Information on EC 1.1.3.30 - polyvinyl-alcohol oxidase

Word Map on EC 1.1.3.30
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.1.3.30
-
RECOMMENDED NAME
GeneOntology No.
polyvinyl-alcohol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
polyvinyl alcohol + O2 = oxidized polyvinyl alcohol + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
polyvinyl-alcohol:oxygen oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
119940-13-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain BX1
-
-
Manually annotated by BRENDA team
strain BX1
-
-
Manually annotated by BRENDA team
strain PD
-
-
Manually annotated by BRENDA team
strain PH
-
-
Manually annotated by BRENDA team
strain WF9101
-
-
Manually annotated by BRENDA team
strain WF9101
-
-
Manually annotated by BRENDA team
strain KCCM10507
-
-
Manually annotated by BRENDA team
strain KCCM10507
-
-
Manually annotated by BRENDA team
no activity in Alcaligenes faecalis
strain KK314
-
-
Manually annotated by BRENDA team
no activity in Alcaligenes faecalis KK314
strain KK314
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp.
strain N1
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp. VM15C
strain N1
-
-
Manually annotated by BRENDA team
no activity in Rhodococcus erythropolis
but supports growth and degradation of polyvinyl alcohol by Sphingomonas sp.
-
-
Manually annotated by BRENDA team
strain KCCM 10508
-
-
Manually annotated by BRENDA team
strain KCCM 10508
-
-
Manually annotated by BRENDA team
strain WSH02-21
-
-
Manually annotated by BRENDA team
strain WSH02-21
-
-
Manually annotated by BRENDA team
gene pvadh; strain 113P3, gene pvadh or pvaA
SwissProt
Manually annotated by BRENDA team
polyvinyl alcohol dehydrogenase, part of pva operon; strain 113P3
SwissProt
Manually annotated by BRENDA team
strain PVA3
-
-
Manually annotated by BRENDA team
strain GY1
-
-
Manually annotated by BRENDA team
strain GY1
-
-
Manually annotated by BRENDA team
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
-
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
-
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
-
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
-
14.6% of activity with polyvinyl alcohol
-
?
3-heptanol + O2
3-heptanone + H2O2
show the reaction diagram
-
68.8% of activity with polyvinyl alcohol
-
?
3-hexanol + O2
3-hexanone + H2O2
show the reaction diagram
-
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
-
13.7% of activity with polyvinyl alcohol
-
?
cyclohexanediol + O2
?
show the reaction diagram
cyclohexanol + O2
cyclohexanal + H2O2
show the reaction diagram
-
41.8% of activity with polyvinyl alcohol
-
?
polypropylene glycol + O2
?
show the reaction diagram
-
-
-
?
polyvinyl alcohol + O2
oxidized polyvinyl alcohol + H2O2
show the reaction diagram
pyrroloquinoline quinone + O2
?
show the reaction diagram
low activity
-
-
?
additional information
?
-
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no requirement for pyrroloquinoline quinone (PQQ) as does the PQQ-dependent PVA dehydrogenase
-
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+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
1 mM, 23% inhibition
Fe2+
-
1 mM, 88% inhibition
Hg2+
-
1 mM, 93% inhibition
Sn2+
-
1 mM, 89% inhibition
Thiourea
-
1 mM, 20% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
1.68
-
polyvinyl alcohol
18
purified recombinant enzyme, substrate PVA117
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.4
dependent on buffer system, recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
-
almost constant activity in this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
activity associated with cells of co-isolated degrader strain Rhodococcus erythropolis
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
gel filtration
68000
recombinant enzyme, gel filtration
75000
-
gel filtration
85000
-
1 * 85000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
stable for at least 24 h at 30°C
287626
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
stable for 30 min, complete loss of activity after 30 min at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant enzyme, 20 mM Tris/HCl buffer, pH 8.0, stable for more than a month
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain O3
-
native enzyme from strain PD
-
Q-Sepharose, AF blue Toyopearl, Q-Sepharose
-
recombinant His6-tagged enzyme from Escherichia coli 44fold to homogeneity
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