-
1
-
-
0032984477
-
Molecular and biotechnological aspects of xylanases
-
Kulkarni N., Shendye A., and Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol Rev 23 (1999) 411-456
-
(1999)
FEMS Microbiol Rev
, vol.23
, pp. 411-456
-
-
Kulkarni, N.1
Shendye, A.2
Rao, M.3
-
3
-
-
0036210191
-
Biotechnology of microbial xylanases: enzymology, molecular biology and application
-
Subramaniyan S., and Prema P. Biotechnology of microbial xylanases: enzymology, molecular biology and application. Crit Rev Biotechnol 22 (2002) 33-46
-
(2002)
Crit Rev Biotechnol
, vol.22
, pp. 33-46
-
-
Subramaniyan, S.1
Prema, P.2
-
4
-
-
0032712358
-
Alkaliphiles: some applications of their products for biotechnology
-
Horikoshi K. Alkaliphiles: some applications of their products for biotechnology. Microbiol Mol Biol Rev 63 (1999) 735-750
-
(1999)
Microbiol Mol Biol Rev
, vol.63
, pp. 735-750
-
-
Horikoshi, K.1
-
5
-
-
12144282020
-
Xylanases, xylanase families and extremophilic xylanases
-
Collins T., Gerday C., and Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 29 (2005) 3-23
-
(2005)
FEMS Microbiol Rev
, vol.29
, pp. 3-23
-
-
Collins, T.1
Gerday, C.2
Feller, G.3
-
6
-
-
0024087074
-
Multiplicity of β-1,4-xylanase in microorganisms: functions and applications
-
Wong K.K.Y., Tan L.U.L., and Saddler J.N. Multiplicity of β-1,4-xylanase in microorganisms: functions and applications. Microbiol Rev 52 (1988) 305-307
-
(1988)
Microbiol Rev
, vol.52
, pp. 305-307
-
-
Wong, K.K.Y.1
Tan, L.U.L.2
Saddler, J.N.3
-
7
-
-
0027259353
-
Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. 41M-1
-
Nakamura S., Wakabayashi K., Nakai R., Aono R., and Horikoshi K. Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. 41M-1. Appl Env Microbiol 59 (1993) 2311-2316
-
(1993)
Appl Env Microbiol
, vol.59
, pp. 2311-2316
-
-
Nakamura, S.1
Wakabayashi, K.2
Nakai, R.3
Aono, R.4
Horikoshi, K.5
-
8
-
-
0031715687
-
Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp.
-
Gessesse A. Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp. Appl Env Microbiol 64 (1998) 3533-3535
-
(1998)
Appl Env Microbiol
, vol.64
, pp. 3533-3535
-
-
Gessesse, A.1
-
9
-
-
0344406096
-
Three dimensional structures of thermophilic β-1,4-xylanases from Chaetomimum thermophilum and Nonomuraea flexuosa
-
Hakulinen N., Turunen O., Janis J., Leisola M., and Rouvinen J. Three dimensional structures of thermophilic β-1,4-xylanases from Chaetomimum thermophilum and Nonomuraea flexuosa. Eur J Biochem 270 (2003) 1399-1412
-
(2003)
Eur J Biochem
, vol.270
, pp. 1399-1412
-
-
Hakulinen, N.1
Turunen, O.2
Janis, J.3
Leisola, M.4
Rouvinen, J.5
-
10
-
-
0029588275
-
Alkaline-active xylanase produced by an alkaliphilic Bacillus sp. isolated from kraft pulp
-
Yang V.W., Zhuang Z., Elegir G., and Jeffries T.W. Alkaline-active xylanase produced by an alkaliphilic Bacillus sp. isolated from kraft pulp. J Ind Microbiol 15 (1995) 434-444
-
(1995)
J Ind Microbiol
, vol.15
, pp. 434-444
-
-
Yang, V.W.1
Zhuang, Z.2
Elegir, G.3
Jeffries, T.W.4
-
12
-
-
0026666350
-
Chemical and kinetic evidence for an essential histidine in horseradish peroxidase for iodide oxidation
-
Bhattacharyya D.K., Bandyopadhyay U., and Banerjee R.K. Chemical and kinetic evidence for an essential histidine in horseradish peroxidase for iodide oxidation. J Biol Chem 267 (1992) 9800-9804
-
(1992)
J Biol Chem
, vol.267
, pp. 9800-9804
-
-
Bhattacharyya, D.K.1
Bandyopadhyay, U.2
Banerjee, R.K.3
-
13
-
-
0034832020
-
Conformation and polarity of the active site of xylanase I from Thermomonospora sp. as deduced by fluorescent chemoaffinity labeling
-
George S.P., and Rao M.B. Conformation and polarity of the active site of xylanase I from Thermomonospora sp. as deduced by fluorescent chemoaffinity labeling. Eur J Biochem 268 (2001) 2881-2888
-
(2001)
Eur J Biochem
, vol.268
, pp. 2881-2888
-
-
George, S.P.1
Rao, M.B.2
-
14
-
-
0033134965
-
Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium
-
Olano J., Soler J., Busto F., and Arriaga D. Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium. Eur J Biochem 261 (1999) 640-649
-
(1999)
Eur J Biochem
, vol.261
, pp. 640-649
-
-
Olano, J.1
Soler, J.2
Busto, F.3
Arriaga, D.4
-
15
-
-
0029873547
-
Structure-function relationship of xylanase: fluorimetric analysis of the tryptophan environment
-
Bandivadekar K.R., and Deshpande V.V. Structure-function relationship of xylanase: fluorimetric analysis of the tryptophan environment. Biochem J 315 (1996) 583-587
-
(1996)
Biochem J
, vol.315
, pp. 583-587
-
-
Bandivadekar, K.R.1
Deshpande, V.V.2
-
16
-
-
34447100148
-
-
Ladokhin AS. Fluoroscence spectroscopy in peptide and protein analysis. In: Encyclopedia of analytical chemistry. John & Wiley Sons Ltd., 2000, p. 1-15.
-
-
-
-
17
-
-
33846427726
-
A novel cellulase free alkaliphilic xylanase from alkali tolerant Penicillium citrinum: production, purification and characterization
-
Dutta T., Sengupta R., Sahoo R., Sinha Ray S., Bhattacharjee A., and Ghosh S. A novel cellulase free alkaliphilic xylanase from alkali tolerant Penicillium citrinum: production, purification and characterization. Lett Appl Microbiol 44 (2007) 206-211
-
(2007)
Lett Appl Microbiol
, vol.44
, pp. 206-211
-
-
Dutta, T.1
Sengupta, R.2
Sahoo, R.3
Sinha Ray, S.4
Bhattacharjee, A.5
Ghosh, S.6
-
18
-
-
0017184389
-
A rapid and sensitive method for detecting microgram amounts of protein utilizing the principle of protein-dye binding
-
Bradford M.M. A rapid and sensitive method for detecting microgram amounts 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
-
19
-
-
0025324282
-
Chemical modification of chloroperoxidase with diethylpyrocarbonate. Evidence for the presence of an essential histidine residue
-
Blanke S.R., and Hager L.P. Chemical modification of chloroperoxidase with diethylpyrocarbonate. Evidence for the presence of an essential histidine residue. J Biol Chem 265 (1990) 12454-12461
-
(1990)
J Biol Chem
, vol.265
, pp. 12454-12461
-
-
Blanke, S.R.1
Hager, L.P.2
-
20
-
-
0021796302
-
Modification of histidines in human prothrombin. Effect on the interaction of fibrinogen with thrombin from diethyl pyrocarbonate-modified prothrombin
-
Church F.C., Lundblad R.L., and Noyes C.M. Modification of histidines in human prothrombin. Effect on the interaction of fibrinogen with thrombin from diethyl pyrocarbonate-modified prothrombin. J Biol Chem 260 (1985) 4936-4940
-
(1985)
J Biol Chem
, vol.260
, pp. 4936-4940
-
-
Church, F.C.1
Lundblad, R.L.2
Noyes, C.M.3
-
21
-
-
0000399944
-
Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds
-
Levy H.M., Leber P.D., and Ryan E.M. Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds. J Biol Chem 238 (1963) 3654-3659
-
(1963)
J Biol Chem
, vol.238
, pp. 3654-3659
-
-
Levy, H.M.1
Leber, P.D.2
Ryan, E.M.3
-
22
-
-
0017632673
-
Modification of histidyl residues in proteins by diethylpyrocarbonate
-
Miles E.W. Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol 47 (1977) 431-442
-
(1977)
Methods Enzymol
, vol.47
, pp. 431-442
-
-
Miles, E.W.1
-
23
-
-
0022730961
-
Chemical modification by diethylpyrocarbonate of an essential histidine residues in 3-ketovalidoxylamine A C-N lyase
-
Takeuchi M., Asano N., Kameda Y., and Matsui K. Chemical modification by diethylpyrocarbonate of an essential histidine residues in 3-ketovalidoxylamine A C-N lyase. J Biochem (Tokyo) 99 (1986) 1571-1577
-
(1986)
J Biochem (Tokyo)
, vol.99
, pp. 1571-1577
-
-
Takeuchi, M.1
Asano, N.2
Kameda, Y.3
Matsui, K.4
-
24
-
-
0032499716
-
Structure and function of Bacillus 486 hybrid enzyme GluXln-1: Native like jellyroll fold preserved after insertion of autonomous globular domain
-
Gotz F., Borriss R., and Heinemann U. Structure and function of Bacillus 486 hybrid enzyme GluXln-1: Native like jellyroll fold preserved after insertion of autonomous globular domain. Proc Natl Acad Sci USA 95 (1998) 6613-6618
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 6613-6618
-
-
Gotz, F.1
Borriss, R.2
Heinemann, U.3
-
25
-
-
0034716940
-
Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
-
Joshi M.D., Sidhu G., Pot I., Brayer G.D., Withers S.G., and McIntosh L.P. Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase. J Mol Biol 299 (2000) 255-279
-
(2000)
J Mol Biol
, vol.299
, pp. 255-279
-
-
Joshi, M.D.1
Sidhu, G.2
Pot, I.3
Brayer, G.D.4
Withers, S.G.5
McIntosh, L.P.6
-
26
-
-
0028211360
-
Mutational and crystallographic analyses of the active site residues of Bacillus circulans xylanase
-
Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., and Yaguchi M. Mutational and crystallographic analyses of the active site residues of Bacillus circulans xylanase. Protein Sci 3 (1994) 467-475
-
(1994)
Protein Sci
, vol.3
, pp. 467-475
-
-
Wakarchuk, W.W.1
Campbell, R.L.2
Sung, W.L.3
Davoodi, J.4
Yaguchi, M.5
-
27
-
-
0035964164
-
Dissecting the electrostatic interactions and ph dependent activity of a family 11 glycosidase
-
Joshi M.D., Sidhu G., Pot I., Brayer G.D., Withers S.G., and McIntosh L.P. Dissecting the electrostatic interactions and ph dependent activity of a family 11 glycosidase. Biochemistry 40 (2001) 10115-10139
-
(2001)
Biochemistry
, vol.40
, pp. 10115-10139
-
-
Joshi, M.D.1
Sidhu, G.2
Pot, I.3
Brayer, G.D.4
Withers, S.G.5
McIntosh, L.P.6
-
28
-
-
0028911057
-
Structural comparison of two major endo-β-1,4-xylanase from Trichoderma reesei
-
Torronen A., and Rouvinen J. Structural comparison of two major endo-β-1,4-xylanase from Trichoderma reesei. Biochemistry 34 (1995) 847-856
-
(1995)
Biochemistry
, vol.34
, pp. 847-856
-
-
Torronen, A.1
Rouvinen, J.2
-
29
-
-
0028338985
-
Three dimensional structure endo-β-1,4-xylanase II from Trichoderma reesei: two conformational states in the active site
-
Torronen A., Harkki A., and Rouvinen J. Three dimensional structure endo-β-1,4-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J 13 (1994) 2493-2501
-
(1994)
EMBO J
, vol.13
, pp. 2493-2501
-
-
Torronen, A.1
Harkki, A.2
Rouvinen, J.3
-
30
-
-
0030592470
-
Three dimensional structure of endo-β-1,4-xylanase I from Aspergillus niger, molecular basis of its low pH optimum
-
Krungel U., and Dijkstra B.W. Three dimensional structure of endo-β-1,4-xylanase I from Aspergillus niger, molecular basis of its low pH optimum. J Mol Biol 263 (1996) 70-78
-
(1996)
J Mol Biol
, vol.263
, pp. 70-78
-
-
Krungel, U.1
Dijkstra, B.W.2
-
31
-
-
0032407988
-
Crystallography and mutational analysis of an extremely acidophilic and acid-stable xylanase; biased distribution of acidic residues and importance of Asp 37 for catalysis at low pH
-
Fushinobu S., Ito K., Konno M., Wakagi T., and Matsuzawa H. Crystallography and mutational analysis of an extremely acidophilic and acid-stable xylanase; biased distribution of acidic residues and importance of Asp 37 for catalysis at low pH. Protein Eng 11 (1998) 1121-1128
-
(1998)
Protein Eng
, vol.11
, pp. 1121-1128
-
-
Fushinobu, S.1
Ito, K.2
Konno, M.3
Wakagi, T.4
Matsuzawa, H.5
-
32
-
-
0035723208
-
Direct evolution to produce an alkaliphilic variant from a Neocallimastix patriciarum xylanase
-
Chen Y.L., Tang T.Y., and Cheng K.J. Direct evolution to produce an alkaliphilic variant from a Neocallimastix patriciarum xylanase. Can J Microbiol 47 (2001) 1088-1094
-
(2001)
Can J Microbiol
, vol.47
, pp. 1088-1094
-
-
Chen, Y.L.1
Tang, T.Y.2
Cheng, K.J.3
-
33
-
-
0036217687
-
Engineering of multiple arginines in to the Ser/Thr surface of Trichoderma reesei endo-β-1,4-xylanase II increases the thermo tolerance and shifts the pH optimum towards alkaline pH
-
Turunen O., Vourio M., Fenel F., and Leisola M. Engineering of multiple arginines in to the Ser/Thr surface of Trichoderma reesei endo-β-1,4-xylanase II increases the thermo tolerance and shifts the pH optimum towards alkaline pH. Protein Eng 15 (2002) 141-145
-
(2002)
Protein Eng
, vol.15
, pp. 141-145
-
-
Turunen, O.1
Vourio, M.2
Fenel, F.3
Leisola, M.4
-
34
-
-
0030842357
-
Characterization of two important histidine residues in the active site of xylanase a from Streptomyces lividans, a family 10 glycanase
-
Roberge M., Shareck F., Morosoli R., Kluepfel D., and Dupont C. Characterization of two important histidine residues in the active site of xylanase a from Streptomyces lividans, a family 10 glycanase. Biochemistry 36 (1997) 7769-7775
-
(1997)
Biochemistry
, vol.36
, pp. 7769-7775
-
-
Roberge, M.1
Shareck, F.2
Morosoli, R.3
Kluepfel, D.4
Dupont, C.5
-
35
-
-
0031841904
-
Site-directed mutagenesis study of a conserved residue in family 10 glycanases: histidine 86 of xylanase A from Streptomyces lividans
-
Roberge M., Shareck F., Morosoli R., Kluepfel D., and Dupont C. Site-directed mutagenesis study of a conserved residue in family 10 glycanases: histidine 86 of xylanase A from Streptomyces lividans. Protein Eng 11 (1998) 399-404
-
(1998)
Protein Eng
, vol.11
, pp. 399-404
-
-
Roberge, M.1
Shareck, F.2
Morosoli, R.3
Kluepfel, D.4
Dupont, C.5
-
36
-
-
0031731750
-
Structure of xylanase from Penicillium simplicissimum
-
Schmidt A., Schlacher A., Steiner W., Schwab H., and Kratky C. Structure of xylanase from Penicillium simplicissimum. Protein Sci 7 (1998) 2081-2088
-
(1998)
Protein Sci
, vol.7
, pp. 2081-2088
-
-
Schmidt, A.1
Schlacher, A.2
Steiner, W.3
Schwab, H.4
Kratky, C.5
-
37
-
-
0031715607
-
Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutant
-
Notenboom V., Birsan C., Nitz M., Rose D.R., Warren R.A.J., and Wither S.G. Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutant. Nature 5 (1998) 812-818
-
(1998)
Nature
, vol.5
, pp. 812-818
-
-
Notenboom, V.1
Birsan, C.2
Nitz, M.3
Rose, D.R.4
Warren, R.A.J.5
Wither, S.G.6
|