Information on EC 1.1.99.12 - sorbose dehydrogenase

Substrates: -
Products: -

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

D-sorbitol + acceptor

L-sorbose + reduced acceptor

L-sorbose + 2,6-dichlorophenolindophenol

5-keto-D-fructose + reduced 2,6-dichlorophenolindophenol

Substrates: no activity with D-fructose, sucrose and dulcitol
Products: -

L-sorbose + acceptor

5-dehydro-D-fructose + reduced acceptor

L-sorbose + acceptor

L-sorbosone + reduced acceptor

3 entries

D-sorbitol + acceptor

L-sorbose + reduced acceptor

Gluconobacter oxydans WSH-003

740828

Substrates: -
Products: -

D-sorbitol + acceptor

L-sorbose + reduced acceptor

740828

Substrates: -
Products: -

L-sorbose + acceptor

5-dehydro-D-fructose + reduced acceptor

Ketogulonicigenium vulgare DSM 4025

Substrates: -
Products: -

L-sorbose + acceptor

5-dehydro-D-fructose + reduced acceptor

Substrates: -
Products: -

L-sorbose + acceptor

L-sorbosone + reduced acceptor

287727, 657424

Substrates: -
Products: -

L-sorbose + acceptor

L-sorbosone + reduced acceptor

Substrates: strain DSM 4025, enzyme has both L-sorbose dehydrogenase and L-sorbosone dehydrogenase activity, 10.9% of activity with 1-propanol
Products: -

L-sorbose + acceptor

L-sorbosone + reduced acceptor

Substrates: -
Products: -

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

cytochrome c

strain DSM 4025, physiological electron acceptor

pyrroloquinoline quinone

4 entries

pyrroloquinoline quinone

pyrroloquinoline quinone

740005, 740828

pyrroloquinoline quinone

pyrroloquinoline quinone

strain DSM 4025, non-covalently bound, 2 mol PQQ/mol enzyme

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

Ag+

1 mM, complete inhibition

Citric acid

CoCl2

Cu2+

EDTA

EGTA

strain DSM 4025, 5 mM, 89% inhibition

Fe2+

FeCl2

strain DSM 4025, 5 mM, 89% inhibition

FeCl3

strain DSM 4025, 5 mM, 97% inhibition

Hg2+

1 mM, complete inhibition

NiSO4

strain DSM 4025, 5 mM, 77% inhibition

p-chloromercuribenzoate

1 mM, 40% inhibition

Phenylmercuric nitrate

1 mM, 40% inhibition

Semicarbazide

1 mM, 40% inhibition

ZnCl2

strain DSM 4025, 5 mM, 90% inhibition

CoCl2

strain DSM 4025, 5 mM, 84% inhibition

CoCl2

strong inhibition

Cu2+

1 mM, complete inhibition

Cu2+

EDTA

strain DSM 4025, 5 mM, 87% inhibition

EDTA

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

azide

1 mM, 30-40% increase in activity, 2,6-dichlorophenol as electron acceptor

Ca2+

cyanide

1 mM, 30-40% increase in activity, 2,6-dichlorophenol as electron acceptor

FeCl3

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1-propanol

strain DSM 4025

4.3 - 230

L-sorbose

3 entries

4.3

L-sorbose

L-sorbose

230

L-sorbose

strain DSM 4025

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.0099

10.3

promoters has strong activity

6.73

strain DSM 4025

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.2

6.4

7 - 9

strain DSM 4025

7.4

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 8.7

pH 5.0: about 40% of activity maximum, pH 8.7: about 30% of activity maximum

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

30 - 40

strain DSM 4025

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

10 - 50

strain DSM 4025

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

brenda

3 entries

isolated from japanese persimmon

Gluconobacter oxydans WSH-003

brenda

740005, 740828

brenda

Ketogulonicigenium vulgare DSM 4025

Ketogulonicigenium vulgare HB602

brenda

725870

brenda

287726, 657424, 673382, 740005, 740828

brenda

isolated from japanese persimmon

brenda

strain DSM 4025

brenda

724570, 725582, 725870

brenda

DSM 4025

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

particle-bound

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

physiological function

Ketogulonicigenium vulgare HB602

overexpression of sorbose dehydrogenase in Ketogulonigenium vulgare leads to a metabolic burden that enhances 2-keto-L-gulonic acid production

725870

physiological function

overexpression of sorbose dehydrogenase in Ketogulonigenium vulgare leads to a metabolic burden that enhances 2-keto-L-gulonic acid production

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).

E2PT11 pBLAST

E2PT11_ASPNC

Aspergillus niger (strain CBS 513.88 / FGSC A1513)

428

46845

TrEMBL

Show Sequence

other Location (Reliability: 1)

A0A0F4YZT2 pBLAST

A0A0F4YZT2_TALEM

Rasamsonia emersonii CBS 393.64

577

64262

TrEMBL

Show Sequence

other Location (Reliability: 1)

E2PSU8 pBLAST

E2PSU8_ASPNC

Aspergillus niger (strain CBS 513.88 / FGSC A1513)

566

62851

TrEMBL

Show Sequence

other Location (Reliability: 1)

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

135000

strain DSM 4025, gel filtration

190000

46000

SDS-PAGE

58000

x * 58000, SDS-PAGE

60000

62500

strain DSM 4025, 1 * 62500 + 1 * 64500, SDS-PAGE

64500

strain DSM 4025, 1 * 62500 + 1 * 64500, SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

strain DSM 4025, 1 * 62500 + 1 * 64500, SDS-PAGE

x * 58000, SDS-PAGE

x * 58000, SDS-PAGE

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 min, 20°C, complete inactivation

287726

6 - 6.5

30 min, 20°C, highest stability

287726

7.5

30 min, 20°C, complete inactivation

287726

additional information

strain DSM 4025, enzyme is stable in alkaline pH and unstable with increasing acidity

287728

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 min, complete inactivation

additional information

strain DSM 4025, enzyme is stable at and below 30°C, but unstable above 40°C

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

287727, 657424

strain DSM 4025, PEG 600, DEAE-Toyopearl, Q-Sepharose

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

constructs with and without sequences of promoters, identification of the transcription initiation site

expressed in Escherichia coli JM109 cells

expression in Escherichia coli, constructs with and without sequences of promoters, identification of the transcription initiation site

strain T-100, expression in Escherichia coli and Gluconobacter oxydans G624

expressed in Escherichia coli JM109 cells

740005

expressed in Escherichia coli JM109 cells

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

food industry

food industry

L-sorbose can be catalyzed into L-ascorbic acid by Ketogulonicigenium vulgare, vitamin C industry

food industry

L-sorbose can be catalyzed into L-ascorbic acid by Ketogulonicigenium vulgare, vitamin C industry

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Sato, K.; Yamada, Y.; Aida, K.; Uemura, T.

Enzymatic studies on the oxidation of sugar and sugar alcohol. 8. Particle-bound L-sorbose dehydrogenase from Gluconobacter suboxydans

J. Biochem.

521-527

1969

Gluconobacter oxydans

5354025

brenda

Saito, Y.; Ishil, Y.; Hayashi, H.; Imao, Y.; Akashi, T.; Yoshikawa, K.; Noguchi, Y.; Soeda, S.; Yoshida, M.; Niwa, M.; Hosodo, J.; Shimomura.

Cloning of genes coding for L-sorbose and L-sorbosone dehydrogenases from Gluconobacter oxydans and microbial production of 2-keto-L-gulonate, a precursor of L-ascorbic acid, in a recombinant G. oxydans strain

Appl. Environ. Microbiol.

454-460

1997

Gluconobacter oxydans, Gluconobacter oxydans T-100

9023923

brenda

Asakura, A.; Hoshino, T.

Isolation and Characterization of a New Quinoprotein Dehydrogenase, L-Sorbose/L-Sorbosone Dehydrogenase.

Biosci. Biotechnol. Biochem.

46-53

1999

Gluconobacter oxydans

27392874

brenda

Hao, L.; Chen, H.; Cao, G.; Cao, T.; Cao, J.; Feng, S.; Zhang, C.; Zhang, Z.

Properties and functions of L-sorbose dehydrogenase in two-step fermentation of vitamin C

Yingyong Yu Huanjing Shengwu Xuebao

204-208

2002

Gluconobacter oxydans

brenda

Zhang, W.; Yan, B.; Wang, J.; Yao, J.; Yu, Z.

Purification and characterization of membrane-bound L-sorbose dehydrogenase from Gluconobacter oxydans GO112

Enzyme Microb. Technol.

643-648

2006

Gluconobacter oxydans

brenda

Fu, S.; Zhang, W.; Guo, A.; Wang, J.

Identification of promoters of two dehydrogenase genes in Ketogulonicigenium vulgare DSM 4025 and their strength comparison in K. vulgare and Escherichia coli

Appl. Microbiol. Biotechnol.

1127-1132

2007

Escherichia coli, Ketogulonicigenium vulgare

17404730

brenda

724570

Zhu, Y.; Liu, J.; Du, G.; Zhou, J.; Chen, J.

Sporulation and spore stability of Bacillus megaterium enhance Ketogulonigenium vulgare propagation and 2-keto-L-gulonic acid biosynthesis

Biores. Technol.

107

399-404

2012

Ketogulonicigenium vulgare

22257860

brenda