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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
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The purified xylanase from Bacillus pumilus TX703 was modified with various chemical modifiers to determine the active sites of the enzyme. Treatment of the enzyme with group-specific reagents such as carbodiimide or N-bromosuccinimide resulted in complete loss of enzyme activity. These results assumed that these reagents reacted with glutamic acid or aspartic acid and tryptophan residues located at or near the active site. In each case, inactivation was performed by pseudo first-order kinetics. Inhibition of enzyme activity by carbodiimide and N-bromosuccinimide showed non-competitive and competitive inhibition type, respectively. Addition of xylan to the enzyme solution containing N-bromosuccinimide prevented the inactivation, indicating the presence of tryptophan at the substrate binding site. Analysis of kinetics for inactivation showed that the loss of enzyme activity was due to modification of two glutamic acid or aspartic acid residues and single tryptophan residue.
목차
Abstract
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참고문헌
참고문헌 (26)
참고문헌 신청
Bandivadekar, K. R. and V. V. Deshpande. 1996. Structurefunction relationship of xylanase: fluorimetric analysis of the tryptophan environment. Biochem. J. 315, 583-587.
Biely, P. 1985. Microbial xylanolytic systems. Trends Biotechnol. 3, 286-290.
Blanke, S. R. and L. P. Hager. 1990. Chemical modification of chloroperoxidase with diethylpyrocarbonate. Evidence for the presence of an essential histidine residue. J. Biol. Chem. 265, 12454-12461.
Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
Church, F. C., R. L. Lundblad and C. M. Noyes. 1985. Modification of histidines on human prothrombin. Effect on the interaction of fibrinogen with thrombin from diethyl pyrocarbonate-modified prothrombin. J. biol. Chem. 260, 4936-4940.
Biely, P. 1985. Microbial xylanolytic systems. Trends Biotechnol. 3, 286-290.
Blanke, S. R. and L. P. Hager. 1990. Chemical modification of chloroperoxidase with diethylpyrocarbonate. Evidence for the presence of an essential histidine residue. J. Biol. Chem. 265, 12454-12461.
Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
Church, F. C., R. L. Lundblad and C. M. Noyes. 1985. Modification of histidines on human prothrombin. Effect on the interaction of fibrinogen with thrombin from diethyl pyrocarbonate-modified prothrombin. J. biol. Chem. 260, 4936-4940.
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UCI(KEPA) : I410-ECN-0101-2009-470-015375441