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Literature summary for 1.1.2.8 extracted from

  • Keitel, T.; Diehl, A.; Knaute, T.; Stezowski, J.J.; Höhne, W.; Görisch, H.
    X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity (2000), J. Mol. Biol., 297, 961-974.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.6 A resolution, by molecular replacement. Eight W-shaped beta-sheet motifs are arranged circularly in a propeller-like fashion forming a disk-shaped superbarrel. The prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion. Most amino acid residues found in close contact with the prosthetic group pyrroloquinoline quinone and the Ca2+ are conserved between the quinoprotein ethanol dehydrogenase structure and that of the methanol dehydrogenases from Methylobacterium extorquens or Methylophilus W3A1. The main differences in the active-site region are a bulky tryptophan residue in the active-site cavity of methanol dehydrogenase, which is replaced by a phenylalanine and a leucine side-chain in the ethanol dehydrogenase structure and a leucine residue right above the pyrrolquinoline quinone group in methanol dehydrogenase which is replaced by a tryptophan side-chain. Both amino acid exchanges contribute to different substrate specificities of these otherwise very similar enzymes. In addition to the Ca2+ in the active-site cavity, ethanol dehydrogenase contains a second Ca2+-binding site at the N-terminus, which contributes to the stability of the native enzyme Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion.In addition, enzyme contains a second Ca2+-binding site at the N-terminus, which contributes to the stability of the native enzyme Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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