Article (Scientific journals)
The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G
Joris, Bernard; Van Beeumen, Jozef; Casagrande, Fabiana et al.
1983In European Journal of Biochemistry, 130 (1), p. 53-69
Peer Reviewed verified by ORBi
 

Files


Full Text
JORIS_1983_the-complete-amino.pdf
Publisher postprint (11.39 MB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
amino acid sequence; amino acids/analysis; carboxypeptidases/*analysis; cyanogen bromide; disulfides/analysis; muramoylpentapeptide carboxypeptidase/*analysis; peptide fragments/analysis; streptomyces/*enzymology
Abstract :
[en] The 22076-Mr Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces abuls G effectively catalyses the transfer of the N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolysing penicillin into penicilloate at a very low rate. This protein consists of 212 amino acid residues in a single polypeptide chain. The N terminus is partially blocked as a result of the cyclization of the dipeptide Asn-Gly into anhydroaspartylglycine imide. The protein has been fragmented by cyanogen bromide into five fragments whose sequences have been determined via appropriate subcleavages with various proteases. The ordering of the cyanogen bromide peptide fragments has been carried out (a) by submitting the S-carboxymethylated protein to complete tryptic digestion and labelling the methionine-containing peptides thus obtained with iodo[14C]-acetamide, and (b) by submitting to limited tryptic digestion the S-[2-(4'-pyridyl)ethyl]-cysteine protein whose amino groups have been blocked by reaction with exo-cis-3,6-endoxo-delta 4-tetrahydrophthalic anhydride prior to digestion. The protein contains six cysteine residues in the form of three disulfide bridges. No homology is found by comparing this peptidase with other Zn2+-containing enzymes (carboxypeptidase A, thermolysin, carbonic anhydrase B and alcohol dehydrogenase) and several completely or partially sequenced, serine-containing D-alanyl-D-alanine-cleaving peptidases and Zn2+/serine-containing beta-lactamases.
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Joris, Bernard ;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Van Beeumen, Jozef;  Rijksuniverstieit-Gent > Laboratorium voor Microbiologie en microbiele Genetica
Casagrande, Fabiana
Gerday, Charles ;  Université de Liège - ULiège > Relations académiques et scientifiques (Sciences)
Frère, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Language :
English
Title :
The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G
Publication date :
17 January 1983
Journal title :
European Journal of Biochemistry
ISSN :
0014-2956
eISSN :
1432-1033
Publisher :
Blackwell Science, Oxford, United Kingdom
Volume :
130
Issue :
1
Pages :
53-69
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 27 January 2011

Statistics


Number of views
84 (3 by ULiège)
Number of downloads
210 (4 by ULiège)

Scopus citations®
 
30
Scopus citations®
without self-citations
23
OpenCitations
 
34

Bibliography


Similar publications



Contact ORBi