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The primary structure of escherichia coli k 12 asparto kinase ec 2.7.2.4 homo serine dehydrogenase ec 1.1.1.3 part 1 distribution of the methioninyl residues and of the cysteinyl and tryptophanyl tryptic peptides


, : The primary structure of escherichia coli k 12 asparto kinase ec 2.7.2.4 homo serine dehydrogenase ec 1.1.1.3 part 1 distribution of the methioninyl residues and of the cysteinyl and tryptophanyl tryptic peptides. Biochimie (Paris) 59(11-12): 943-946

The distribution of the methionine, cysteine and tryptophan residues of E. coli aspartokinase [EC 2.7.2.4] I-homoserine dehydrogenase [EC 1.1.1.3] I is presented.

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Sibilli, L.; Cossart, P.; Chalvignac, M.A.; Briley, P.A.; Costrejean, J.M.; L.B.as, G.; Cohen, G.N., 1977: The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Distribution of the methioninyl residues and of the cysteinyl and tryptophanyl tryptic peptides. Biochimie 59(11-12): 943-946

Cossart-Gheerbrant, P.; Sibilli-Weill, L.; Briley, P.A.; Chalvignac, M.A.; Le-Bras, G.; Cohen, G.N., 1978: The primary structure of escherichia coli k 12 asparto kinase i ec 2.7.2.4 homo serine dehydrogenase i ec 1.1.1.3 isolation and characterization of the peptides produced by cyanogen bromide/. The aspartokinase I[EC 2.7.2.4]-homoserine dehydrogenase I [EC 1.1.1.3] from E. coli K12, composed of four identical subunits of MW 86,000, was carboxymethylated, fragmented by CNBr treatment and citraconylated. Using gel filtration, ion exchange...

Sibilli, L.; Le-Bras, G.; Cossart, P.; Chalvignac, M.A.; Le-Bras, G.; Briley, P.A.; Cohen, G.N., 1979: The primary structure of escherichia coli k 12 asparto kinase i ec 2.7.2.4 homo serine dehydrogenase i ec 1.1.1.3 sequence of cyanogen bromide peptide cb 3. The sequence of peptide CB 3 (79 residues) produced by CNBr cleavage of aspartokinase I-homoserine dehydrogenase I, was determined. This peptide belongs to the N-terminal region of the entire protein.

Dautry-Varsat, A.; Cohen, G.N., 1977: Proteolysis of the bi functional methionine repressible asparto kinase ec 2.7.2.4 ii homo serine dehydrogenase ec 1.1.1.3 ii of escherichia coli k 12 production of an active homo serine dehydrogenase fragment. The dimeric bifunctional enzyme aspartokinase [EC 2.7.2.4] II-homoserine dehydrogenase [EC 1.1.1.3] II (MW = 2 .times. 88,000) of E. coli K12 can be cleaved into 2 nonoverlapping fragments by limited proteolysis with subtilisin. These 2 fragments...

Fazel, A.; Guillou, Y.; Cohen, G.N., 1983: A hybrid proteolytic fragment of escherichia coli asparto kinase i ec 2.7.2.4 homo serine dehydrogenase i ec 1.1.1.3 structure inhibition pattern dissociation properties and generation of 2 homo dimers. A hybrid dimeric fragment of E. coli aspartokinase I-homoserine dehydrogenase I was purified and possesses aspartokinase and homoserine dehydrogenase activities and is rather stable in the presence of L-threonine. Its 2 activities are still inhibi...

Dautry-Varsat, A.; Sibilli-Weill, L.; Cohen, G.N., 1977: Subunit structure of the methionine repressible asparto kinase ii ec 2.7.2.4 homo serine dehydrogenase ii ec 1.1.1.3 from escherichia coli k 12. The quaternary structure of E. coli K12 aspartokinase II[EC 2.7.2.4]-homoserine dehydrogenaseII[EC 1.1.1.3] was examined. This multifunctional protein has a MW = 176,000. It is composed of 2 subunits having the same MW and the same charge. The res...

Zakin, M.M.; Duchange, N.; Ferrara, P.; Cohen, G.N., 1983: Nucleotide sequence of the met l gene of escherichia coli its product the bi functional asparto kinase ii ec 2.7.2.4 homo serine dehydrogenase ii ec 1.1.1.3 and the bi functional product of the thr a gene asparto kinase i homo serine dehydrogenase i derive from a common ancestor. The total nucleotide sequence (2427 nucleotides) of the metL gene of E. coli coding for the dimeric aspartokinase II-homoserine dehydrogenase II (809 amino acid residues, MW = 88,726/chain) is presented. Comparison of the translated sequence with...

Hirth C.G.; Veron M.; Villar Palasi C.; Hurion N.; Cohen G.N., 1975: The threonine sensitive homo serine dehydrogenase and asparto kinase activities of escherichia coli strain k 12 specific inactivation of the homo serine dehydrogenase activity by the affinity label 2 amino 4 oxo 5 chloro pentanoic acid. European Journal of Biochemistry 50(2): 425-430

Falcoz Kelly F.; Janin J.; Saari J.C.; Veron M.; Truffa Bachi P.; Cohen G.N., 1972: Revised structure of asparto kinase 1 homo serine dehydrogenase 1 of escherichia coli k 12 evidence for 4 identical subunits. European Journal of Biochemistry 28(4): 507-519

Truffa Bachi P.; Veron M.; Cohen G.N., 1974: Structure function and possible origin of a bi functional allo steric enzyme escherichia coli asparto kinase 1 homo serine dehydrogenase 1. Critical Reviews in Biochemistry 2(3): 379-415