Literature DB >> 3153617

Enzyme specialization during the evolution of amino acid biosynthetic pathways.

C Parsot1, I Saint-Girons, G N Cohen.   

Abstract

Amino acid sequence similarities detected between enzymes involved in methionine and cysteine biosynthesis, and between enzymes involved in the threonine, isoleucine and tryptophan biosynthetic pathways allow an experimental investigation of the mechanisms whereby metabolic pathways have evolved.

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Year:  1987        PMID： 3153617

Source DB:  PubMed          Journal:  Microbiol Sci        ISSN： 0265-1351


  4 in total

1.  Direct sulfhydrylation for methionine biosynthesis in Leptospira meyeri.

Authors:  J Belfaiza; A Martel; D Margarita; I Saint Girons
Journal:  J Bacteriol       Date:  1998-01       Impact factor: 3.490

2.  A novel aromatic alcohol dehydrogenase in higher plants: molecular cloning and expression.

Authors:  D Goffner; J Van Doorsselaere; N Yahiaoui; J Samaj; J Grima-Pettenati; A M Boudet
Journal:  Plant Mol Biol       Date:  1998-03       Impact factor: 4.335

3.  Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment.

Authors:  H Cherest; D Thomas; Y Surdin-Kerjan
Journal:  J Bacteriol       Date:  1993-09       Impact factor: 3.490

4.  Expression of the Vibrio cholerae gene encoding aldehyde dehydrogenase is under control of ToxR, the cholera toxin transcriptional activator.

Authors:  C Parsot; J J Mekalanos
Journal:  J Bacteriol       Date:  1991-05       Impact factor: 3.490
  4 in total

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