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Titolo:
OVEREXPRESSION, PURIFICATION, AND CHARACTERIZATION OF UDP-N-ACETYLMURAMYL - L-ALANINE LIGASE FROM ESCHERICHIA-COLI
Autore:
GUBLER M; APPOLDT Y; KECK W;
Indirizzi:
HOFFMANN LA ROCHE AG,PHARMACEUT RES,DEPT INFECT DIS,ROOM 70-103 CH-4002 BASEL SWITZERLAND
Titolo Testata:
Journal of bacteriology
fascicolo: 3, volume: 178, anno: 1996,
pagine: 906 - 910
SICI:
0021-9193(1996)178:3<906:OPACOU>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL WALL PEPTIDOGLYCAN; ADDING ENZYME; OVER-PRODUCTION; D-GLUTAMATE; PEPTIDE; PRECURSORS; MUREIN; STEPS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
M. Gubler et al., "OVEREXPRESSION, PURIFICATION, AND CHARACTERIZATION OF UDP-N-ACETYLMURAMYL - L-ALANINE LIGASE FROM ESCHERICHIA-COLI", Journal of bacteriology, 178(3), 1996, pp. 906-910

Abstract

UDP-N-acetylmuramyl: L-alanine ligase from Escherichia coli was overexpressed more than 600-fold and purified to near homogeneity. The purified enzyme was found to ligate L-alanine, L-serine, and glycine, as well as the nonnatural amino acid beta-chloro-L-alanine, to UDP-N-acetylmuramic acid. On the basis of (i) the specificity constants of the enzyme determined for L-alanine, L-serine, and glycine and (ii) the levels of these amino acids in the intracellular pool, it was calculated that the rates of incorporation of L-serine and glycine into peptidoglycan precursor metabolites could maximally amount to 0.1 and 0.5%, respectively, of the rate of L-alanine incorporation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:25:17