The Chemical Modification of the Essential Groups of β -N-Acetyl-D-glucosaminidase from Turbo cornutus Solander

IUBMB Life

Volumn 55, Issue 9, 2003, Pages 547-552

  Lin, Jian Cheng ^a,b   Chen, Qing Xi ^a   Shi, Yan ^a   Li, Shao Wei ^a   Zhao, Hong ^a  

^a XIAMEN UNIVERSITY   (China)

^b PUTIAN UNIVERSITY   (China)

Author keywords

N Acetyl D glucosaminidase; Chemical modification; Essential groups

Indexed keywords

CARBOXYL GROUP; CYSTEINE; FORMALDEHYDE; HYDROXYL GROUP; IMIDAZOLE; LYSINE; N ACETYL BETA GLUCOSAMINIDASE; N BROMOSUCCINIMIDE; TRINITROBENZENESULFONIC ACID; TRYPTOPHAN;

ANIMAL TISSUE; ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; ENZYME CONFORMATION; ENZYME INACTIVATION; FLUORESCENCE; MOLLUSC; NONHUMAN; PROTEIN FUNCTION; TURBO CORNUTUS;

ACETYLGLUCOSAMINIDASE; ANIMALS; HISTIDINE; SERINE; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL COMPOUNDS; TRYPTOPHAN;

ANIMALIA; BATILLUS CORNUTUS; MOLLUSCA;

EID: 0345306745     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216540310001626601     Document Type: Article

References (26)

1. Banat, B. M. A., Kameyama, Y., Yoshioka, T., and Koga, D. (1999) Purification and characterization of a 54 kDa chitinase from Bombyx mori. Insect Biol. 29, 537-547.
2. Koga, D., Nakashima, M., Matsukura, T., Kimura, S., and Ide, A. (1986) Purifications and some properties of β-N-acetyl-D-glucosaminidase from alimentary canal of the silkworm, Bombyx mori. Argric. Biol. Chem. 50(9), 2357-2368.
3. Broadway, R. M., Williams, D. L., Kaln, W. C., Harman, G. E., Lorito, M., and Labeda, D. P. (1995) Partial characterization of chitinolytic enzymes from Streptomyces albidoflavus. Letters in Appl. Microbiol. 20, 271-276.
4. Krishnaveni, S., Liang, G. H., Muthukrishnan, S., and Manickam, A. (1999) Purification and partial characterization of chitinase from sorghum seeds. Plant Sci. 144(1), 1-7.
5. Wright, D. A., and Smucker, R. A. (1986) Ionic requirements for chitinase/chitobiase activity in the oyster, Crassostrea virginica. Comp. Biochem. Physiol. 84A, 495-497.
6. Kono, M., Matsui, T., Shimizu, C., and Kaga, D. (1990) Purifications and some properties of chitinase from the liver of a prawn, Penaeus japonicus. Agric. Biol. Chem. 54(8), 2145-2147.
7. Lynn, K. R. (1990) Chitinases and chitobiases from the american lobster (Homarus americanus). Comp. Biochem. Physiol. 96B, 761-766.
8. Peters, G., Saborowski, R., Buchholz, F., and Mentlein, R. (1999) Two distinct form of the chitin-degrading enzyme β-N-acetyl-D-glucosaminidase in the Antarctic Krill: specialists in digestion and moult. Marine Biol. 134, 697-703.
9. Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M., and Tanaka, H. (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268(25), 18567-18572.
10. Zhang, H., Huang, X., Fukamizo, T., Muthukrishnan, S., and Kramer, K. J. (2002) Site-directed mutagenesis and functional analysis of an active site tryptophan of insect chitinase. Insect Biochem. Mol. Biol. 32, 1477-1488.
11. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-269.
12. Chen, Q. X., Zhang, W., Zheng, W. Z., Zhao, H., Yan, S. H., Wang, H. R., and Zhou, H. M. (1996) Kinetic of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide. J. Protein Chem. 15(4), 345-350.
13. Rapala-Kozik, M., and Kozik, A. (1996) Mechanism of ligand-protein interaction in plant seed thiamine-binding proteins. Preliminary chemical identification of amino acid residues essential for thiamine binding to the buckwheat-seed protein. Biochimie 78, 77-84.
14. Nosal, F., Masson, A., Legrand, R., Blanot, D., Schoot, B., Heijenoort, J. V., and Parquet, C. (1998) Site-directed mutagenesis and chemical modification of the two cysteine residues of the UDP-N-acetymuramoyl: L-alanine ligase of Escherichia coli. FEBS Letters 426, 309-313.
15. Kamińska, J., Wiśniewska, A., and Kościelak, J. (2003) Chemical modifications of α 1,6-fucosyltransferase define amino acid residues of catalytic importance. Biochimie 85, 303-310.
16. Fishman, W. H., and Ghosh, V. K. (1967) Influence of reagents reacting with metal, thiol amino sites on catalytic activity and L-phenylalanine of rat intestinal alkaline phosphatase. Biochem. J. 105, 1163-1167.
17. Khajeh, K., Naderi-Manesh, H., Ranjbar, B., Moosavi-Movahedi, A. A., and Nemat-Gorgani, M. (2001) Chemical modification of lysine residues in Bacillus α-amylases: effect on activity and stability. Enzyme and Microbial Technology 28, 543-549.
18. Zhou, H. M., and Wang, H. R. (1998) Chemical Modification of Proteins. pp. 30-32, Tsinghua University Press, Beijing.
19. Britten, C. J., and Bird, M. I. (1997) Chemical modification of an α-3-fucosyltransferase; definition of amino acid residues essential for enzyme activity. Biochim. Biophy. Acta. 1334, 57-64.
20. Zheng, W. Z., Chen, Q. X., Zhao, H., Zhang, Z., Zhang, W., and Zhou, H. M. (1997) An essential tryptophan residue of green crab (Syclla serrata) alkaline phosphatase. Biochem. Mol. Biol. Int. 41(5), 951-959.
21. Freishim, J. H., and Huennekens, F. M. (1969) Effect of N-bromosuccinimide on dihydrofolate reductase. Biochem 8, 2271-2276.
22. Yang, P. Z., Chen, Q. X., Li, L., Chen, S. L., and Zhou, H. M. (1998) Kinetics of inactivation of Penaeus penicillatus acid phosphatase during inhibition by N-bromosuccinimide. Biochem. Mol. Biol. Int. 45(5), 953-962.
23. Ding, S. H., Li, Y. W., and Zhu, L. Q. (2002) Identification of histidine residues at the active site of Megalobatrachus japonicus alkaline phosphatase by chemical modification. Biochim. Biophy. Acta. 1594, 100-108.
24. Mata, I., Castillon, M. P., Dominguez, J. M., Macarron, R., and Acebal, C. (1993) Chemical modification of β-glucosidase from Trichoderma reesei QM 9414. J. Biochem. 114, 754-759.
25. Chen, Q. X., Chen, S. L., and Zhou, H. M. (1998) Kinetics of inhibition of Penaeus penicillatus acid phosphatase by bromoacetic acid. Biochem. Mol. Biol. Int. 46(2), 215-223.
26. Chen, Q. X., Zhang, Z., Zhou, X. W., and Zhuang, Z. L. (2000) Kinetics of inhibition of β-glucosidase from Ampullarium crossean by bromoacetic acid. The Int. J. Biochem. Cell Biol. 32, 717-723.