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Titolo:
STUDY OF THE OVERPRODUCED URIDINE-DIPHOSPHATE-N-ACETYLMURAMATE-L-ALANINE LIGASE FROM ESCHERICHIA-COLI
Autore:
LIGER D; MASSON A; BLANOT D; VANHEIJENOORT J; PARQUET C;
Indirizzi:
UNIV PARIS 11,URA 1131 CNRS,BATIMENT 432 F-91405 ORSAY FRANCE UNIV PARIS 11,URA 1131 CNRS F-91405 ORSAY FRANCE
Titolo Testata:
Microbial drug resistance
fascicolo: 1, volume: 2, anno: 1996,
pagine: 25 - 27
SICI:
1076-6294(1996)2:1<25:SOTOU>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
OVER-PRODUCTION; ADDING ENZYME; D-GLUTAMATE; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
11
Recensione:
Indirizzi per estratti:
Citazione:
D. Liger et al., "STUDY OF THE OVERPRODUCED URIDINE-DIPHOSPHATE-N-ACETYLMURAMATE-L-ALANINE LIGASE FROM ESCHERICHIA-COLI", Microbial drug resistance, 2(1), 1996, pp. 25-27

Abstract

The UDP-N-acetylmuramate:L-alanine ligase of Escherichia coli is responsible for the addition of the first amino acid of the peptide moietyin the assembly of the monomer unit of peptidoglycan. It catalyzes the formation of the amide bond between UDP-N-acetylmuramic acid (UDP-MurNAc) and L-alanine. The UDPMurNAc-L-alanine ligase was overproduced 2000-fold in a strain harboring a recombinant plasmid (pAM1005) with the murC gene under the control of the inducible promoter trc, The murC gene product appears as a 50-kDa protein accounting for ca, 50% of total cell proteins. A two-step purification led to 1 g of a homogeneous protein from an 18-liter culture, The N-terminal sequence of the purified protein correlated with the nucleotide sequence of the gene, The stability of the enzymatic activity is strictly dependent on the presence of 2-mercaptoethanol. The K-m values for substrates UDP-N-acetylmuramic acid, L-alanine, and ATP were estimated: 100, 20, and 450 mu M respectively. The specificity of the enzyme for its substrates was investigated with various analogues, Preliminary experiments attempting to elucidate the enzymatic mechanism were consistent with the formation of an acylphosphate intermediate.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 00:13:09