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1.1.2.8: alcohol dehydrogenase (cytochrome c)

This is an abbreviated version!
For detailed information about alcohol dehydrogenase (cytochrome c), go to the full flat file.

Word Map on EC 1.1.2.8

Reaction

a primary alcohol
+
2 ferricytochrome c
=
an aldehyde
+ 2 ferrocytochrome c + 2 H+

Synonyms

Ca2+-dependent PQQ-ADH, EC 1.1.99.8, EDH, ethanol dehydrogenase, exaA, exaF, PedE, PedH, PpADH, PP_2674, PP_2679, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-dependent alcohol dehydrogenase, PQQ-dependent type I alcohol dehydrogenase, PQQ-DH9, pyrroloquinoline quinone ethanol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenases, pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.2 With a cytochrome as acceptor
                1.1.2.8 alcohol dehydrogenase (cytochrome c)

Crystallization

Crystallization on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alignment with the amino acid sequence of the large subunit of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens. The amino acid residues involved in the binding of pyrroloquinoline quinone and Ca2+ at the active site are conserved
diffraction to beyond 2.5 A, space group R3
-
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
-