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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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, 37C
0.8
(S)-2-butanol
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pH 5.8, 37C
1.2
2-butanol
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pH 5.8, 37C
7.2
2-Pentanol
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pH 5.8, 37C
2.2 - 2.5
2-propanol
6.1
Cyclopentanol
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pH 5.8, 37C
4.3
Cyclopentanone
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pH 5.8, 37C
0.018
oxidized coenzyme F420
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pH 5.8, 37C
0.25 - 0.5
propanone
0.008
reduced coenzyme F420
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pH 5.8, 37C
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, 37C
38.5
(S)-2-butanol
Methanofollis liminatans
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pH 5.8, 37C
49
2-butanol
Methanofollis liminatans
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pH 5.8, 37C
2.1
2-butanone
Methanofollis liminatans
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pH 5.8, 37C
23.1
2-Pentanol
Methanofollis liminatans
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pH 5.8, 37C
1.3
2-Pentanone
Methanofollis liminatans
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pH 5.8, 37C
85
2-propanol
Methanofollis liminatans
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pH 5.8, 37C
12.8
Cyclopentanol
Methanofollis liminatans
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pH 5.8, 37C
4.4
Cyclopentanone
Methanofollis liminatans
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pH 5.8, 37C
85
oxidized coenzyme F420
Methanofollis liminatans
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pH 5.8, 37C
161.5
propanone
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, 37C
2292
48
(S)-2-butanol
Methanofollis liminatans
-
pH 5.8, 37C
1990
40.8
2-butanol
Methanofollis liminatans
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pH 5.8, 37C
1132
3.2
2-Pentanol
Methanofollis liminatans
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pH 5.8, 37C
2329
323
2-Pentanone
Methanofollis liminatans
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pH 5.8, 37C
1911
38.6
2-propanol
Methanofollis liminatans
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pH 5.8, 37C
682
2.1
Cyclopentanol
Methanofollis liminatans
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pH 5.8, 37C
2729
1
Cyclopentanone
Methanofollis liminatans
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pH 5.8, 37C
2478
4700
oxidized coenzyme F420
Methanofollis liminatans
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pH 5.8, 37C
1665
20200
reduced coenzyme F420
Methanofollis liminatans
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pH 5.8, 37C
1244
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110
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2-propanone, pH 4.2, 40C
176
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2-propanol, pH 4.2, 40C
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
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 0-28C is least around pH 5.8 (30% in 23 days at 23C)
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 4C 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
4C, 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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