, M.A.M.5
  • 4
    • 0034832020 scopus 로고    scopus 로고
    • Conformation and polarity of active site of xylanase I from Thermomonospora sp. as deduced by fluorescent chemoaffinity labeling: Site and significance of a histidine residue
    • George S., and Rao M. Conformation and polarity of active site of xylanase I from Thermomonospora sp. as deduced by fluorescent chemoaffinity labeling: Site and significance of a histidine residue. Eur. J. Biochem. 268 (2001) 2881-2888
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2881-2888
    • George, S.1    Rao, M.2
  • 5
    • 0035314559 scopus 로고    scopus 로고
    • Studies on carboxymethyl cellulose produced by an alkalothermophilic actinomycete
    • George S.P., Ahmad A., and Rao M. Studies on carboxymethyl cellulose produced by an alkalothermophilic actinomycete. Bioresour. Technol. 77 (2001) 171-175
    • (2001) Bioresour. Technol. , vol.77 , pp. 171-175
    • George, S.P.1    Ahmad, A.2    Rao, M.3
  • 6
    • 0034814476 scopus 로고    scopus 로고
    • Involvement of a lysine residue in the active site of a thermostable xylanase from Thermomonospora sp
    • George S., Ahmad A., and Rao M. Involvement of a lysine residue in the active site of a thermostable xylanase from Thermomonospora sp. Biochem. Biophys. Res. Commun. 282 (2001) 48-54
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 48-54
    • George, S.1    Ahmad, A.2    Rao, M.3
  • 7
    • 13844256879 scopus 로고    scopus 로고
    • Purification and properties of a low molecular weight 1,4-β-D-Glucan glucano hydrolase having one active site for carboxy methyl cellulose and xylan from an alkalothermophilic Thermomonospora sp
    • Jagtap S., and Rao M. Purification and properties of a low molecular weight 1,4-β-D-Glucan glucano hydrolase having one active site for carboxy methyl cellulose and xylan from an alkalothermophilic Thermomonospora sp. Biochem. Biophys. Res. Commun. 329 (2005) 111-116
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 111-116
    • Jagtap, S.1    Rao, M.2
  • 8
    • 33745901081 scopus 로고    scopus 로고
    • Conformation and microenvironment of the active site of a low molecular weight 1,4-β-D-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues
    • Jagtap S., and Rao M. Conformation and microenvironment of the active site of a low molecular weight 1,4-β-D-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues. Biochem. Biophys. Res. Commun. 347 (2006) 428-432
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 428-432
    • Jagtap, S.1    Rao, M.2
  • 9
    • 33645768143 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray characterization of a thermostable low molecular weight 1,4-β-D glucan-glucohydrolase from an alkalothermophilic Thermomonospora sp
    • Manikandan K., Jagtap S., Rao M., and Ramakumar S. Crystallization and preliminary X-ray characterization of a thermostable low molecular weight 1,4-β-D glucan-glucohydrolase from an alkalothermophilic Thermomonospora sp. Acta Crystallogr. Sect. F 62 (2006) 385-387
    • (2006) Acta Crystallogr. Sect. F , vol.62 , pp. 385-387
    • Manikandan, K.1    Jagtap, S.2    Rao, M.3    Ramakumar, S.4
  • 10
    • 36248953682 scopus 로고    scopus 로고
    • R. Anish, A. Ahmad, M.B. Rao, M.S. Rahman, C. Trivedi, A process for the biofinishing of denims in textile industry, (2004) Indian patent application No. 1299/DEL/2004.
  • 11
    • 33845954264 scopus 로고    scopus 로고
    • Application of cellulases from an alkalothermophilic Thermomonospora sp. in biopolishing of Denims
    • Anish R., Rahman M.S., and Rao M. Application of cellulases from an alkalothermophilic Thermomonospora sp. in biopolishing of Denims. Biotechnol. Bioeng. 96 (2007) 48-56
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 48-56
    • Anish, R.1    Rahman, M.S.2    Rao, M.3
  • 12
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.M. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.M.1
  • 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
    • 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
  • 15
    • 0014018296 scopus 로고
    • Determination of disulphide groups in proteins
    • Cavallini D., Graziani M.T., and Dupre S. Determination of disulphide groups in proteins. Nature 212 (1966) 294-295
    • (1966) Nature , vol.212 , pp. 294-295
    • Cavallini, D.1    Graziani, M.T.2    Dupre, S.3
  • 16
    • 77956994950 scopus 로고
    • Determination of tryptophan content of proteins with N-bromosuccimide
    • Hirs C.H.W. (Ed), Academic Press Inc, New York
    • Spande T.F., and Witkop B. Determination of tryptophan content of proteins with N-bromosuccimide. In: Hirs C.H.W. (Ed). Methods in Enzymology (1967), Academic Press Inc, New York 498-506
    • (1967) Methods in Enzymology , pp. 498-506
    • Spande, T.F.1    Witkop, B.2
  • 17
    • 0023866374 scopus 로고
    • A kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates
    • Keleti T., Leocini R., Pagani R., and Marinello E. A kinetic method for distinguishing whether an enzyme has one or two active sites for two different substrates. Eur. J. Biochem. 170 (1987) 179-183
    • (1987) Eur. J. Biochem. , vol.170 , pp. 179-183
    • Keleti, T.1    Leocini, R.2    Pagani, R.3    Marinello, E.4
  • 18
    • 0018247422 scopus 로고
    • Reaction of o-phthalaldehyde and thiols with primary amines: fluorescence properties of 1-alky (and aryl) thio-2-alkylisoindoles
    • Simons S.S., and Johnson D.F. Reaction of o-phthalaldehyde and thiols with primary amines: fluorescence properties of 1-alky (and aryl) thio-2-alkylisoindoles. Anal. Biochem. 90 (1978) 705-725
    • (1978) Anal. Biochem. , vol.90 , pp. 705-725
    • Simons, S.S.1    Johnson, D.F.2
  • 19
    • 0013889689 scopus 로고    scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
    • Habeeb A.F.S.A. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Biochem. 14 (1996) 328-336
    • (1996) Anal. Biochem. , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 22
    • 0027231373 scopus 로고
    • A bifunctional enzyme, with separate xylanase and (1,3-1,4)-glucanase domains, encoded by the xynD gene of Runinococcus flavaciens
    • Flint H.J., Martin J., McPherson C.A., Daniel A.S., and Zhang J.X. A bifunctional enzyme, with separate xylanase and (1,3-1,4)-glucanase domains, encoded by the xynD gene of Runinococcus flavaciens. J. Bacterial. 175 (1993) 2943-2951
    • (1993) J. Bacterial. , vol.175 , pp. 2943-2951
    • Flint, H.J.1    Martin, J.2    McPherson, C.A.3    Daniel, A.S.4    Zhang, J.X.5
  • 23
    • 0029560330 scopus 로고
    • Contribution of disulphide bridge to the stability of β-1-3, 1-4 glucan 4-glucanohydrolase from Bacillus licheniformis
    • Pons J., Planas A., and Querol E. Contribution of disulphide bridge to the stability of β-1-3, 1-4 glucan 4-glucanohydrolase from Bacillus licheniformis. Prot. Eng. 89 (1995) 939-945
    • (1995) Prot. Eng. , vol.89 , pp. 939-945
    • Pons, J.1    Planas, A.2    Querol, E.3
  • 24
    • 0026694062 scopus 로고
    • Essential catalytic role of glu134 in endo-β-1,3-1,4-d-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis
    • Planas A., Juncosa M., Lloberas J., and Querol E. Essential catalytic role of glu134 in endo-β-1,3-1,4-d-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis. FEBS Lett. 308 (1992) 141-145
    • (1992) FEBS Lett. , vol.308 , pp. 141-145
    • Planas, A.1    Juncosa, M.2    Lloberas, J.3    Querol, E.4
  • 25
    • 0026047493 scopus 로고
    • Active site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of two 1,3-1,4-beta-D-glucan 4-glucanohydrolases. The importance of epoxide stereochemistry for enzyme inactivation
    • Hoj P.B., Rodriguez E.B., Iser J.R., Stick R.V., and Stone B.A. Active site-directed inhibition by optically pure epoxyalkyl cellobiosides reveals differences in active site geometry of two 1,3-1,4-beta-D-glucan 4-glucanohydrolases. The importance of epoxide stereochemistry for enzyme inactivation. J. Biol. Chem. 266 (1991) 11628-11631
    • (1991) J. Biol. Chem. , vol.266 , pp. 11628-11631
    • Hoj, P.B.1    Rodriguez, E.B.2    Iser, J.R.3    Stick, R.V.4    Stone, B.A.5
  • 26
    • 0028271963 scopus 로고
    • Cation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability
    • Keitel T., Meldgaard M., and Heinemann U. Cation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability. Eur. J. Biochem. 222 (1994) 203-214
    • (1994) Eur. J. Biochem. , vol.222 , pp. 203-214
    • Keitel, T.1    Meldgaard, M.2    Heinemann, U.3
  • 27
    • 0032508394 scopus 로고    scopus 로고
    • Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues
    • Viladot J.L., de Ramon E., Durany O., and Planas A. Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues. Biochemistry 37 (1998) 11332-11342
    • (1998) Biochemistry , vol.37 , pp. 11332-11342
    • Viladot, J.L.1    de Ramon, E.2    Durany, O.3    Planas, A.4
  • 28
    • 0029866675 scopus 로고    scopus 로고
    • D. von Wettstein, Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-β-glucanase during germination
    • Jensen L.G., Olsen O., Kops O., Wolf N., and Thomsen K.K. D. von Wettstein, Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-β-glucanase during germination. Proc. Natl. Acad. Sci. USA 93 (1996) 3487-3491
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3487-3491
    • Jensen, L.G.1    Olsen, O.2    Kops, O.3    Wolf, N.4    Thomsen, K.K.5
  • 29
    • 0027995966 scopus 로고
    • Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-beta-glucanases secreted from yeast
    • Meldgaard M., and Svendsen I. Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-beta-glucanases secreted from yeast. Microbiology 140 (1994) 159-166
    • (1994) Microbiology , vol.140 , pp. 159-166
    • Meldgaard, M.1    Svendsen, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.