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Information on EC 1.12.98.1 - coenzyme F420 hydrogenase and Organism(s) Methanothermobacter thermautotrophicus and UniProt Accession P19498

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IUBMB Comments
An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methyl viologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
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This record set is specific for:
Methanothermobacter thermautotrophicus
UNIPROT: P19498 not found.
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Word Map
The taxonomic range for the selected organisms is: Methanothermobacter thermautotrophicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
f420-reducing hydrogenase, f420h2 dehydrogenase, f420-reducing [nife]-hydrogenase, frhagb-encoded hydrogenase, frhabg, 8-hydroxy-5-deazaflavin-reducing hydrogenase, coenzyme f420-dependent hydrogenase, f420-reducing [nife] hydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8-hydroxy-5-deazaflavin-reducing hydrogenase
-
-
-
-
coenzyme F420-dependent hydrogenase
-
-
-
-
coenzyme F420-reducing dehydrogenase
-
-
deazaflavin-reducing hydrogenase
-
-
-
-
F420-reducing hydrogenase
-
-
-
-
hydrogen:(acceptor) oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen:coenzyme F420 oxidoreductase
An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methyl viologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-05-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2 + coenzyme F0
reduced coenzyme F0
show the reaction diagram
H2 + coenzyme F420
reduced coenzyme F420
show the reaction diagram
H2 + methyl viologen
?
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H2 + coenzyme F420
reduced coenzyme F420
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO
-
dead end inhibitor, competitive for H2, uncompetetitive versus F0
coenzyme F0
-
substrate inhibition above 0.05 mM
methyl viologen
-
noncompetitive for F0
Procion Blue HB
-
inhibits F0 reduction
reduced coenzyme F0
-
noncompetitive product inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Procion Blue HB
-
stimulates methyl viologen reduction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026 - 0.034
coenzyme F0
0.019 - 0.036
coenzyme F420
0.002 - 0.012
H2
0.42 - 1.5
methyl viologen
0.1
reduced coenzyme F0
-
anaerobic conditions
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
725 - 2250
coenzyme F0
725 - 2050
coenzyme F420
725 - 4000
methyl viologen
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49
-
purified enzyme, F0-linked activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
-
optimum pH for methyl viologen reduction above pH 11
6.5 - 7.5
-
F420 reduction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
-
increasing methyl viologen activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
smallest species with enzymatic activity, native SDS-PAGE
26000
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
31000
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
47000
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
500000
-
native enzyme bigger than 500000
670000
-
membrane-associated protein complex, native PAGE
790000
-
native SDS-PAGE, sucrose density centrifugation
800000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multimer
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic purification yields the stable but inactive enzyme, can be reactivated under reducing conditions
-
395086
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 year, inactive form maintains 70% of initial activity after reactivation
-
room temperature, activated enzyme loses 20% of inital activity within 24 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aerobic purification causes reversible inhibition with O2
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacobson, F.S.; Daniels, L.; Fox, J.A.; Walsh, C.T.; Orme-Johnson, W.H.
Purification and properties of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum
J. Biol. Chem.
257
3385-3388
1982
Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
Kojima, N.; Fox, J.A.; Hausinger, R.P.; Daniels, L.; Orme-Johnson, W.H.; Walsh, C.
Paramagnetic centers in the nickel-containig, deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum
Proc. Natl. Acad. Sci. USA
80
378-382
1983
Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
Wackett, L.P.; Hartwieg, E.A.; King, J.A.; Orme-Johnson, W.H.; Walsh, C.T.
Electron microscopy of nickel-containing methanogenic enzymes: methyl reductase and F420-reducing hydrogenase
J. Bacteriol.
169
718-727
1987
Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
Fox, J.A.; Livingston, D.J.; Orme-Johnson, W.H.; Walsh, C.T.
8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization
Biochemistry
26
4219-4227
1987
Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
Sprott, G.D.; Shaw, K.M.; Beveridge, T.J.
Properties of the particulate enzyme F420-reducing hydrogenase isolated from Methanospirillum hungatei
Can. J. Microbiol.
33
896-904
1987
Methanothermobacter thermautotrophicus, Methanospirillum hungatei
-
Manually annotated by BRENDA team
Livingston, D.J.; Fox, J.A.; Orme-Johnson, W.H.; Walsh, C.T.
8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 2. Kinetic and hydrogen-transfer studies
Biochemistry
26
4228-4237
1987
Methanothermobacter thermautotrophicus, Methanococcus voltae
Manually annotated by BRENDA team
Alex, L.A.; Reeve, J.N.; Orme-Johnson, W.H.; Walsh, C.T.
Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H
Biochemistry
29
7237-7244
1990
Methanothermobacter thermautotrophicus (P19496 and P19499 and P19498)
Manually annotated by BRENDA team
Tachibana, A.; Tanaka, T.; Taniguchi, M.; Oi, S.
Some properties of F420-reducing hydrogenase of Methanobacterium thermoformicicum strain SF-4
Biosci. Biotechnol. Biochem.
57
156-157
1993
Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
Braks, I.J.; Hoppert, M.; Roge, S.; Mayer, F.
Structural aspects and immunolocalization of the F420-reducing and non-F420-reducing hydrogenases from Methanobacterium thermoautotrophicum Marburg
J. Bacteriol.
176
7677-7687
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
Manually annotated by BRENDA team
de Poorter, L.M.; Geerts, W.J.; Keltjens, J.T.
Hydrogen concentrations in methane-forming cells probed by the ratios of reduced and oxidized coenzyme F420
Microbiology
151
1697-1705
2005
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team
Surin, S.; Cubonova, L.; Majernik, A.I.; Smigan, P.
Amiloride resistance in the methanoarcheon Methanothermobacter thermoautotrophicus: characterization of membrane-associated proteins
Folia Microbiol. (Praha)
51
313-316
2006
Methanothermobacter thermautotrophicus
Manually annotated by BRENDA team