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Titolo:
PURIFICATION, CHARACTERIZATION AND PARTIAL AMINO-ACID-SEQUENCES OF A NOVEL CEPHALOSPORIN-C DEACETYLASE FROM BACILLUS-SUBTILIS
Autore:
TAKIMOTO A; MITSUSHIMA K; YAGI S; SONOYAMA T;
Indirizzi:
SHIONOGI & CO LTD,DIV MFG,BIOPROC RES & DEV,2-5-1 MISHIMA SETTSU OSAKA 566 JAPAN
Titolo Testata:
Journal of fermentation and bioengineering
fascicolo: 1, volume: 77, anno: 1994,
pagine: 17 - 22
SICI:
0922-338X(1994)77:1<17:PCAPAO>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
15
Recensione:
Indirizzi per estratti:
Citazione:
A. Takimoto et al., "PURIFICATION, CHARACTERIZATION AND PARTIAL AMINO-ACID-SEQUENCES OF A NOVEL CEPHALOSPORIN-C DEACETYLASE FROM BACILLUS-SUBTILIS", Journal of fermentation and bioengineering, 77(1), 1994, pp. 17-22

Abstract

Cephalosporin-C deacetylase [EC 3.1.1.41] was purified electrophoretically to homogeneity from the newly isolated Bacillus subtilis SHS 0133 (FERM BP-2755). The enzyme was purified about 27-fold with a yield of 9 % and a specific activity of 187.4 U/mg protein. The native enzyme(molecular weight, 280,000) was composed of eight identical subunits with apparent molecular weights of 35,000. The cephalosporin-C deacetylase was stable up to 60-degrees-C for 30 min at pH 7.0. The enzyme exhibited Michaelis-Menten kinetics with the substrates cephalosporin C,7-aminocephalosporanic acid (7-ACA) and p-nitrophenyl acetate; the K(m) values were 24.0, 7.9 and 1.0 mM, respectively. One of the reactionproducts from 7-ACA, deacetyl-7-ACA, was a weak noncompetitive inhibitor and other product, acetate, was a weak competitive inhibitor; the K(i) values were 171 and 290 mM, respectively. However, these weak product inhibitors did not prevent the completion of the deacetylation of7-ACA. The pI value of the enzyme was determined to be 5.3 using isoelectric focusing. The observed data indicate that the enzyme is different from known cephalosporin-C deacetylases. In addition, amino acid sequencing of the N-terminus and Achromobacter proteinase 1-digested peptides yielded no sequences with similarities to other known proteins by a computer search.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 11:45:02