Literature DB >> 363710

The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin.

P A Briley, L Sibilli, M A Chalvignac, P Cossart, G Le Bras, A De Wolf, G N Cohen.   

Abstract

The sequence of the first 25 residues of the homoserine dehydrogenase fragment, produced by limited proteolysis of aspartokinase I-homoserine dehydrogenase I with substilisin, has been determined. The sequence of a cyanogen bromide peptide (CB5, 59 residues), isolated from the entire protein, is also presented. Residues 1 to 18 of the subtilisin homoserine dehydrogenase fragment match the sequence 42 to 59 of peptide CB5.

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Year:  1978        PMID: 363710

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  5 in total

1.  A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein.

Authors:  C J Gallione; J K Rose
Journal:  J Virol       Date:  1985-05       Impact factor: 5.103

2.  Construction and expression of a hybrid plasmid containing the Escherichia coli thrA and thrB genes.

Authors:  P Cossart; M Katinka; M Yaniv; I Saint Girons; G N Cohen
Journal:  Mol Gen Genet       Date:  1979-08

3.  Nucleotide sequence of the thrA gene of Escherichia coli.

Authors:  M Katinka; P Cossart; L Sibilli; I Saint-Girons; M A Chalvignac; G Le Bras; G N Cohen; M Yaniv
Journal:  Proc Natl Acad Sci U S A       Date:  1980-10       Impact factor: 11.205

4.  The soluble glycoprotein of vesicular stomatitis virus is formed during or shortly after the translation process.

Authors:  L Graeve; C Garreis-Wabnitz; M Zauke; M Breindl; J Kruppa
Journal:  J Virol       Date:  1986-03       Impact factor: 5.103

5.  Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum.

Authors:  P Zagouras; A Ruusala; J K Rose
Journal:  J Virol       Date:  1991-04       Impact factor: 5.103

  5 in total

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