Characterization of the pro-aminopeptidase from Aeromonas caviae T-64

Bioscience, Biotechnology and Biochemistry

Volumn 65, Issue 2, 2001, Pages 420-423

  Zhang, Zhen Zhong ^a   Nirasawa, Satoru ^a   Nakajima, Yoshiaki ^a   Yoshida, Michiteru ^b   Kusakabe, Isao ^c   Hayashi, Kiyoshi ^a  

^a NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

^b TOKYO UNIVERSITY OF SCIENCE   (Japan)

^c UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

Aeromonas caviae; Aminopeptidase; Enzyme stability; Pro enzyme; Substrate specificity

Indexed keywords

1,10 PHENANTHROLINE; 1,10-PHENANTHROLINE; AMINOPEPTIDASE; BESTATIN; DRUG DERIVATIVE; EDETIC ACID; ENZYME PRECURSOR; LEUCINE; OLIGOPEPTIDE; PHENANTHROLINE DERIVATIVE;

AEROMONAS; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; DRUG ANTAGONISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; HEAT; KINETICS; METABOLISM; PH;

AEROMONAS; AMINOPEPTIDASES; EDETIC ACID; ENZYME PRECURSORS; ENZYME STABILITY; HEAT; HYDROGEN-ION CONCENTRATION; KINETICS; LEUCINE; OLIGOPEPTIDES; PHENANTHROLINES; SUBSTRATE SPECIFICITY;

EID: 0035257587     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.420     Document Type: Article

References (12)

1. Izawa, N., Ishikawa, S., Tanokura, T., Ohta, K., and Hayashi, K., Purification and characterization of Aeromonas caviae aminopeptidase possessing debittering activity. J. Agric. Food Chem., 45, 4897-4902 (1997).
2. Izawa, N., Tokuyasu, K., and Hayashi, K., Debittering of protein hydrolysates using Aeromonas caviae aminopeptidase. J. Agric. Food Chem., 45, 543-545 (1997).
3. Izawa, N. and Hayashi, K., Cloning and nucleotide sequencing of the aminopeptidase gene from Aeromonas caviae T-64. J. Ferment. Bioeng., 82, 544-548 (1996).
4. Nirasawa, S., Nakajima, Y., Zhang, Z., Yoshida, M., and Hayashi, K., Intramolecular chaperone and inhibitor activities of a propeptide from a bacterial zinc aminopeptidase. Biochem. J., 341, 25-31 (1999).
5. Avilés, F. X., Vendrell, J., Guasch, A., Coll, M., and Huber, R., Advances in metallo-procarboxypeptidases. Eur. J. Biochem., 211, 381-389 (1993).
6. Uren, J. R. and Neurath, H., Intrinsic enzymatic activity of bovine procarboxypeptidase S5. Biochemistry, 13, 3512-3520 (1974).
7. Groves, W. E., Davis, Jr., F. C., and Sells, B. H., Spectrophotometric determination of microgram quantities of protein without nucleic acid interference. Anal. Biochem., 22, 195-210 (1968).
8. Gorden, M. J., Huang, X., Pentoney, S. L., and Zare, R. N., Capillary electrophoresis. Science, 242, 224-228 (1988).
9. Bergman, T., Agerberth, B., and Jornvall, H., Direct analysis of peptides and amino acids from capillary electrophoresis. FEBS Lett., 283, 100-103 (1991).
10. Suda, H., Aoyagi, T., Takeuchi, T., and Umezawa, H., Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer. Arch. Biochem. Biophys., 177, 196-200 (1976).
11. Vilanova, M., Burgos, F. J., Cuchillo, C. M., and Aviles, F. X., The properties of the complex between ribsomal protein L2 and tRNA. FEBS Lett., 191, 273-277 (1985).
12. Bazzone, T. J. and Vallee, B. L., Bovine procarboxypeptidase A: kinetics of peptide and ester hydrolysis. Biochemistry, 4, 868-875 (1976).