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Literature summary for 1.2.1.95 extracted from

  • Guo, S.; Bhattacharjee, J.K.
    Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe (2004), Yeast, 21, 1279-1288.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
G910A mutation in the activation domain (IGGHSI), no activity Schizosaccharomyces pombe
additional information enzyme Lys1 is active when expressed in Escherichia coli and exhibits significant alpha-aminoadipate reductase activity without the addition of CoA or Schizosaccharomyces pombe phosphopantetheinyl transferase Schizosaccharomyces pombe
S913A mutation in the activation domain (IGGHSI), no activity Schizosaccharomyces pombe
S913T mutation in the activation domain (IGGHSI), no activity Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe P40976
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification enzyme Lys1 is active when expressed in Escherichia coli and exhibits significant alpha-aminoadipate reductase activity without the addition of CoA or Schizosaccharomyces pombe phosphopantetheinyl transferase Schizosaccharomyces pombe