1.2.5.2: aldehyde dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about aldehyde dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.2.5.2
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1.2.5.2
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dehydrogenases
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quinoprotein
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synthesis
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ferricyanide
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acetobacter
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acetaldehyde
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pqq-adh
- 1.2.5.2
- dehydrogenases
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quinoprotein
- synthesis
- ferricyanide
- acetobacter
- acetaldehyde
- pqq-adh
Reaction
Synonyms
ADH I, ADH IIB, ADH IIG, aldehyde dehydrogenase (acceptor), ALDH, BOH, dehydrogenase, aldehyde (acceptor), EC 1.2.99.3, FOE, formaldehyde-oxidizing enzyme, glucose sorbosone dehydrogenase, NAD+-independent, PQQ-containing alcohol dehydrogenase, PQQ-AldDH, PQQ-AlDH, pyrroloquinoline quinone-dependent aldehyde dehydrogenase, quinohemoprotein dehydrogenase, Swit_4395, tetrahydrofurfuryl alcohol dehydrogenase
ECTree
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Cofactor
Cofactor on EC 1.2.5.2 - aldehyde dehydrogenase (quinone)
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cytochrome b
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the enzyme complex contains one cytochrome b
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cytochrome c
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the enzyme shows the typical absorption spectrum of c-type cytochrome
cytochrome c
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the smaller subunit bears three cytochromes c
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the enzyme contains one heme c group, and full reconstitution is achieved with 1 mol of pyrroloquinoline quinone/mol
heme c
isozyme ADH IIB is a quinohemoprotein dehydrogenase, determination of heme content, overview
heme c
isozymes ADH IIB and ADH IIG are quinohemoprotein dehydrogenases, while ADH I is a non-heme quinoprotein, determination of heme contents, overview
heme c
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the quinohemoprotein contains one covalently bound heme c per monomer
pyrroloquinoline quinone
PQQ, a prosthetic group, ADH I is a non-heme quinoprotein containing 2.2 mol of PQQ per mol of enzyme
pyrroloquinoline quinone
PQQ, a prosthetic group, isozyme ADH IIB is a quinohemoprotein dehydrogenase. ADH IIB contains 1.4 mol of PQQ per mol of enzyme on the basis of a molecular weight of 70000 Da
pyrroloquinoline quinone
PQQ, a prosthetic group, isozyme ADH IIG is a quinohemoprotein dehydrogenase. ADH IIG contains 1.2 mol of PQQ per mol of enzyme on the basis of a molecular weight of 70000 Da
pyrroloquinoline quinone
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the quinohemoprotein contains one pyrroloquinoline quinone per monomer
pyrroloquinoline quinone
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after reconstitution to the holoenzyme by the addition of pyrroloquinoline quinone, addition of substrate changes the absorption spectrum to that of reduced cytochrome c, indicating that the heme c group participates in the enzymic mechanism, one molecule of pyrroloquinoline quinone is bound per enzyme molecule
pyrroloquinoline quinone
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electrons removed from substrate by alcohol dehydrogenase complex are initially transferred to the pyrroloquinoline quinone centre and further tunnelled across four cytochromes c to the membrane ubiquinone
pyrroloquinoline quinone
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two molecules of pyrroloquinoline quinone per enzyme molecule
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ADH I shows no activity with NAD(P), potassium ferricyanide, or molecular oxygen as electron acceptors
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additional information
ADH I shows no activity with NAD(P), potassium ferricyanide, or molecular oxygen as electron acceptors
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additional information
ADH I shows no activity with NAD(P), potassium ferricyanide, or molecular oxygen as electron acceptors
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