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http://purl.uniprot.org/citations/7601127http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7601127http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7601127http://www.w3.org/2000/01/rdf-schema#comment"The UDP-N-acetylmuramate:L-alanine ligase of Escherichia coli was over-produced in strains harbouring recombinant plasmids bearing the murC gene under the control of the lac or trc promoter. Plasmid pAM1005, in which the promoter and ribosome-binding site region of murC were removed and in which the gene was directly under the control of promoter trc, led to a 2000-fold amplification of the L-alanine-adding activity after induction by isopropyl-thio-beta-D-galactopyranoside. The murC gene product was visualized as a 50-kDa protein accounting for approximately 50% of the cell protein. A two-step purification led to 1 g of a homogeneous protein from an 18-1 culture. The N-terminal sequence of the purified protein correlated with the nucleotide sequence of the murC gene. The presence of 2-mercaptoethanol and glycerol was essential for the stability of the enzyme. The Km values for UDP-N-acetylmuramic acid, L-alanine and ATP/Mg2+ were estimated at 100, 20 and 450 microM, respectively. Under the optimal in vitro conditions a turnover number of 928 min-1 was calculated and a copy number/cell of 600 could be roughly estimated. The specificity of the enzyme for its substrates was investigated with various analogues. The enzyme also catalysed the reverse reaction."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1995.0080i.x"xsd:string
http://purl.uniprot.org/citations/7601127http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1995.0080i.x"xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Blanot D."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Blanot D."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Liger D."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Liger D."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"van Heijenoort J."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"van Heijenoort J."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Parquet C."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Parquet C."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Masson A."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/author"Masson A."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/pages"80-87"xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/pages"80-87"xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/title"Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/title"Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/volume"230"xsd:string
http://purl.uniprot.org/citations/7601127http://purl.uniprot.org/core/volume"230"xsd:string