Information on EC 1.1.98.5 - secondary-alcohol dehydrogenase (coenzyme-F420)

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The expected taxonomic range for this enzyme is: Methanomicrobiaceae

EC NUMBER
COMMENTARY hide
1.1.98.5
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RECOMMENDED NAME
GeneOntology No.
secondary-alcohol dehydrogenase (coenzyme-F420)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
R-CHOH-R' + oxidized coenzyme F420 = R-CO-R' + reduced coenzyme F420
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lactate biosynthesis (archaea)
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chorismate metabolism
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SYSTEMATIC NAME
IUBMB Comments
secondary-alcohol:coenzyme F420 oxidoreductase
The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
show the reaction diagram
(S)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
show the reaction diagram
2-butanone + reduced coenzyme F420
2-butanol + oxidized coenzyme F420
show the reaction diagram
2-pentanol + oxidized coenzyme F420
2-pentanone + reduced coenzyme F420
show the reaction diagram
2-pentanone + reduced coenzyme F420
2-pentanol + oxidized coenzyme F420
show the reaction diagram
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-
-
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r
2-propanol + oxidized coenzyme F420
2-propanone + reduced coenzyme F420
show the reaction diagram
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2-propanone i.e. acetone
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r
2-propanol + oxidized coenzyme F420
propanone + reduced coenzyme F420
show the reaction diagram
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propanone i.e. acetone
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r
cyclopentanol + oxidized coenzyme F420
cyclopentanone + reduced coenzyme F420
show the reaction diagram
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-
-
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r
cyclopentanone + reduced coenzyme F420
cyclopentanol + oxidized coenzyme F420
show the reaction diagram
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-
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r
propanone + reduced coenzyme F420
2-propanol + oxidized coenzyme F420
show the reaction diagram
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the enzyme is Si-face specific with respect to the C5 atom of coenzyme F420, 2-propanone i.e. acetone
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r
propanone + reduced coenzyme F420
propanol + oxidized coenzyme F420
show the reaction diagram
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2-propanone i.e. acetone
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r
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme contains no zinc ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5 mM, 87% inhibition
2,2'-dipyridyl
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2 mM, 18% inhibition
4-hydroxymercuribenzoate
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0.1 mM, complete inhibition
K2SO4
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100 mM, more than 90% inhibition
Na2SO4
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100 mM, more than 90% inhibition
additional information
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no inhibition be EDTA (2-5 mM), iodoacetate (2-5 mM), or 4-hydroxymercurobenzoate (0.01-0.1 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.01
(R)-2-butanol
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pH 5.8, 37°C
0.8
(S)-2-butanol
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pH 5.8, 37°C
1.2
2-butanol
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pH 5.8, 37°C
7.2
2-Pentanol
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pH 5.8, 37°C
2.2 - 2.5
2-propanol
6.1
Cyclopentanol
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pH 5.8, 37°C
4.3
Cyclopentanone
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pH 5.8, 37°C
0.018
oxidized coenzyme F420
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pH 5.8, 37°C
0.25 - 0.5
propanone
0.008
reduced coenzyme F420
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pH 5.8, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
51.3
(R)-2-butanol
Methanofollis liminatans
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pH 5.8, 37°C
38.5
(S)-2-butanol
Methanofollis liminatans
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pH 5.8, 37°C
49
2-butanol
Methanofollis liminatans
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pH 5.8, 37°C
2.1
2-butanone
Methanofollis liminatans
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pH 5.8, 37°C
23.1
2-Pentanol
Methanofollis liminatans
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pH 5.8, 37°C
1.3
2-Pentanone
Methanofollis liminatans
-
pH 5.8, 37°C
85
2-propanol
Methanofollis liminatans
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pH 5.8, 37°C
12.8
Cyclopentanol
Methanofollis liminatans
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pH 5.8, 37°C
4.4
Cyclopentanone
Methanofollis liminatans
-
pH 5.8, 37°C
85
oxidized coenzyme F420
Methanofollis liminatans
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pH 5.8, 37°C
161.5
propanone
Methanofollis liminatans
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pH 5.8, 37°C
161.5
reduced coenzyme F420
Methanofollis liminatans
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pH 5.8, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
(R)-2-butanol
Methanofollis liminatans
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pH 5.8, 37°C
2292
48
(S)-2-butanol
Methanofollis liminatans
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pH 5.8, 37°C
1990
40.8
2-butanol
Methanofollis liminatans
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pH 5.8, 37°C
1132
3.2
2-Pentanol
Methanofollis liminatans
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pH 5.8, 37°C
2329
323
2-Pentanone
Methanofollis liminatans
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pH 5.8, 37°C
1911
38.6
2-propanol
Methanofollis liminatans
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pH 5.8, 37°C
682
2.1
Cyclopentanol
Methanofollis liminatans
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pH 5.8, 37°C
2729
1
Cyclopentanone
Methanofollis liminatans
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pH 5.8, 37°C
2478
4700
oxidized coenzyme F420
Methanofollis liminatans
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pH 5.8, 37°C
1665
20200
reduced coenzyme F420
Methanofollis liminatans
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pH 5.8, 37°C
1244
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110
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2-propanone, pH 4.2, 40°C
176
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2-propanol, pH 4.2, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
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pH 3.0: about 30% of maximal activity, pH 7.0: about 30% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
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4 * 39000, SDS-PAGE
39500
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2 * 39500, SDS-PAGE
68000
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gel filtration
100000
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ultrafiltration
150000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 39500, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the enzyme at 1.8 A resolution in complex with a F420-acetone adduct. The position of F420and isopropanol defines the active site for hydride transfer in the interior of Adf that is completely shielded from bulk solvent. The distance of 2.9 A between the C2 atom of isopropanol and the C5 atom of F420 is optimal for hydride transfer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
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activity loss of a 50fold diluted extract tested at 0-28°C is least around pH 5.8 (30% in 23 days at 23°C)
724134
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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pH 5.8, the activity of a 20-fold dilution decreases to 5% within 20 min. If 100 mM potassium sulfate is present 40% of the activity is left after 20 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in 40 mM phosphate or Tris-HC1 buffer at 4°C and also in low-ionic-strength buffers in which precipitation occurrs and enzyme activity is lost irreversibly. The enzyme can be stabilized by addition of 200 mM sodium sulfate and 10 mM 2-propanol to the buffer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, almost no loss in specific activity after 1 year
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isolated under anaerobic conditions
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by its substrate, expression is faster if H2 and CO2 are present as energy source
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