Structure and function of poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1

Journal of Bacteriology

Volumn 179, Issue 22, 1997, Pages 6965-6970

  Nojiri, Masaki ^a,b   Saito, Terumi ^a  

^a KANAGAWA UNIVERSITY   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

POLY(3 HYDROXYBUTYRIC ACID);

ALCALIGENES FAECALIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHIMERA; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME STRUCTURE; GENE DELETION; HYDROLYSIS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ALCALIGENES FAECALIS; PAUCIMONAS LEMOIGNEI; PSEUDOMONAS;

EID: 0030730849     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.22.6965-6970.1997     Document Type: Article

References (32)

1. Anderson, A. J., and E. A. Dawes. 1990. Occurrence, metabolism, metabolic role, and industrial use of bacterial polyhydroxyalkanoates. Microbiol. Rev. 54:450-472.
2. Behrends, A., B. Klingbeil, and D. Jendrossek. 1996. Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site. FEMS Microbiol. Lett. 143:191-194.
3. Briese, B. H., B. Schmidt, and D. Jendrossek. 1994. Pseudomonas lemoignei has five poly(hydroxyalkanoic acid) (PHA) depolymerase genes: a comparative study of bacterial and eukaryotic PHA depolymerases. J. Environ. Polym. Degrad. 2:75-87.
4. Caeser, G. V., and M. L. Cushing. 1941. The starch molecule. J. Phys. Chem. 45:776-790.
5. Doi, Y. 1990. Microbial polyesters. VCH, New York, N.Y.
6. Fukui, T., T. Narikawa, K. Miwa, Y. Shirakura, T. Saito, and K. Tomita. 1988. Effect of limited tryptic modification of a bacterial poly(3-hydroxybutyrate) depolymerase on its catalytic activity. Biochim. Biophys. Acta 952: 164-171.
7. Gilkes, N. R., R. A. J. Warren, R. C. Miller, Jr., and D. G. Kilburn. 1988. Precise excision of the cellulose-binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J. Biol. Chem. 263:10401-10407.
8. Hayashida, S., K. Nakahara, W. Kanlayakrit, T. Hara, and Y. Teramoto. 1989. Characteristics and function of raw-starch-affinity on Aspergillus awamori var. kawachi glucoamylase I module. Agric. Biol. Chem. 53:143-149.
9. Jaeger, K. E., S. Ransac, B. W. Dijkstra, C. Colson, M. Heuvel, and O. Misset. 1994. Bacterial lipases. FEMS Microbiol. Rev. 15:29-63.
10. Jendrossek, D., A. Frisse, A. Behrends, M. Andermann, H. D. Kratzin, T. Stanislawski, and H. G. Schlegel. 1995. Biochemical and molecular characterization of the Pseudomonas lemoignei polyhydroxyalkanoate depolymerase system. J. Bacteriol. 177:596-607.
11. Jendrossek, D., B. Müller, and H. G. Schlegel. 1993. Cloning and characterization of the poly(hydroxyalkanoic acid)-depolymerase gene locus, phaZ1, of Pseudomonas lemoignei and its gene product. Eur. J. Biochem. 218:701-710.
12. Jendrossek, D., A. Schirmer, and H. G. Schlegel. 1996. Biodegradation of polyhydroxyalkanoic acids. Appl. Microbiol. Biotechnol. 46:451-463.
13. Kumagai, Y., Y. Kanesawa, and Y. Doi. 1992. Enzymatic degradation of microbial poly(3-hydroxybutyrate) films. Makromol. Chem. 193:53-57.
14. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
15. Layne, E. 1957. Spectrophotometric and turbidimetric methods for measuring proteins. Methods Enzymol. 3:447-454.
16. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
17. Saito, T., A. Iwata, and T. Watanabe. 1993. Molecular structure of extracellular poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1. J. Environ. Polym. Degrad. 1:99-105.
18. Saito, T., K. Suzuki, J. Yamamoto, T. Fukui, K. Miwa, K. Tomita, S. Nakanishi, S. Odani, J.-I. Suzuki, and K. Ishikawa. 1989. Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. J. Bacteriol. 171:184-189.
19. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
20. Semimaru, T., M. Goto, K. Furukawa, and S. Hayashida. 1995. Functional analysis of threonine- and serine-rich Gp-1 domain of glucoamylase I from Aspergillus awamori var. kawachi. Appl. Environ. Microbiol. 61:2885-2890.
21. Shinohe, T., M. Nojiri, T. Saito, T. Stanislawski, and D. Jendrossek. 1996. Determination of the active site serine of the poly (3-hydroxybutyrate) depolymerase of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis. FEMS Microbiol. Lett. 141:103-109.
22. Shirakura, Y., T. Fukui, T. Saito, Y. Okamoto, T. Narikawa, K. Koide, K. Tomita, T. Takemasa, and S. Masamune. 1986. Degradation of poly(3-hydroxybutyrate) by poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1. Biochim. Biophys. Acta 880:46-53.
23. Shirakura, Y., T. Fukui, T. Tanio, K. Nakayama, R. Matsuno, and K. Tomita. 1983. An extracellular D(-)-3-hydroxyburyrate oligomer hydrolase from Alcaligenes faecalis. Biochim. Biophys. Acta 748:331-339.
24. Smibert, R. M., and N. R. Krieg. 1994. Phenotypic characterization, p. 607-654. In P. Gerhardt, R. G. E. Murray, W. A. Wood, and N. R. Krieg (ed.), Methods for general and molecular bacteriology. American Society for Microbiology, Washington, D.C.
25. Steinbüchel, A., and H. E. Valentin. 1995. Diversity of bacterial polyhydroxyalkanoic acids. FEMS Microbiol. Lett. 128:219-228.
26. Tanio, T., T. Fukui, T. Saito, Y. Okamoto, T. Narikawa, K. Koide, K. Tomita, T. Takemasa, and S. Masamune. 1982. An extracellular poly( 3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. Eur. J. Biochem. 124:71-77.
27. Tomme, P., D. P. Driver, E. A. Amandoron, R. C. Miller, Jr., R. Antony, J. Warren, and D. G. Kilburn. 1995. Comparison of a fungal (family I) and bacterial (family II) cellulose-binding domain. J. Bacteriol. 177:4356-4363.
28. Tomme, P., H. Van Tilbeurgh, G. Pettersson, J. Van Damme, J. Vandekerckhove, J. Knowles, T. Teeri, and M. Claeyssens. 1988. Studies on the cellulolytic system of Trichoderma reesei QM94I4. Eur. J. Biochem. 170:575-581.
29. Van Tilbeurgh, H., P. Tomme, M. Claeysson, R. Bhikhabhai, and G. Pettersson. 1986. Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei. FEBS Lett. 204:223-227.
30. Voet, D., and J. D. Voet. 1995. Biochemistry, 2nd ed. John Wiley and Sons, Inc., New York, N.Y.
31. Warren, R. A. J. 1996. Engineering cellulases: catalysis, binding, and modules. ASM News 62:85-88.
32. Watanabe, T., Y. Ito, T. Yamada, M. Hashimoto, S. Sekine, and H. Tanaka. 1994. The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176: 4465-4472.