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Information on EC 1.1.98.5 - secondary-alcohol dehydrogenase (coenzyme-F420)
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1.1.98.5 secondary-alcohol dehydrogenase (coenzyme-F420)IUBMB Comments
The enzyme isolated from the methanogenic archaea Methanogenium liminatans catalyses the reversible oxidation of various secondary and cyclic alcohols to the corresponding ketones.
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The expected taxonomic range for this enzyme is: Methanomicrobiaceae
Synonyms
F420-dependent alcohol dehydrogenase, F420-dependent secondary alcohol dehydrogenase, F420-specific sec-ADH, F420-specific secondary alcohol dehydrogenase, propane-2-ol:F420 oxidoreductase, secondary alcohol:F420 oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F420-dependent alcohol dehydrogenase
F420-dependent secondary alcohol dehydrogenase
secondary alcohol:F420 oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
R-CHOH-R' + oxidized coenzyme F420 = R-CO-R' + reduced coenzyme F420
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-pentanone + reduced coenzyme F420
2-pentanol + oxidized coenzyme F420
-
-
-
-
r
2-propanol + oxidized coenzyme F420
2-propanone + reduced coenzyme F420
-
-
2-propanone i.e. acetone
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r
2-propanol + oxidized coenzyme F420
propanone + reduced coenzyme F420
-
-
propanone i.e. acetone
-
r
cyclopentanol + oxidized coenzyme F420
cyclopentanone + reduced coenzyme F420
-
-
-
-
r
cyclopentanone + reduced coenzyme F420
cyclopentanol + oxidized coenzyme F420
-
-
-
-
r
propanone + reduced coenzyme F420
2-propanol + oxidized coenzyme F420
-
the enzyme is Si-face specific with respect to the C5 atom of coenzyme F420, 2-propanone i.e. acetone
-
-
r
propanone + reduced coenzyme F420
propanol + oxidized coenzyme F420
-
2-propanone i.e. acetone
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-
r
(R)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
-
-
-
r
(R)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
-
-
-
r
(S)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
-
-
-
r
(S)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
-
-
-
r
2-butanone + reduced coenzyme F420
2-butanol + oxidized coenzyme F420
-
-
-
-
r
2-butanone + reduced coenzyme F420
2-butanol + oxidized coenzyme F420
-
-
-
-
r
2-pentanol + oxidized coenzyme F420
2-pentanone + reduced coenzyme F420
-
-
-
-
r
2-pentanol + oxidized coenzyme F420
2-pentanone + reduced coenzyme F420
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-
-
-
r
additional information
?
-
-
activity with ethanol or 1-propanol at the same concentration is only 0.1% compared to activity with 2-propanol. Acetaldehyde and propionaldehyde are reduced at the same rate as 2-propanone
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-
?
additional information
?
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-
the enzyme catalysed the oxidation of various secondary and cyclic alcohols to the corresponding ketones and the reverse reaction. No primary alcohols are oxidized. 1,3-butandiol, glycerol, methanol, ethanol, 1,2-ethandiol, 1 -propanol, 1-amino-2-propanol, 1-butanol, 1-pentanol, 1-hexanol and benzylalcohol are not oxidized nor are the respective aldehydes or ketones reduced
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-
?
additional information
?
-
-
the enzyme catalysed the oxidation of various secondary and cyclic alcohols to the corresponding ketones and the reverse reaction. No primary alcohols are oxidized. 1,3-butandiol, glycerol, methanol, ethanol, 1,2-ethandiol, 1 -propanol, 1-amino-2-propanol, 1-butanol, 1-pentanol, 1-hexanol and benzylalcohol are not oxidized nor are the respective aldehydes or ketones reduced
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
-
pH 3.0: about 30% of maximal activity, pH 7.0: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
-
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
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
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Widdel, F.; Wolfe, R.S.
Expression of secondary alcohol dehydrogenase in methanogenic bacteria and purification of the F420-specific enzyme from Methanogenium thermophilum strain TCI
Arch. Microbiol.
152
322-328
1989
Methanoculleus thermophilus
-
brenda
Bleicher, K.; Winter, J.
Purification and properties of F420- and NADP(+)-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols
Eur. J. Biochem.
200
43-51
1991
Methanofollis liminatans, Methanofollis liminatans DSM 4140
brenda
Klein, A.R.; Berk, H.; Purwantini, E.; Daniels, L.; Thauer, R.K.
Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis and F420-dependent alcohol dehydrogenase from Methanoculleus thermophilicus
Eur. J. Biochem.
239
93-97
1996
Methanoculleus thermophilus
brenda
Aufhammer, S.W.; Warkentin, E.; Berk, H.; Shima, S.; Thauer, R.K.; Ermler, U.
Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family
Structure
12
361-370
2004
Methanoculleus thermophilus (O93734), Methanoculleus thermophilus, Methanoculleus thermophilus DSM 3915 (O93734)
brenda
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