Information on EC 1.1.1.245 - cyclohexanol dehydrogenase

Substrates: relative oxidation activity at 22% the rate of cyclohexanol oxidation
Products: -

cyclohexane-1,4-diol + NAD+

cyclohexane-1,4-dione + NADH

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: inducible
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: inducible
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: -
Products: reverse reaction at pH 7

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: inducible
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Substrates: metabolism of cyclohexane
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: preferred substrate
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: metabolism of cyclohexane
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH + H+

667621, 667502

Substrates: -
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH + H+

Substrates: temperature-induced conformational change is associated with the flexible loops directly involved in the substrate and coenzyme binding
Products: -

cyclopentanol + NAD+

cyclopentanone + NADH

Substrates: relative oxidation activity at 232% the rate of cyclohexanol oxidation
Products: -

cyclopentanol + NAD+

cyclopentanone + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Substrates: -
Products: relative reduction activity at 4% the rate of cyclohexanone reduction

cyclopentanol + NAD+

cyclopentanone + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

Substrates: relative oxidation activity at 77% the rate of cyclohexanol oxidation
Products: -

cyclopentanol + NAD+

cyclopentanone + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Substrates: relative oxidation activity at 77% the rate of cyclohexanol oxidation
Products: -

ethanol + NAD+

acetaldehyde + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

Substrates: relative activity at 20% the rate of cyclohexanol oxidation
Products: -

ethanol + NAD+

acetaldehyde + NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Substrates: relative activity at 20% the rate of cyclohexanol oxidation
Products: -

methanol + NAD+

formaldehyde + NADH + H+

Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

Substrates: relative activity at 2% the rate of cyclohexanol oxidation
Products: -

methanol + NAD+

formaldehyde + NADH + H+

Substrates: relative activity at 2% the rate of cyclohexanol oxidation
Products: -

additional information

Substrates: 2-hydroxycyclohexanone, 1,3,5-trihydroxycyclohexane, menthol, ethanol, 1-propanol, 1-butanol and 1-pentanol are not oxidized with NAD+
Products: 2-cyclopentenone, 1,3-cyclohexanedione, 1,3-cyclopentanedione and 5-oxocapronate are not reduced with NADH

additional information

Substrates: cyclohexane-1,2-dione is not oxidized with NAD+
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

cyclohexanol + NAD+

cyclohexanone + NADH

5 entries

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: inducible
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: inducible
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: inducible
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: metabolism of cyclohexane
Products: -

cyclohexanol + NAD+

cyclohexanone + NADH

Substrates: metabolism of cyclohexane
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NAD+

6 entries

NADH

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

enzyme exhibits linearity of NAD(H) binding at pH 9.8 and at moderate ionic strength, in addition to positive cooperativity at pH 7.8 and 6.8, and at pH 9.8 in the presence of salt. NADH binding is positively cooperative below 20°C and negatively cooperative at 4050°. Steady-state kinetic measurements show that SsADH displays standard MichaelisMenten kinetics between 35°C and 45°C, but exhibits positive and negative cooperativity for NADH oxidation below and above this range of temperatures, respectively. Mutant N249Y displays non-cooperative behavious in coenzyme binding under the same experimental conditions used for the wild-type enzyme

NADP+

NAD+

NAD+

NAD+

NAD+

isoenzyme II

NAD+

NAD+

temperature-induced conformational change is associated with the flexible loops directly involved in the substrate and coenzyme binding

NADP+

less than 5% activity than with NAD+

NADP+

weaker activity than with NAD+

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ba2+

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

increase of activity at 10 mM

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Mg2+

increase of activity at 10 mM

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

Al3+

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

almost complete inhibition of activity at 10 mM

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Ca2+

inhibition of activity at 10 mM

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Co2+

inhibition of activity at 10 mM

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Cu2+

almost complete inhibition of activity at 10 mM

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Mn2+

93% inhibition of activity at 10 mM

p-chloromercuribenzoate

100% inhibition

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

Zn2+

91% inhibition of activity at 10 mM

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.41

Cyclohexane-1,2-diol

pH 10.3

0.5

Cyclohexane-1,3-diol

pH 10.3

0.59

Cyclohexane-1,4-diol

pH 10.3

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

0.0013 - 0.05

Cyclohexanol

4 entries

0.0142

Cyclopentanol

isoenzyme II at pH 7.6

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

0.0135

hexane-1,2-diol

isoenzyme II at pH 7.6

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

0.024 - 0.04

NAD+

2 entries

0.0028

trans-Cyclohexane-1,2-diol

isoenzyme II at pH 7.6

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

0.0137

trans-cyclopentane-1,2-diol

isoenzyme II at pH 7.6

additional information

steady-state kinetic measurements show that SsADH displays standard MichaelisMenten kinetics between 35°C and 45°C, but exhibits positive and negative cooperativity for NADH oxidation below and above this range of temperatures, respectively

667502

0.0013

Cyclohexanol

pH 10.3

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

0.0017

Cyclohexanol

isoenzyme II at pH 7.6

0.037

Cyclohexanol

0.05

Cyclohexanol

0.024

NAD+

0.04

NAD+

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.04

cell extract

286382

0.28

cell extract at pH 10

0.8

oxidation of cyclohexanol at pH 7.8

0.87

1.9

reduction of cyclohexanone at pH 7.8

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

127

purified enzyme

143.5

purified enzyme

2.5

pH 10

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

10.1 - 10.5

oxidation of alcohol

10.5

10.6

show all columns Go to Temperature Range Search

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 - 65

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

Acidovorax sp.

A0A2D0WG37

UniProt

brenda

brenda

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

brenda

brenda

brenda

Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

brenda

brenda

brenda

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

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).

Q6TMA3 pBLAST

CHNA_RHOS6

Rhodococcus sp. (strain TK6)

270

28376

Swiss-Prot

Show Sequence

Q9F7E0 pBLAST

CHNA_ACISS

Acinetobacter sp. (strain SE19)

251

26159

Swiss-Prot

Show Sequence

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

145000

gel filtration

150000

SDS-PAGE

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

28000

2 * 28000, SDS-PAGE, isoenzyme II

37500

4 * 37500, SDS-PAGE

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

60000

gel filtration, isoenzyme II

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

2 entries

homotetramer

4 * 37500, SDS-PAGE

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

dimer

2 * 28000, SDS-PAGE, isoenzyme II

Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

dimer

2 * 28000, SDS-PAGE, isoenzyme II

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

N249Y

mutant N249Y displays non-cooperative behavious in coenzyme binding under the same experimental conditions used for the wild-type enzyme (that exhibits linearity of NAD(H) binding at pH 9.8 and at moderate ionic strength, in addition to positive cooperativity at pH 7.8 and 6.8, and at pH 9.8 in the presence of salt. NADH binding is positively cooperative below 20°C and negatively cooperative at 4050°)

667502

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

10.5

rapid inactivation above pH 10.5

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

7.5 - 8.5

stable

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

labile

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

90% activity after incubation for 20 min

1 min 50% loss of activity

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

less than 20% activity after incubation for 20 min

1 min 85% loss of activity

1 min 95% loss of activity

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, stable for several days

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

126fold, affinity chromatograpy

Rhodococcus sp. (in: high G+C Gram-positive bacteria)

9.8fold, isoenzyme II

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli

expression in Pseudomonas taiwanensis VLB120

Acidovorax sp.

A0A2D0WG37

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

synthesis

Acidovorax sp.

A0A2D0WG37

synthesis of lactones from cycloalkanes. A heterologous pathway comprising enzymes with compatible kinetics is designed in Pseudomonas taiwanensis VLB120 enabling in-vivo cascade for synthesizing lactones from cycloalkanes. The respective pathway includes cytochrome P450 monooxygenase (CHX), cyclohexanol dehydrogenase (CDH), and cyclohexanone monooxygenase (CHXON) from Acidovorax sp. CHX100. Resting cells of the recombinant host Pseudomonas taiwanensis VLB120 convert cyclohexane, cyclohexanol, and cyclohexanone to epsilon-caprolactone at 22, 80-100, and 170 U/g cell dry weight, respectively. Cyclohexane (5 mM) is completely converted with a selectivity of 65% for epsilon-caprolactone formation in 2 h without accumulation of intermediate products

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Dangel, W.; Tschech, A.; Fuchs, G.

Enzyme reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species

Arch. Microbiol.

152

273-279

1989

Pseudomonas sp.

brenda

Donoghue, N.A.; Trudgill, P.W.

The metabolism of cyclohexanol by Acinetobacter NCIB 9871

Eur. J. Biochem.

1-7

1975

Acinetobacter sp., Acinetobacter sp. NCIB 9871

1261

brenda

Trower, M.K.; Buckland, R.M.; Higgins, R.; Griffin, M.

Isolation and characterization of a cyclohexane-metabolizing Xanthobacter sp.

Appl. Environ. Microbiol.

1282-1289

1985

Xanthobacter sp.

16346796

brenda

Stirling, L.A.; Perry, J.J.

Purification and properties of a nicotinamide adenine dinucleotide-linked cyclohexanol dehydrogenase from a Nocardia species

Curr. Microbiol.

37-40

1980

Nocardia sp.

brenda

286382

Anderson M.A.; Hall, R.A.; Griffin, M.

Microbial metabolism of alicyclic hydrocarbons: cyclohexane catabolism by a pure strain of Pseudmonas sp.

J. Gen. Microbiol.

120

89-94

1980

Pseudomonas sp.

brenda

Tae-Kang, K.; Choi, J.H.; Rhee, I.K.

Purification and characterization of a cyclohexanol dehydrogenase from Rhodococcus sp. TK6

J. Microbiol. Biotechnol.

39-45

2002

Rhodococcus sp. (in: high G+C Gram-positive bacteria), Rhodococcus sp. (in: high G+C Gram-positive bacteria) TK6

brenda

667502

Giordano, A.; Febbraio, F.; Russo, C.; Rossi, M.; Raia, C.A.

Evidence for co-operativity in coenzyme binding to tetrameric Sulfolobus solfataricus alcohol dehydrogenase and its structural basis: fluorescence, kinetic and structural studies of the wild-type enzyme and non-co-operative N249Y mutant

Biochem. J.

388

657-667

2005

Saccharolobus solfataricus

15651978

brenda

Secundo, F.; Russo, C.; Giordano, A.; Carrea, G.; Rossi, M.; Raia, C.A.

Temperature-induced conformational change at the catalytic site of Sulfolobus solfataricus alcohol dehydrogenase highlighted by Asn249Tyr substitution. A hydrogen/deuterium exchange, kinetic, and fluorescence quenching study

Biochemistry

11040-11048

2005

Saccharolobus solfataricus

16101287

brenda