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Literature summary 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)

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

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.5 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 ?
-
 ?
1.1.5.5 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

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.5 additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Gluconobacter oxydans ?
-
 ?
1.1.5.5 additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acetobacter pasteurianus ?
-
 ?
1.1.5.5 additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acidomonas methanolica ?
-
 ?
1.1.5.5 additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Gluconacetobacter polyoxogenes ?
-
 ?
1.1.5.5 additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acetobacter aceti ?
-
 ?
1.1.5.5 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 ?
-
 ?
1.1.5.5 additional information the quinohemoprotein is able to oxidize alcohols, structure-function relationship, overview Acetobacter pasteurianus SKU1108 ?
-
 ?
1.1.5.5 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

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

Synonyms

EC Number Synonyms Comment Organism
1.1.5.5 ADHIIB
-
-
1.1.5.5 ADHIIG
-
-
1.1.5.5 alcohol dehydrogenase
-
-
1.1.5.5 BOH
-
-
1.1.5.5 GLDH
-
-
1.1.5.5 glycerol dehydrogenase
-
-
1.1.5.5 lupanine hydroxylase (PQQ/heme c)
-
-
1.1.5.5 PEGDH
-
-
1.1.5.5 polyethyleneglycol dehydrogenase
-
-
1.1.5.5 polypropyleneglycol dehydrogenase
-
-
1.1.5.5 polyvinylalcohol dehydrogenase
-
-
1.1.5.5 PPGDH
-
-
1.1.5.5 PVADH
-
-
1.1.5.5 quinohemoprotein alcohol dehydrogenase
-
 Gluconobacter oxydans
1.1.5.5 quinohemoprotein alcohol dehydrogenase
-
 Acetobacter pasteurianus
1.1.5.5 quinohemoprotein alcohol dehydrogenase
-
 Acidomonas methanolica
1.1.5.5 quinohemoprotein alcohol dehydrogenase
-
 Gluconacetobacter polyoxogenes
1.1.5.5 quinohemoprotein alcohol dehydrogenase
-
 Acetobacter aceti
1.1.5.5 quinoprotein ethanol dehydrogenase
-
-
1.1.5.5 tetrahydrofurfuryl alcohol dehydrogenase
-
-
1.1.5.5 THFADH
-
-
1.1.5.5 type I ADH (PQQ)
-
-
1.1.5.5 type II ADH
-
-
1.1.5.5 type II ADH (PQQ/heme c)
-
-
1.1.5.5 type III ADH (PQQ/heme c /3 hemes c)
-
-
1.1.5.5 vanillyl alcohol dehydrogenase
-
-
1.1.5.11 1-butanol dehydrogenase
-
-
1.1.99.12 sorbose/sorbosone dehydrogenase
-
-

Cofactor

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