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Information on EC 1.1.98.5 - secondary-alcohol dehydrogenase (coenzyme-F420)
for references in articles please use BRENDA:EC1.1.98.5
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.98 With other, known, physiological acceptors
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.
The expected taxonomic range for this enzyme is: Methanomicrobiaceae
- 1.1.98.5
-
methanoculleus
-
methanogen
- isopropanol
-
prochiral
- archaea
-
re-face
- ketones
showSynonyms
f420-dependent alcohol dehydrogenase, more
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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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PATHWAY SOURCE
PATHWAYS
MetaCyc
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phenylpropan-1-one + reduced coenzyme F420
(S)-1-phenylpropan-1-ol + oxidized coenzyme F420
Substrates: the (S)-alcohol is obtained in excellent enantiopurity (above 99% ee)
Products: -
Products: -
?
2-pentanol + oxidized coenzyme F420
2-pentanone + reduced coenzyme F420
-
Substrates: -
Products: -
Products: -
r
2-pentanone + reduced coenzyme F420
2-pentanol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
r
2-propanol + oxidized coenzyme F420
propanone + reduced coenzyme F420
-
Substrates: -
Products: propanone i.e. acetone
Products: propanone i.e. acetone
r
4-methylpentan-2-one + reduced coenzyme F420
(S)-4-methylpentan-2-ol + oxidized coenzyme F420
Substrates: the (S)-alcohol is obtained in excellent enantiopurity (above 99% ee)
Products: -
Products: -
?
acetophenone + reduced coenzyme F420
(S)-1-phenylethanol + oxidized coenzyme F420
Substrates: the (S)-alcohol is obtained in excellent enantiopurity (above 99% ee)
Products: -
Products: -
?
cyclopentanol + oxidized coenzyme F420
cyclopentanone + reduced coenzyme F420
-
Substrates: -
Products: -
Products: -
r
cyclopentanone + reduced coenzyme F420
cyclopentanol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
r
methoxyacetone + reduced coenzyme F420
(2S)-1-methoxypropan-2-ol + oxidized coenzyme F420
Substrates: the (S)-alcohol is obtained in excellent enantiopurity (above 99% ee)
Products: -
Products: -
?
octan-3-one + reduced coenzyme F420
(S)-3-octanol + oxidized coenzyme F420
Substrates: the (S)-alcohol is obtained in excellent enantiopurity (above 99% ee)
Products: -
Products: -
?
pentan-2-one + reduced coenzyme F420
(S)-2-pentanol + oxidized coenzyme F420
Substrates: -
Products: -
Products: -
?
(R)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
Substrates: -
Products: -
Products: -
r
(R)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
Substrates: -
Products: -
Products: -
r
(S)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
Substrates: -
Products: -
Products: -
r
(S)-2-butanol + oxidized coenzyme F420
2-butanone + reduced coenzyme F420
-
Substrates: -
Products: -
Products: -
r
2-butanone + reduced coenzyme F420
2-butanol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
r
2-butanone + reduced coenzyme F420
2-butanol + oxidized coenzyme F420
-
Substrates: -
Products: -
Products: -
r
2-propanol + oxidized coenzyme F420
2-propanone + reduced coenzyme F420
-
Substrates: -
Products: 2-propanone i.e. acetone
Products: 2-propanone i.e. acetone
r
2-propanol + oxidized coenzyme F420
2-propanone + reduced coenzyme F420
-
Substrates: -
Products: 2-propanone i.e. acetone
Products: 2-propanone i.e. acetone
r
propanone + reduced coenzyme F420
2-propanol + oxidized coenzyme F420
-
Substrates: the enzyme is Si-face specific with respect to the C5 atom of coenzyme F420, 2-propanone i.e. acetone
Products: -
Products: -
r
propanone + reduced coenzyme F420
2-propanol + oxidized coenzyme F420
-
Substrates: 2-propanone i.e. acetone
Products: -
Products: -
r
propanone + reduced coenzyme F420
2-propanol + oxidized coenzyme F420
-
Substrates: 2-propanone i.e. acetone
Products: -
Products: -
r
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). O93734_9EURY
330
0
37158
TrEMBL
Secretory Pathway (Reliability: 1)
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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)
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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
Martin, C.; Tjallinks, G.; Trajkovic, M.; Fraaije, M.W.
Facile stereoselective reduction of prochiral ketones by using an F420-dependent alcohol dehydrogenase
ChemBioChem
22
156-159
2021
Methanoculleus thermophilus (O93734), Methanoculleus thermophilus
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.98.5)
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