EC Number | Crystallization (Comment) | Organism |
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1.1.2.8 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.8 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
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1.1.2.8 | Pseudomonas aeruginosa | - |
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EC Number | Synonyms | Comment | Organism |
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1.1.5.5 | quinoprotein ethanol dehydrogenase | - |
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