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evolution
CCU55317
high similarity between genes encoding subunits I and II of PQQ-ADH
evolution
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high similarity between genes encoding subunits I and II of PQQ-ADH
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malfunction
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exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
malfunction
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inactivation of PA1982 by insertion mutagenesis results in inability of the mutant to utilise ethanol and in reduced growth on geraniol. Growth on ethanol is restored by transferring an intact copy of the PA1982 gene into the mutant
malfunction
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mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
malfunction
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mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
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malfunction
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mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
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malfunction
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exaA2 and exaA3 mutants are less competitive than the wild type during colonization of rice roots
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malfunction
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mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
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malfunction
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mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
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malfunction
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mutant strains defective in the adhS gene of Acetobacter pasteurianus lose ADH activity because they produce only the subunit II but fail to produce the subunit I as well as the subunit III
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing Q in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing Q in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinnone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
-
metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overvoew
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview. Model for the intramolecular electron transport of PQQ-ADH, overview
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metabolism
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ethanol is oxidized to acetic acid by a sequential action of PQQ-ADH and membrane-bound aldehyde dehydrogenase, EC 1.1.1.2, reducing ubiquinone in the cytoplasmic membrane, overview
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physiological function
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ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
physiological function
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the PQQ-dependent alcohol dehydrogenase of Pseudomonas aeruginosa functions in ethanol metabolism and is involved in catabolism of acyclic terpenes, overview
physiological function
reduced expression of the transcriptional regulator C6TF leads to reduced expression of genes for polyketide synthase PKS2, P450, a cytochrome P450 monoxygenase, YogA, an alcohol dehydrogenase/quinone reductase, RTA1, a lipid transport exporter superfamily member and MFS, a Major Facilitator Superfamily transporter, as well as a marked reduction in phomenoic acid production
physiological function
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the enzyme plays an important role in the catabolism of alcohols in bacteria. Inactivation of exaA affects the growth of Azospirillum brasilense on glycerol
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
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physiological function
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ethanol is an important carbon source for the endophytic life of Azoarcus sp. in Oryza sativa roots
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain
-
physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
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physiological function
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the enzyme plays an important role in the catabolism of alcohols in bacteria. Inactivation of exaA affects the growth of Azospirillum brasilense on glycerol
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
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physiological function
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reduced expression of the transcriptional regulator C6TF leads to reduced expression of genes for polyketide synthase PKS2, P450, a cytochrome P450 monoxygenase, YogA, an alcohol dehydrogenase/quinone reductase, RTA1, a lipid transport exporter superfamily member and MFS, a Major Facilitator Superfamily transporter, as well as a marked reduction in phomenoic acid production
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physiological function
-
PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism. The subunit III seems to work as a molecular chaperone for folding and/or maturation of the subunit I
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physiological function
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PQQ-ADH functions as the primary dehydrogenase in the ethanol oxidation respiratory chain. The PQQ-ADH has a central role in vinegar production by the organism
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additional information
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Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
additional information
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Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
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