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Information on EC 1.1.2.6 - polyvinyl alcohol dehydrogenase (cytochrome)
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EC Tree
1.1.2.6 polyvinyl alcohol dehydrogenase (cytochrome)IUBMB Comments
A quinoprotein. The enzyme is involved in bacterial polyvinyl alcohol degradation. Some Gram-negative bacteria degrade polyvinyl alcohol by importing it into the periplasmic space, where it is oxidized by polyvinyl alcohol dehydrogenase, an enzyme that is coupled to the respiratory chain via cytochrome c. The enzyme contains a pyrroloquinoline quinone cofactor.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
poly(vinyl alcohol) dehydrogenase, pva-dh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, polyvinyl alcohol
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EC 1.1.99.23
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formerly
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poly(vinyl alcohol) dehydrogenase
PVA dehydrogenase
pvaA
PVADH
PVADH-S
pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase
PVA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
polyvinyl alcohol + ferricytochrome c = oxidized polyvinyl alcohol + ferrocytochrome c + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
polyvinyl alcohol:ferricytochrome-c oxidoreductase
A quinoprotein. The enzyme is involved in bacterial polyvinyl alcohol degradation. Some Gram-negative bacteria degrade polyvinyl alcohol by importing it into the periplasmic space, where it is oxidized by polyvinyl alcohol dehydrogenase, an enzyme that is coupled to the respiratory chain via cytochrome c. The enzyme contains a pyrroloquinoline quinone cofactor.
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CAS REGISTRY NUMBER
COMMENTARY
119940-13-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
polyvinyl alcohol + 2 ferricytochrome c
polyvinyl alcohol containing oxo-groups + 2 ferrocytochrome c + 2 H+
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the enzyme is involved in polyvinyl alcohol degradation
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?
polyvinyl alcohol + acceptor
polyvinyl alcohol containing beta-dioxo groups + reduced acceptor
polyvinyl alcohol + acceptor
polyvinyl alcohol containing oxo-groups + reduced acceptor
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pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase requires pyrroloquinoline quinone for polyvinyl alcohol dehydrogenation with phenazine methosulfate, phenazine ethosulfate, and 2,6-dichlorophenolindophenol as electron acceptors
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?
polyvinyl alcohol + ferricytochrome c
polyvinyl alcohol containing oxo-groups + ferrocytochrome c + 2 H+
polyvinyl alcohol + ferricytochrome c
polyvinyl alcohol containing oxo-groups + ferrocytochrome c + H+
cytochrome c involved in the pva operon is a physiological primary electron acceptor for PVADH
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?
polyvinyl alcohol + oxidized 2,6-dichlorophenolindophenol
polyvinyl alcohol containing oxo-groups + reduced 2,6-dichlorophenolindophenol
polyvinyl alcohol + oxidized acceptor
polyvinyl alcohol containing oxo-groups + reduced acceptor
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reaction in bacterial polyvinyl alcohol degradation, couples polyvinyl alcohol dehydrogenation to cytochrome reduction
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?
1,2-cyclohexanediol + oxidized 2,6-dichlorophenolindophenol
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1.8% of activity with polyvinyl alcohol
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?
1,2-cyclohexanediol + oxidized 2,6-dichlorophenolindophenol
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1.8% of activity with polyvinyl alcohol
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?
1,3-butanediol + oxidized 2,6-dichlorophenolindophenol
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57% of activity with 2,4-pentanediol
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1,3-butanediol + oxidized 2,6-dichlorophenolindophenol
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57% of activity with 2,4-pentanediol
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?
1,3-cyclohexanediol + oxidized 2,6-dichlorophenolindophenol
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393% of activity with 2,4-pentanediol
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1,3-cyclohexanediol + oxidized 2,6-dichlorophenolindophenol
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393% of activity with 2,4-pentanediol
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1,3-cyclohexanediol + oxidized 2,6-dichlorophenolindophenol
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?
1,3-cyclohexanedione + reduced 2,6-dichlorophenolindophenol
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?
2,4-pentanediol + oxidized 2,6-dichlorophenolindophenol
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enzyme shows only activity against meso-2,4-pentanediol
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?
2,4-pentanediol + oxidized 2,6-dichlorophenolindophenol
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enzyme shows only activity against meso-2,4-pentanediol
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polyvinyl alcohol + acceptor
polyvinyl alcohol containing beta-dioxo groups + reduced acceptor
the enzyme introduces beta-dioxo groups into the polyvinyl alcohol molecule. The saturation level of beta-diketone groups introduced into polyvinyl alcohol is about 3.5% of the total vinyl alcohol units
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polyvinyl alcohol + acceptor
polyvinyl alcohol containing beta-dioxo groups + reduced acceptor
the enzyme introduces beta-dioxo groups into the polyvinyl alcohol molecule. The saturation level of beta-diketone groups introduced into polyvinyl alcohol is about 3.5% of the total vinyl alcohol units
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?
polyvinyl alcohol + ferricytochrome c
polyvinyl alcohol containing oxo-groups + ferrocytochrome c + 2 H+
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polyvinyl alcohol + ferricytochrome c
polyvinyl alcohol containing oxo-groups + ferrocytochrome c + 2 H+
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?
polyvinyl alcohol + oxidized 2,6-dichlorophenolindophenol
polyvinyl alcohol containing oxo-groups + reduced 2,6-dichlorophenolindophenol
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activity is 6.7fold higher than activity with 2,4-pentanediol
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polyvinyl alcohol + oxidized 2,6-dichlorophenolindophenol
polyvinyl alcohol containing oxo-groups + reduced 2,6-dichlorophenolindophenol
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increasing hydrophobicity of polyvinyl alcohol increases affinity and activity of the enzyme
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?
polyvinyl alcohol + oxidized 2,6-dichlorophenolindophenol
polyvinyl alcohol containing oxo-groups + reduced 2,6-dichlorophenolindophenol
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activity is 6.7fold higher than activity with 2,4-pentanediol
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polyvinyl alcohol + oxidized 2,6-dichlorophenolindophenol
polyvinyl alcohol containing oxo-groups + reduced 2,6-dichlorophenolindophenol
polyvinyl alcohol(117)
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additional information
?
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no activity with methanol, ethanol, 1-propanol, 1-butanol, 4-heptanol, 2-hexanol and 2-pentanol
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additional information
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the enzyme shows dehydrogenase activity with 2,5-hexanediol, 4-heptanol, 2-hexanol, and 2-pentanol at 20-45% of the activity with polyvinyl alcohol
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additional information
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no activity with methanol, ethanol, 1-propanol, 1-butanol, 4-heptanol, 2-hexanol and 2-pentanol
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additional information
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degradation of polyvinyl alcohol must be performed by periplasmic polyvinyl alcohol dehydrogenase after uptake into the periplasm. A specific ultrastructural change on the cell surface is induced by polyvinyl alcohol and enhances the uptake of polyvinyl alcohol in the Sphingopyxis sp. strain 113P3
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
polyvinyl alcohol + 2 ferricytochrome c
polyvinyl alcohol containing oxo-groups + 2 ferrocytochrome c + 2 H+
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the enzyme is involved in polyvinyl alcohol degradation
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?
polyvinyl alcohol + ferricytochrome c
polyvinyl alcohol containing oxo-groups + ferrocytochrome c + H+
cytochrome c involved in the pva operon is a physiological primary electron acceptor for PVADH
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?
polyvinyl alcohol + oxidized acceptor
polyvinyl alcohol containing oxo-groups + reduced acceptor
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reaction in bacterial polyvinyl alcohol degradation, couples polyvinyl alcohol dehydrogenation to cytochrome reduction
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?
additional information
?
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degradation of polyvinyl alcohol must be performed by periplasmic polyvinyl alcohol dehydrogenase after uptake into the periplasm. A specific ultrastructural change on the cell surface is induced by polyvinyl alcohol and enhances the uptake of polyvinyl alcohol in the Sphingopyxis sp. strain 113P3
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
cytochrome c involved in the pva operon is a physiological primary electron acceptor for polyvinyl-alcohol dehydrogenase
pyrroloquinoline quinone
enzyme expressed in Escherichia coli requires pyrroloquinoline quinone for activity
pyrroloquinoline quinone
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functions as a coenzyme, mutant strain NDl (a polyvinyl alcohol oxidase-deficient mutant of Pseudomonas sp. strain VM15C) grows on polyvinyl alcohol and required PQQ for utilization of polyvinyl alcohol as an essential growth factor
pyrroloquinoline quinone
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the enzyme purified in presence of EDTA shows no activity until pyrroloquinoline quinone, Ca2+, Mg2+ are added
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
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stimulates, the enzyme purified in presence of EDTA shows no activity until pyrroloquinoline quinone, Ca2+, Mg2+ are added
Mg2+
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stimulating effect is far less than with Ca2+, the enzyme purified in presence of EDTA shows no activity until pyrroloquinoline quinone, Ca2+, Mg2+ are added
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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effect of saponification degree and ethylene contents of polyvinyl acohol-related polymers, effect of polymerization degree of polyvinyl acohol-related polymers, effect on tacticity of polyvinyl acohol-related polymers, Km-values in mg/ml
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain VM15C, strain NDl (a polyvinyl alcohol oxidase-deficient mutant of Pseudomonas sp. strain VM15C)
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brenda
the gene encoding the enzyme is located in the pva operon
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the gene pvaB encodes oxidized polyvinyl alcohol hydrolase and forms an operon with the polyvinyl alcohol dehydrogenase gene pvaA
metabolism
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the gene pvaB encodes oxidized polyvinyl alcohol hydrolase and forms an operon with the polyvinyl alcohol dehydrogenase gene pvaA
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physiological function
the cytochrome c involved in the pva operon is a physiological primary electron acceptor for PVADH, and PVA dehydrogenation is linked with the respiratory chain in Sphingopyxis sp. strain 113P3
physiological function
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the enzyme is involved in polyvinyl alcohol degradation
Show AA Sequence and Transmembrane Helices (105 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
pva operon, DNA and amino acid sequence determination and analysis of the complete operon in strain 113P3, genetic organization, overview
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recombinant PVADH tagged with hexahistidine is expressed in Escherichia coli. The three genes encoding oxidized polyvinyl alcohol hydrolase (EC 3.7.1.7), poly(vinyl alcohol) dehydrogenase and cytochrome c are expressed constitutively and form an operon
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimao, M.; Onishi, S.; Kato, N.; Sakazawa, C.
Pyrroloquinoline quinone-dependent cytochrome reduction in polyvinyl alcohol-degrading Pseudomonas sp. strain VM15C
Appl. Environ. Microbiol.
55
275-278
1989
Pseudomonas sp.
brenda
Shimao, M.; Ninomiyaaa, K.; Kuno, O.; Kato, N.; Sakazawa, C.
Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C
Appl. Environ. Microbiol.
51
268-275
1986
Pseudomonas sp., Pseudomonas sp. VM15C
brenda
Hatanaka, T.; Asahi, N.; Tsuji, M.
Purification and characterization of poly(vinyl alcohol) dehydrogenase from Pseudomonas sp. 113P3
Biosci. Biotechnol. Biochem.
59
1813-1816
1995
Pseudomonas sp., Pseudomonas sp. 113P3
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brenda
Hatanaka, T.; Kawahara, T.; Asahi, N.; Tsuji, M.
Effects of the structure of poly(vinyl alcohol) on the dehydrogenation reaction by poly(vinyl alcohol) dehydrogenase from Pseudomonas sp. 113P3
Biosci. Biotechnol. Biochem.
59
1229-1231
1995
Pseudomonas sp., Pseudomonas sp. 113P3
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brenda
Shimao, M.; Tamogami, T.; Nishi, K.; Harayama, S.
Cloning and characterization of the gene encoding pyrroloquinoline quinone-dependent poly(vinyl alcohol) dehydrogenase of Pseudomonas sp. strain VM15C
Biosci. Biotechnol. Biochem.
60
1056-1062
1996
Pseudomonas sp. (P77931), Pseudomonas sp., Pseudomonas sp. VM15C (P77931)
brenda
Shimao, M.; Tamogami, T.; Kishida, S.; Harayama, S.
The gene pvaB encodes oxidized polyvinyl alcohol hydrolase of Pseudomonas sp. strain VM15C and forms an operon with the polyvinyl alcohol dehydrogenase gene pvaA
Microbiology
146
649-657
2000
Pseudomonas sp. (P77931), Pseudomonas sp. VM15C (P77931)
brenda
Hirota-Mamoto, R.; Nagai, R.; Tachibana, S.; Yasuda, M.; Tani, A.; Kimbara, K.; Kawai, F.
Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase
Microbiology
152
1941-1949
2006
Sphingopyxis sp. (Q588Z1)
brenda
Mamoto, R.; Hu, X.; Chiue, H.; Fujioka, Y.; Kawai, F.
Cloning and expression of soluble cytochrome c and its role in polyvinyl alcohol degradation by polyvinyl alcohol-utilizing Sphingopyxis sp. strain 113P3
J. Biosci. Bioeng.
105
147-151
2008
Sphingopyxis sp. (Q588Z1)
brenda
Kawai, F.; Hu, X.
Biochemistry of microbial polyvinyl alcohol degradation
Appl. Microbiol. Biotechnol.
84
227-237
2009
Sphingopyxis sp.
brenda
Hu, X.; Mamoto, R.; Shimomura, Y.; Kimbara, K.; Kawai, F.
Cell surface structure enhancing uptake of polyvinyl alcohol (PVA) is induced by PVA in the PVA-utilizing Sphingopyxis sp. strain 113P3
Arch. Microbiol.
188
235-241
2000
Sphingopyxis sp.
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brenda
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