Information on EC 1.1.3.30 - polyvinyl-alcohol oxidase

Substrates: pva operon characterized
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: the enzyme is involved in polyvinyl alcohol-degradation
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

A0A1B2N825

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

additional information

Substrates: no activity with primary nor secondary alcohols
Products: -

additional information

A0A1B2N825

Substrates: no substrate: vinyl alcohol oligomer
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

24 entries

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Brevundimonas vesicularis PD

287626, 695840

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Brevundimonas vesicularis PH

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Geotrichum sp.

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Geotrichum sp. WF9101

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Microbacterium barkeri

Microbacterium barkeri KCCM10507

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Paenibacillus amylolyticus

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Paenibacillus amylolyticus KCCM 10508

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Penicillium sp.

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Penicillium sp. WSH02-21

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

695840, 740326

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Priestia megaterium BX1

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

287623, 287624, 287625, 695840

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

287623

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

287623, 287625

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: the enzyme is involved in polyvinyl alcohol-degradation
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: the enzyme is involved in polyvinyl alcohol-degradation
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

polyvinyl alcohol + O2

oxidized polyvinyl alcohol + H2O2

Substrates: -
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

additional information

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

287625

additional information

A0A1B2N825

no requirement for pyrroloquinoline quinone

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

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+

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

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

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

pyrroloquinoline quinone

additional information

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

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0017

polyvinyl alcohol

0.0017

polyvinyl alcohol

A0A1B2N825

pH 7.2, 30°C, absence of pyrroloquinoline quinone

0.0017

polyvinyl alcohol

A0A1B2N825

pH 7.2, 30°C, presence of pyrroloquinoline quinone

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

44.7 - 45.3

polyvinyl alcohol

44.7

polyvinyl alcohol

A0A1B2N825

pH 7.2, 30°C, presence of pyrroloquinoline quinone

45.3

polyvinyl alcohol

A0A1B2N825

pH 7.2, 30°C, absence of pyrroloquinoline quinone

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

26700

polyvinyl alcohol

26700

polyvinyl alcohol

A0A1B2N825

pH 7.2, 30°C, absence of pyrroloquinoline quinone

26700

polyvinyl alcohol

A0A1B2N825

pH 7.2, 30°C, presence of pyrroloquinoline quinone

show all columns Go to Specific Activity Search

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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

0.7

1.68

polyvinyl alcohol

purified recombinant enzyme, substrate PVA117

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

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to pH Range Search

7.2

7.2 - 7.4

dependent on buffer system, recombinant enzyme

7.5

7.2

assay at

7.2

activity assay at

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7 - 11

almost constant activity in this range

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

recombinant enzyme

show all columns Go to Temperature Range Search

assay at

activity assay at

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

35 - 45

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Brevundimonas vesicularis PD

Brevundimonas vesicularis PH

brenda

brenda

Geotrichum sp.

brenda

Geotrichum sp. WF9101

brenda

Microbacterium barkeri

Microbacterium barkeri KCCM10507

brenda

brenda

no activity in Alcaligenes faecalis

brenda

no activity in Alcaligenes faecalis KK314

brenda

no activity in Pseudomonas sp.

strain N1

brenda

no activity in Pseudomonas sp. VM15C

strain N1

brenda

no activity in Rhodococcus erythropolis

but supports growth and degradation of polyvinyl alcohol by Sphingomonas sp.

Paenibacillus amylolyticus

brenda

Paenibacillus amylolyticus KCCM 10508

brenda

brenda

Penicillium sp.

brenda

Penicillium sp. WSH02-21

brenda

695840, 740326

brenda

Priestia megaterium BX1

brenda

brenda

A0A1B2N825

UniProt

brenda

brenda

brenda

brenda

var. povalolyticus PH

brenda

in symbiotic culture with Pseudomonas putida during PVA utilization

brenda

strains O3, VM15C, and A-41

brenda

CCM 7450, growth and PVA degradation supported by co-isolated strain Rhodococcus erythropolis OT3

brenda

strains TJ7 and SA3

brenda

brenda

gene pvadh; gene pvadh or pvaA

SwissProt

brenda

polyvinyl alcohol dehydrogenase, part of pva operon

SwissProt

brenda

reidentified from Sphingomonas sp. strain 113P3 by taxonomic analysis

brenda

strain PVA3, no activity in strain 113P3

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

additional information

5 entries

brenda

brenda

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

Priestia megaterium BX1

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

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

A0A1B2N825

brenda

additional information

activity associated with cells of co-isolated degrader strain Rhodococcus erythropolis

brenda

amount depending on growth rate

brenda

amount depending on growth rate

brenda

amount depending on growth rate

brenda

A0A1B2N825

brenda

the enzyme is excreted

brenda

the enzyme is excreted

brenda

brenda

membrane-bound amount depending on growth rate, 50% of enzyme activity is localized on cytoplasmic membrane

287623

brenda

periplasm

membrane-bound amount depending on growth rate, 50% of enzyme activity is localized on cytoplasmic membrane

brenda

periplasm

membrane-bound amount depending on growth rate, 50% of enzyme activity is localized on cytoplasmic membrane

brenda

periplasm

brenda

brenda

extracellular or cell-associated enzyme activity undetectable in strain 113P3

brenda

brenda

Highest Expressing Human Cell Lines

Filter by:

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Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

A0A1B2N825

knocking out BAY15_3292 results in a significant decline in polyvinyl alcohol-degrading activity

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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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).

Q588Z1 pBLAST

PVADH_SPHS1

Sphingopyxis sp. (strain 113P3)

654

69486

Swiss-Prot

Show Sequence

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

134300

gel filtration

31000

gel filtration

68000

recombinant enzyme, gel filtration

75000

gel filtration

85000

1 * 85000, SDS-PAGE

show all columns Go to Subunit Search

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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

monomer

1 * 85000, SDS-PAGE

monomer

1 * 68000, recombinant enzyme, SDS-PAGE

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6 - 10

stable for at least 24 h at 30°C

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

stable for 30 min, complete loss of activity after 30 min at 60°C

Go to Storage Stability Search

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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

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

ammonium sulfate precipitation and Q-Sepharose column chromatography

740326

native enzyme from strain O3

native enzyme from strain PD

Q-Sepharose, AF blue Toyopearl, Q-Sepharose

Go to Cloned (commentary) Search

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

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

287623

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.

8-10

1985

Pseudomonas sp.

16346711

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.

275-278

1989

no activity in Pseudomonas sp., no activity in Pseudomonas sp. VM15C, Pseudomonas sp.

16347841

brenda

287625

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.

268-275

1986

Pseudomonas sp.

3513704

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.

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.

804-811

2006

Sphingopyxis sp., Sphingopyxis sp. PVA3

16583228

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)

16804170

brenda

Vaclavkova, T.; Ruzicka, J.; Julinova, M.; Vicha, R.; Koutny, M.

Novel aspects of symbiotic (polyvinyl alcohol) biodegradation

Appl. Microbiol. Biotechnol.

911-917

2007

no activity in Rhodococcus erythropolis, Sphingomonas sp.

17594087

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.

685-693

2008

Sphingopyxis sp. (Q588Z1), Sphingopyxis sp.

18214469

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.

17453173

brenda

Kawai, F.; Hu, X.

Biochemistry of microbial polyvinyl alcohol degradation

Appl. Microbiol. Biotechnol.

227-237

2009

Brevundimonas vesicularis, Brevundimonas vesicularis PD, Brevundimonas vesicularis PH, Geotrichum sp., Geotrichum sp. WF9101, Microbacterium barkeri, Microbacterium barkeri KCCM10507, no activity in Alcaligenes faecalis, no activity in Alcaligenes faecalis KK314, Paenibacillus amylolyticus, Paenibacillus amylolyticus KCCM 10508, Penicillium sp., Penicillium sp. WSH02-21, Priestia megaterium, Priestia megaterium BX1, Pseudomonas sp., Sphingomonas sp., Sphingopyxis sp., Streptomyces venezuelae, Streptomyces venezuelae GY1

19590867

brenda

740326

Li, M.; Du, G.

Purification and enzymatic properties of polyvinyl alcohol dehydrogenase

Chin. J. Proc. Engin.

1015-1019

2014

Priestia megaterium

brenda