The amino acid sequences of carboxypeptidases I and II from Aspergillus niger and their stability in the presence of divalent cations

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1387, Issue 1-2, 1998, Pages 369-377

  Svendsen, Ib ^a   Dal Degan, Florence ^b  

^a CARLSBERG LABORATORY   (Denmark)

^b DANISH INSTITUTE OF AGRICULTURAL SCIENCES   (Denmark)

Author keywords

Amino acid sequence; Aminolysis; Enzyme; Serine carboxypeptidase; Substrate binding site

Indexed keywords

AMINO ACID; CALCIUM ION; CYANOGEN BROMIDE; DISULFIDE; DIVALENT CATION; GLUTAMIC ACID; MAGNESIUM ION; SERINE CARBOXYPEPTIDASE;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS NIGER; NONHUMAN; PH; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ASPERGILLUS NIGER; BACTERIAL PROTEINS; CALCIUM; CARBOXYPEPTIDASES; CATIONS, DIVALENT; ENZYME STABILITY; GLYCOSYLATION; HYDROGEN-ION CONCENTRATION; ISOENZYMES; MAGNESIUM; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

ASPERGILLUS NIGER; PENICILLIUM JANTHINELLUM;

EID: 0032497335     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00135-6     Document Type: Article

References (25)

1. Svendsen I., Martin B.M., Viswanatha T., Johansen J.T. Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages. Carlsberg Res. Commun. 47:1982;15-28.
2. Valls L.A., Hunter C.P., Rothman J.H., Stevens T. Protein sorting in yeast: the location determination of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell. 48:1987;887-897.
3. Svendsen I., Hofmann T., Endrizzi J.A., Remington S.J., Breddam K. The primary structure of carboxypeptidase S1 from Penicillium janthinellum. FEBS Lett. 333:1993;39-43.
4. Sørensen S.B., Svendsen I., Breddam K. Primary structure of carboxypeptidase III from malted barley. Carlsberg Res. Commun. 54:1989;193-202.
5. Svendsen I., Day E.S. The primary structure of carboxypeptidase S3 from Penicillium janthinellum. FEBS Lett. 371:1995;1-3.
6. van den Hombergh J.P.T.W., Jarai G., Buxton F.P., Visser J. Cloning, characterization and expression of pepF, a gene encoding a serine carboxypeptidase from Aspergillus niger. Gene. 151:1994;73-79.
7. Sørensen S.B., Breddam K., Svendsen I. Primary structure of carboxypeptidase I from malted barley. Carlsberg Res. Commun. 51:1986;475-485.
8. Sørensen S.B., Svendsen I., Breddam K. Primary structure of carboxypeptidase II from malted barley. Carlsberg Res. Commun. 52:1987;285-295.
9. Breddam K., Sørensen S.B., Svendsen I. Primary structure and enzymatic properties of carboxypeptidase II from wheat bran. Carlsberg Res. Commun. 52:1987;297-311.
10. Endrizzi J.A., Breddam K., Remington S.J. 2.8-Å structure of yeast serine carboxypeptidase. Biochemistry. 33:1994;11106-11120.
11. Shilton B.H., Thomas D.Y., Cygler M. Crystal structure of Kex 1Dp, a prohormome-processing carboxypeptidase from Saccharomyces cerevisiae. Biochemistry. 36:1997;9002-9012.
12. Liao D.-I., Breddam K., Sweet R.M., Bullock T., Remington S.J. Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution. Biochemistry. 31:1992;9796-9812.
13. Rudenko G., Bonten E., d'Azzo A., Hol W.G. Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism. Structure. 3:1995;1249-1259.
14. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J., Sussman J.L., Verschueren K.H.G., Goldman A. The alpha/beta hydrolase fold. Protein Eng. 5:1992;197-211.
15. Breddam K. Serine carboxypeptidases. A review. Carlsberg Res. Commun. 51:1986;83-128.
16. Dal Degan F., Ribadeau-Dumas B., Breddam K. Purification and characterization of two serine carboxypeptidases from Aspergillus niger and their use in C-terminal sequencing of proteins and peptide synthesis. Appl. Environ. Microbiol. 58:1992;2144-2152.
17. Svendsen I., Breddam K. Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. Eur. J. Biochem. 204:1992;165-171.
18. Ballance G.M., Svendsen I. Purification and amino acid sequence determination of an endo-1,3-beta-glucanase from barley. Carlsberg Res. Commun. 53:1988;395-410.
19. Leu substrate preference of carboxypeptidase Y by rational design based on known primary and tertiary structures of serine carboxypeptidases. Biochemistry. 34:1995;15689-15699.
20. Chiba Y., Midorikawa T., Ichishima E. Cloning and expression of the carboxypeptidase gene from Aspergillus saitoi and determination of the catalytic residues by site directed mutagenesis. Biochem. J. 308:1995;405-409.
21. Martineau P., guillet J.-G., Leclerc C., Hofnung M. Expression of heterologous peptides at two permissive sites of the MalE protein: antigenicity and immunogenicity of foreign B and T cell epitopes. Gene. 113:1992;35-46.
22. Olesen K., Mortensen U.H., Aasmul-Olsen S., Kiellandt-Brandt M.C., Remington S.J., Breddam K. The activity of carboxypeptidase Y toward substrates with basic P1 amino acid residues is drastically increased by mutational replacement of leucine 178. Biochemistry. 33:1994;11121-11126.
23. Stennicke H.R., Mortensen U.H., Christensen U., Remington S.J., Breddam K. Effects of introduced aspartic and glutamic acid residues on the P1′ substrate specificity, pH dependence and stability of carboxypeptidase Y. Protein Eng. 7:1994;911-916.
24. Olesen K., Breddam K. Substrates with charged P1 residues are efficiently hydrolyzed by serine carboxypeptidases when S3-P1 interactions are facilitated. Biochemistry. 36:1997;12235-12241.
25. Sørensen S.B., Breddam K. The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S1′ binding pocket. Protein Sci. 6:1997;2227-2232.