Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.5.5 extracted from

  • Toyama, H.; Mathews, F.S.; Adachi, O.; Matsushita, K.
    Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology (2004), Arch. Biochem. Biophys., 428, 10-21.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons, phylogenetic tree Gluconobacter oxydans
sequence comparisons, phylogenetic tree Acetobacter pasteurianus
sequence comparisons, phylogenetic tree Acidomonas methanolica
sequence comparisons, phylogenetic tree Gluconacetobacter polyoxogenes
sequence comparisons, phylogenetic tree Acetobacter aceti

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Gluconobacter oxydans 16020
-
membrane
-
Acetobacter pasteurianus 16020
-
membrane
-
Acidomonas methanolica 16020
-
membrane
-
Gluconacetobacter polyoxogenes 16020
-
membrane
-
Acetobacter aceti 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Acetobacter pasteurianus by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles ?
-
?
additional information Acetobacter pasteurianus SKU1108 by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles ?
-
?

Organism

Organism UniProt Comment Textmining
Acetobacter aceti P18278
-
-
Acetobacter pasteurianus
-
-
-
Acetobacter pasteurianus SKU1108
-
-
-
Acidomonas methanolica
-
-
-
Gluconacetobacter polyoxogenes
-
-
-
Gluconobacter oxydans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Gluconobacter oxydans ?
-
?
additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acetobacter pasteurianus ?
-
?
additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acidomonas methanolica ?
-
?
additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Gluconacetobacter polyoxogenes ?
-
?
additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acetobacter aceti ?
-
?
additional information by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles Acetobacter pasteurianus ?
-
?
additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acetobacter pasteurianus SKU1108 ?
-
?
additional information by the defect of type III ADH in Acetobacter pasteurianus SKU1108, the strain turns out to grow even better than the wild strain in ethanol containing medium, where two NAD-dependent ADHs, present in only a small amount in the wild-type strain, are dramatically increased in the cytoplasm, concomitant to the increase of the key enzyme activities in TCA and glyoxylate cycles Acetobacter pasteurianus SKU1108 ?
-
?

Subunits

Subunits Comment Organism
More structure-function relationship, overview Gluconobacter oxydans
More structure-function relationship, overview Acetobacter pasteurianus
More structure-function relationship, overview Acidomonas methanolica
More structure-function relationship, overview Gluconacetobacter polyoxogenes
More structure-function relationship, overview Acetobacter aceti

Synonyms

Synonyms Comment Organism
ADHIIB
-
-
ADHIIG
-
-
alcohol dehydrogenase
-
-
BOH
-
-
GLDH
-
-
glycerol dehydrogenase
-
-
lupanine hydroxylase (PQQ/heme c)
-
-
PEGDH
-
-
polyethyleneglycol dehydrogenase
-
-
polypropyleneglycol dehydrogenase
-
-
polyvinylalcohol dehydrogenase
-
-
PPGDH
-
-
PVADH
-
-
quinohemoprotein alcohol dehydrogenase
-
Gluconobacter oxydans
quinohemoprotein alcohol dehydrogenase
-
Acetobacter pasteurianus
quinohemoprotein alcohol dehydrogenase
-
Acidomonas methanolica
quinohemoprotein alcohol dehydrogenase
-
Gluconacetobacter polyoxogenes
quinohemoprotein alcohol dehydrogenase
-
Acetobacter aceti
quinoprotein ethanol dehydrogenase
-
-
tetrahydrofurfuryl alcohol dehydrogenase
-
-
THFADH
-
-
type I ADH (PQQ)
-
-
type II ADH
-
-
type II ADH (PQQ/heme c)
-
-
type III ADH (PQQ/heme c /3 hemes c)
-
-
vanillyl alcohol dehydrogenase
-
-

Cofactor

Cofactor Comment Organism Structure
heme c type III ADH is a quinohemoprotein able to oxidize alcohols Gluconobacter oxydans
heme c type III ADH is a quinohemoprotein able to oxidize alcohols Acetobacter pasteurianus
heme c type III ADH is a quinohemoprotein able to oxidize alcohols Acidomonas methanolica
heme c type III ADH is a quinohemoprotein able to oxidize alcohols Gluconacetobacter polyoxogenes
heme c type III ADH is a quinohemoprotein able to oxidize alcohols Acetobacter aceti
pyrroloquinoline quinone PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview Gluconobacter oxydans
pyrroloquinoline quinone PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview Acetobacter pasteurianus
pyrroloquinoline quinone PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview Acidomonas methanolica
pyrroloquinoline quinone PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview Gluconacetobacter polyoxogenes
pyrroloquinoline quinone PQQ, type III ADH is a quinohemoprotein able to oxidize alcohols, PQQ binding structure and electron transfer reaction, overview Acetobacter aceti