Information on EC 1.1.3.30 - polyvinyl-alcohol oxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.1.3.30
-
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RECOMMENDED NAME
GeneOntology No.
polyvinyl-alcohol oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
polyvinyl alcohol + O2 = oxidized polyvinyl alcohol + H2O2
show the reaction diagram
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
-
-
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reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
polyvinyl-alcohol:oxygen oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
119940-13-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
no activity in Alcaligenes faecalis
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-
-
Manually annotated by BRENDA team
no activity in Alcaligenes faecalis KK314
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Manually annotated by BRENDA team
no activity in Pseudomonas sp.
strain N1
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-
Manually annotated by BRENDA team
no activity in Pseudomonas sp. VM15C
strain N1
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-
Manually annotated by BRENDA team
no activity in Rhodococcus erythropolis
but supports growth and degradation of polyvinyl alcohol by Sphingomonas sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene pvadh; gene pvadh or pvaA
SwissProt
Manually annotated by BRENDA team
polyvinyl alcohol dehydrogenase, part of pva operon
SwissProt
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-butanediol + O2
1,3-butanedione + H2O2
show the reaction diagram
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3.8% of activity with polyvinyl alcohol
-
?
1,3-butanediol + O2
?
show the reaction diagram
2,4-pentanediol + O2
2,4-pentanedione + H2O2
show the reaction diagram
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19.3% of activity with polyvinyl alcohol
-
?
2,4-pentanediol + O2
?
show the reaction diagram
2,5-hexanediol + O2
2,5-hexanedione + H2O2
show the reaction diagram
2-butanol + O2
2-butanone + H2O2
show the reaction diagram
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47.3% of activity with polyvinyl alcohol
-
?
2-hexanol + O2
2-hexanone + H2O2
show the reaction diagram
2-pentanol + O2
2-pentanone + H2O2
show the reaction diagram
2-propanol + O2
acetone + H2O2
show the reaction diagram
3-butanol + O2
3-butanone + H2O2
show the reaction diagram
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14.6% of activity with polyvinyl alcohol
-
?
3-heptanol + O2
3-heptanone + H2O2
show the reaction diagram
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68.8% of activity with polyvinyl alcohol
-
?
3-hexanol + O2
3-hexanone + H2O2
show the reaction diagram
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47.3% of activity with polyvinyl alcohol
-
?
4-decanol + O2
4-decanone + H2O2
show the reaction diagram
-
100% of activity with polyvinyl alcohol
-
?
4-heptanol + O2
4-heptanone + H2O2
show the reaction diagram
benzyl alcohol + O2
benzaldehyde + H2O2
show the reaction diagram
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13.7% of activity with polyvinyl alcohol
-
?
cyclohexanediol + O2
?
show the reaction diagram
cyclohexanol + O2
cyclohexanal + H2O2
show the reaction diagram
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41.8% of activity with polyvinyl alcohol
-
?
polypropylene glycol + O2
?
show the reaction diagram
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-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
show the reaction diagram
pyrroloquinoline quinone + O2
?
show the reaction diagram
low activity
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 hide
LITERATURE
Ca2+
high activation
Fe2+
-
1 mol iron/mol enzyme
Mg2+
activates, the activation by Mg2+ is less than 80% of the activation by Ca2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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1 mM, 23% inhibition
Fe2+
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1 mM, 88% inhibition
Hg2+
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1 mM, 93% inhibition
Sn2+
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1 mM, 89% inhibition
Thiourea
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1 mM, 20% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
additional information
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0018
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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
1.68
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polyvinyl alcohol
18
purified recombinant enzyme, substrate PVA117
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.4
dependent on buffer system, recombinant enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
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almost constant activity in this range
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
recombinant enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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activity associated with cells of co-isolated degrader strain Rhodococcus erythropolis
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Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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gel filtration
68000
recombinant enzyme, gel filtration
75000
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gel filtration
85000
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1 * 85000, SDS-PAGE
134300
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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stable for at least 24 h at 30°C
287626
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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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
ammonium sulfate precipitation and Q-Sepharose column chromatography
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native enzyme from strain O3
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native enzyme from strain PD
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Q-Sepharose, AF blue Toyopearl, Q-Sepharose
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recombinant His6-tagged enzyme from Escherichia coli 44fold to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, pCR-XL-TOPO vector
gene pvadh, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His6-tagged enzyme in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.3.30)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)