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Information on EC 1.1.3.30 - polyvinyl-alcohol oxidase
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EC Tree
1.1.3.30 polyvinyl-alcohol oxidaseSpecify your search results
Word Map
- 1.1.3.30
-
pva-degrading
- sphingopyxis
- pqq
-
pyrroloquinoline
- quinone
-
symbiotic
-
symbionts
-
flask
-
quinone-dependent
-
shake
-
sphingomonads
-
biodegradability
-
pqq-binding
-
hexahistidine
-
cell-associated
-
beta-diketone
-
gly-x-ser-x-gly
- sludge
-
polypropylene
-
pqq-dependent
-
depolymerized
-
depolymerases
-
ppic9k
- pmsf
- diketone
-
dehydrogenation
-
low-molecular-weight
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
pvadh, pva oxidase, pva dehydrogenase, polyvinyl alcohol dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PVA oxidase
PVADH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
polyvinyl alcohol + O2 = oxidized polyvinyl alcohol + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
polyvinyl-alcohol:oxygen oxidoreductase
-
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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
1,3-butanediol + O2
1,3-butanedione + H2O2
-
3.8% of activity with polyvinyl alcohol
-
?
2,4-pentanediol + O2
2,4-pentanedione + H2O2
-
19.3% of activity with polyvinyl alcohol
-
?
2-butanol + O2
2-butanone + H2O2
-
47.3% of activity with polyvinyl alcohol
-
?
3-butanol + O2
3-butanone + H2O2
-
14.6% of activity with polyvinyl alcohol
-
?
3-heptanol + O2
3-heptanone + H2O2
-
68.8% of activity with polyvinyl alcohol
-
?
3-hexanol + O2
3-hexanone + H2O2
-
47.3% of activity with polyvinyl alcohol
-
?
4-decanol + O2
4-decanone + H2O2
-
100% of activity with polyvinyl alcohol
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
13.7% of activity with polyvinyl alcohol
-
?
cyclohexanol + O2
cyclohexanal + H2O2
-
41.8% of activity with polyvinyl alcohol
-
?
additional information
?
-
no activity with primary nor secondary alcohols
-
?
2,5-hexanediol + O2
2,5-hexanedione + H2O2
-
3.8% of activity with polyvinyl alcohol
-
?
2,5-hexanediol + O2
2,5-hexanedione + H2O2
-
4.9% of activity with polyvinyl alcohol
-
?
2-hexanol + O2
2-hexanone + H2O2
-
65.4% of activity with polyvinyl alcohol
-
?
2-hexanol + O2
2-hexanone + H2O2
-
101% of activity with polyvinyl alcohol
-
?
2-hexanol + O2
2-hexanone + H2O2
-
101% of activity with polyvinyl alcohol
-
?
2-pentanol + O2
2-pentanone + H2O2
-
36.3% of activity with polyvinyl alcohol
-
?
2-pentanol + O2
2-pentanone + H2O2
-
58% of activity with polyvinyl alcohol
-
?
2-pentanol + O2
2-pentanone + H2O2
-
58% of activity with polyvinyl alcohol
-
?
2-propanol + O2
acetone + H2O2
-
3.5% of activity with polyvinyl alcohol
-
?
2-propanol + O2
acetone + H2O2
-
4.9% of activity with polyvinyl alcohol
-
?
2-propanol + O2
acetone + H2O2
-
4.9% of activity with polyvinyl alcohol
-
?
4-heptanol + O2
4-heptanone + H2O2
-
75.1% of activity with polyvinyl alcohol
-
?
4-heptanol + O2
4-heptanone + H2O2
-
91% of activity with polyvinyl alcohol
-
?
4-heptanol + O2
4-heptanone + H2O2
-
91% of activity with polyvinyl alcohol
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
symbiotic biodegradation of polyvinyl alcohol, measured by hydrogen peroxide production
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
the enzyme is involved in polyvinyl alcohol-degradation
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
substrate PVA117
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
fluorescein-labelled and unlabelled polyvinyl alcohol, degradation after uptake into the periplasm, associated with ultrastructural changes of cell surface
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
pva operon characterized
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
the enzyme is involved in polyvinyl alcohol-degradation
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
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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 + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
the enzyme is involved in polyvinyl alcohol-degradation
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
the enzyme is involved in polyvinyl alcohol-degradation
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no requirement for pyrroloquinoline quinone (PQQ) as does the PQQ-dependent PVA dehydrogenase
-
additional information
-
no requirement for pyrroloquinoline quinone (PQQ) as does the PQQ-dependent PVA dehydrogenase
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
activates, the activation by Mg2+ is less than 80% of the activation by Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
essential for polyvinyl alcohol degradation, another yet unknown growth factor supplied by co-isolated Rhodococcus erythropolis strain
pyrroloquinoline quinone
absolutely required for activity, one mole of PQQ is bound to one mole of apoenzyme
pyrroloquinoline quinone
-
i.e. PQQ, supplemented with polyvinyl alcohol medium at 1 mg/l
additional information
-
the enzyme is induced by polyvinyl alcohol
-
additional information
-
the enzyme is induced by polyvinyl alcohol in strain O3, but is constitutive in strain VM15C
-
additional information
-
the enzyme is induced by polyvinyl alcohol
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0018
-
in association with the co-isolated Rhodococcus erythropolis strain, isolate able to degrade 500 mg of polyvinyl alcohol per litre in 2 weeks, no activity on 2-butanol, 2,4-pentanediol, 2-hexanol, 2-heptanol detected
additional information
additional information
-
degradation of polyvinyl alcohol measured by iodometry, polyvinyl alcohol oxidase assay, ultrastructural change on the cell surface in polyvinyl alcohol-containing media shown by Scanning electron microscopy, binding studies of fluorescein-labelled polyvinyl alcohol onto the cell surface, induction of structural surface changes by polyvinyl alcohol identifed
additional information
upstream and downstream regions of pva operon sequenced, transcript start and operon size, location on megaplasmid and constitutive expression shown, periplasmic enzyme activities from cells grown in polyvinyl alcohol medium and glucose medium compared, increased expression by addition of polyvinyl alcohol
additional information
-
upstream and downstream regions of pva operon sequenced, transcript start and operon size, location on megaplasmid and constitutive expression shown, periplasmic enzyme activities from cells grown in polyvinyl alcohol medium and glucose medium compared, increased expression by addition of polyvinyl alcohol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Rhodococcus erythropolis
but supports growth and degradation of polyvinyl alcohol by Sphingomonas sp.
-
-
brenda
in symbiotic culture with Pseudomonas putida during PVA utilization
-
-
brenda
CCM 7450, growth and PVA degradation supported by co-isolated strain Rhodococcus erythropolis OT3
-
-
brenda
reidentified from Sphingomonas sp. strain 113P3 by taxonomic analysis
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
strain BX1 grows on PVA as a mixed culture with another strain PN19. Strain BX1 has PVA oxidase activity but has no PQQ-dependent PVA-DH and the mixed culture accumulates depolymerized PVA in the culture supernatant
brenda
additional information
-
strain BX1 grows on PVA as a mixed culture with another strain PN19. Strain BX1 has PVA oxidase activity but has no PQQ-dependent PVA-DH and the mixed culture accumulates depolymerized PVA in the culture supernatant
brenda
additional information
-
the enzyme is induced by polyvinyl alcohol in strain O3, but is constitutive in strain VM15C
brenda
additional information
-
the organism grows on polyvinyl alcohol, n-butanol, n-pentanol, n-hexanol, n-heptanol, n-tridecanol, n-tetradecanol, and n-hexadecanol as sole carbon source, but not on aromatic and alkane compounds
brenda
additional information
-
the organism grows on polyvinyl alcohol, n-butanol, n-pentanol, n-hexanol, n-heptanol, n-tridecanol, n-tetradecanol, and n-hexadecanol as sole carbon source, but not on aromatic and alkane compounds
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
activity associated with cells of co-isolated degrader strain Rhodococcus erythropolis
-
brenda
-
membrane-bound amount depending on growth rate, 50% of enzyme activity is localized on cytoplasmic membrane
-
brenda
-
membrane-bound amount depending on growth rate, 50% of enzyme activity is localized on cytoplasmic membrane
-
brenda
-
membrane-bound amount depending on growth rate, 50% of enzyme activity is localized on cytoplasmic membrane
-
brenda
-
extracellular or cell-associated enzyme activity undetectable in strain 113P3
-
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
the enzyme possesses a conserved superbarrel domain SD, probable PQQ-binding amino acids in the SD and a hem-binding domain HBD
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
stable for 30 min, complete loss of activity after 30 min at 60°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant enzyme, 20 mM Tris/HCl buffer, pH 8.0, stable for more than a month
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli 44fold to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pvadh, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His6-tagged enzyme in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimao, M.; Nishimura, Y.; Kato, N.; Sakazawa, C.
Localization of polyvinyl alcohol oxidase produced by a bacterial symbiont, Pseudomonas sp. strain VM15C
Appl. Environ. Microbiol.
49
8-10
1985
Pseudomonas sp.
brenda
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
no activity in Pseudomonas sp., Pseudomonas sp., no activity in Pseudomonas sp. VM15C
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.
brenda
Kawagoshi, Y.; Fujita, M.
Purification and properties of polyvinyl alcohol oxidase with broad substrate range obtained from Pseudomonas vesicularis var. povalolyticus PH
World J. Microbiol. Biotechnol.
13
273-277
1997
Brevundimonas vesicularis
-
brenda
Yamatsu, A.; Matsumi, R.; Atomi, H.; Imanaka, T.
Isolation and characterization of a novel poly(vinyl alcohol)-degrading bacterium, Sphingopyxis sp. PVA3
Appl. Microbiol. Biotechnol.
72
804-811
2006
Sphingopyxis sp., Sphingopyxis sp. PVA3
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
Vaclavkova, T.; Ruzicka, J.; Julinova, M.; Vicha, R.; Koutny, M.
Novel aspects of symbiotic (polyvinyl alcohol) biodegradation
Appl. Microbiol. Biotechnol.
76
911-917
2007
Sphingomonas sp., no activity in Rhodococcus erythropolis
brenda
Hu, X.; Mamoto, R.; Fujioka, Y.; Tani, A.; Kimbara, K.; Kawai, F.
The pva operon is located on the megaplasmid of Sphingopyxis sp. strain 113P3 and is constitutively expressed, although expression is enhanced by PVA
Appl. Microbiol. Biotechnol.
78
685-693
2008
Sphingopyxis sp. (Q588Z1), 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
2007
Sphingopyxis sp.
brenda
Kawai, F.; Hu, X.
Biochemistry of microbial polyvinyl alcohol degradation
Appl. Microbiol. Biotechnol.
84
227-237
2009
Microbacterium barkeri, Paenibacillus amylolyticus, Bacillus megaterium, Brevundimonas vesicularis, Penicillium sp., Geotrichum sp., no activity in Alcaligenes faecalis, Pseudomonas sp., Sphingomonas sp., Streptomyces venezuelae, Sphingopyxis sp., no activity in Alcaligenes faecalis KK314, Brevundimonas vesicularis PD, Brevundimonas vesicularis PH, Streptomyces venezuelae GY1, Bacillus megaterium BX1, Geotrichum sp. WF9101, Microbacterium barkeri KCCM10507, Paenibacillus amylolyticus KCCM 10508, Penicillium sp. WSH02-21
brenda
Li, M.; Du, G.
Purification and enzymatic properties of polyvinyl alcohol dehydrogenase
Chin. J. Proc. Engin.
14
1015-1019
2014
Bacillus megaterium
-
brenda
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