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Literature summary extracted from

  • Irvin, S.D.; Bhattacharjee, J.K.
    A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms (1998), J. Mol. Evol., 46, 401-408.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.36 2-Hydroxy-3-carboxyadipate Saccharomyces cerevisiae enzyme is involved in the L-Lys biosynthesis via 2-aminoadipate pathway ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate Aspergillus nidulans enzyme is involved in the L-Lys biosynthesis via 2-aminoadipate pathway ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate Saccharomyces cerevisiae evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate Aspergillus nidulans evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate Methanocaldococcus jannaschii evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.36 Aspergillus nidulans
-
-
-
4.2.1.36 Methanocaldococcus jannaschii
-
-
-
4.2.1.36 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.36 2-Hydroxy-3-carboxyadipate enzyme is involved in the L-Lys biosynthesis via 2-aminoadipate pathway Saccharomyces cerevisiae ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate enzyme is involved in the L-Lys biosynthesis via 2-aminoadipate pathway Aspergillus nidulans ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea Saccharomyces cerevisiae ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea Aspergillus nidulans ?
-
?
4.2.1.36 2-Hydroxy-3-carboxyadipate evaluation of the possible evolutionary scenario for the origin of the Lys biosynthetic pathway by comparison of similarity of homoaconitate hydratase to isopropylmalate isomerase and iron-responsive element binding proteins from fungi and other eukaryotes, eubacteria, and archaea Methanocaldococcus jannaschii ?
-
?
4.2.1.36 2-hydroxybutane-1,2,4-tricarboxylate
-
Saccharomyces cerevisiae but-1-ene-1,2,4-tricarboxylate + H2O
-
?
4.2.1.36 2-hydroxybutane-1,2,4-tricarboxylate
-
Aspergillus nidulans but-1-ene-1,2,4-tricarboxylate + H2O
-
?
4.2.1.36 2-hydroxybutane-1,2,4-tricarboxylate
-
Methanocaldococcus jannaschii but-1-ene-1,2,4-tricarboxylate + H2O
-
?