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

BRENDA support

Literature summary for 1.2.7.1 extracted from

  • Wang, Q.; Wang, Q.; Tong, W.; Bai, X.; Chen, Z.; Zhao, J.; Zhang, J.; Liu, S.
    Regulation of enzyme activity of alcohol dehydrogenase through its interactions with pyruvate-ferredoxin oxidoreductase in Thermoanaerobacter tengcongensis (2012), Biochem. Biophys. Res. Commun., 417, 1018-1023.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Caldanaerobacter subterraneus subsp. tengcongensis Q8RCI3 subunit PorA
-
Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 Q8RCI3 subunit PorA
-

Synonyms

Synonyms Comment Organism
TTE0445
-
Caldanaerobacter subterraneus subsp. tengcongensis

General Information

General Information Comment Organism
physiological function Zn-dependent dehydrogenase 2-ADH, pyruvate-ferredoxin oxidoreductase PFOR and several glycolytic enzymes coexist in a protein complex. Native 2-ADH is present in two forms, PFOR-bound and PFOR-free. The enzyme activity of 2-ADH is inhibited in a non-competitive mode by PFOR, implying the interaction of 2-ADH and PFOR negatively regulate alcohol formation Caldanaerobacter subterraneus subsp. tengcongensis