EC 1.1.2.B3: quinoprotein methanol dehydrogenase (cytochrome c559)

This is an abbreviated version!
For detailed information about quinoprotein methanol dehydrogenase (cytochrome c559), go to the full flat file.

Reaction

Synonyms

exaA, More, PedE, PedH, PQQ-alcohol dehydrogenase, PQQ-linked alcohol dehydrogenase, pyrroloquinoline quinone -dependent quinoprotein ethanol dehydrogenase, QEDH, quinoprotein ethanol 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.B3 quinoprotein methanol dehydrogenase (cytochrome c559)

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All data fields related to EC 1.1.2.B3

Results	in table
2	Activating Compound
3	AA Sequence
4	Cloned(Commentary)
5	Cofactor
10	KM Value [mM]
1	Localization
1	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
4	Organism
4	Protein Variants
1	Reaction
4	Reference
10	Specific Activity [micromol/min/mg]
10	Substrates and Products (Substrate)
2	Subunits
13	Synonyms
1	Systematic Name

Natural Substrates Products

Natural Substrates Products on EC 1.1.2.B3 - quinoprotein methanol dehydrogenase (cytochrome c559)

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

alcohol + cytochrome c550

aldehyde + reduced cytochrome c550

Pseudomonas aeruginosa

Q9Z4J7

690646

Substrates: the unusual disulfide ring between the adjacent cysteine residues C105 and C106 is essential for efficient electron transfer at pH 7 from quinoprotein ethanol dehydrogenase to its natural electron acceptor cytochrome c550
Products: -

?

ethanol + ferricytochrome c550

acetaldehyde + ferrocytochrome c550

Pseudomonas aeruginosa

Q9Z4J7

688852

Substrates: regulation of ethanol-oxidation system in Pseudomonas aeruginosa
Products: -

?

phenylethanol + ferricytochrome c

phenylacetaldehyde + ferrocytochrome c

Pseudomonas putida

B1N7J0, B1N7J5

686425

Substrates: PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome
Products: -

?