Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.3.14 extracted from

  • Kwon, E.S.; Jeong, J.H.; Roe, J.H.
    Inactivation of homocitrate synthase causes lysine auxotrophy in copper/zinc-containing superoxide dismutase-deficient yeast Schizosaccharomyces pombe (2006), J. Biol. Chem., 281, 1345-1351.
    View publication on PubMed
Search for more literature for 2.3.3.14

Protein Variants

Protein Variants Comment Organism
additional information activity and protein level of homocitrate synthase are dramatically reduced upon depletion of CuZn-superoxide dismutase. Overexpression of the lys4 gene increases homocitrate synthase activity and is sufficient to suppress the lysine requirement of CuZn-superoxide dismutase-deficient cells Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Schizosaccharomyces pombe homocitrate synthase is a labile target for oxidative stress caused by CuZn-superoxide dismutase depletion ?
-
 ?

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
-
 enzyme expression is positively regulated by the putative transcriptional regulatr Phx1. Activity and protein level of homocitrate synthase are dramatically reduced upon depletion of CuZn-superoxide dismutase. Overexpression of the lys4 gene increases homocitrate synthase activity and is sufficient to suppress the lysine requirement of CuZn-superoxide dismutase-deficient cells
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information homocitrate synthase is a labile target for oxidative stress caused by CuZn-superoxide dismutase depletion Schizosaccharomyces pombe ?
-
 ?