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Information on EC 1.12.98.1 - coenzyme F420 hydrogenase and Organism(s) Methanosarcina barkeri and UniProt Accession P80490

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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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Methanosarcina barkeri
UNIPROT: P80490
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The taxonomic range for the selected organisms is: Methanosarcina barkeri
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-reactive hydrogenase
-
8-hydroxy-5-deazaflavin-reducing hydrogenase
-
-
-
-
coenzyme F420-dependent hydrogenase
-
-
-
-
deazaflavin-reducing hydrogenase
-
-
-
-
F420-reducing hydrogenase
hydrogen:(acceptor) oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
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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 F420
reduced coenzyme F420
show the reaction diagram
H2 + oxidized benzyl viologen
reduced benzyl viologen
show the reaction diagram
-
-
-
?
H2 + oxidized coenzyme F0
reduced coenzyme F20
show the reaction diagram
cofactor F0 i.e. 7,8-didemethy1-8-hydroxy-S-deazaflavin
-
-
?
H2 + oxidized coenzyme F420
reduced coenzyme F420
show the reaction diagram
H2 + oxidized methyl viologen
reduced 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
H2 + oxidized coenzyme F420
reduced coenzyme F420
show the reaction diagram
H2 + oxidized methyl viologen
reduced methyl viologen
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
1 mol of the 198000 Da enzyme form contains 2 mol of FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
1 mol of the 198000 Da enzyme form contains 28-32 mol of non-heme iron
KCl
increases activity, maximal activity at 250 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.004
H2
0.025
oxidized coenzyme F420
37°C, pH 7.5
0.0033
oxidized methyl viologen
37°C, pH 8.3
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
353
oxidized coenzyme F420
37°C, pH 7.5
9226
oxidized methyl viologen
37°C, pH 8.3
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25000 - 69000
H2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.34
-
growth with H2 and CO2, enzyme activity depends on growth substrate
0.437
-
growth on methanol, enzyme activity depends on growth substrate
11.5
37°C, pH 7.5, substrate: oxidized coenzyme F420
82.8
37°C, pH 7.2, cosubstrate: oxidized coenzyme F420
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.25
deazaflavin reducing activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
the methylviologen-reducing activity increased with pH from pH 5.5-10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
loss of F420H2 dehydrogenase, and therefore of the 420H2:heterodisulfide oxidoreductase system, does not measurably affect methanogenesis or growth in Methanosarcina barkeri
metabolism
-
the preferred electron transport chain involves production of hydrogen gas in the cytoplasm, which then diffuses out of the cell, where it is reoxidized with transfer of electrons into the energy-conserving electron transport chain. This hydrogen-cycling metabolism leads directly to production of a proton motive force that can be used by the cell for ATP synthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
198000
30000
33000
48000
2 * 48000 (alpha) + 2 * 33000 (beta) + 2 * 30000 (gamma)
8000
x * 8000 + x * 33000 + x * 30000, SDS-PAGE
845000
non-denaturing PAGE, large enzyme form
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 8000 + x * 33000 + x * 30000, SDS-PAGE
hexamer
2 * 48000 (alpha) + 2 * 33000 (beta) + 2 * 30000 (gamma)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Methanosarcina barkeri Delta fpo mutants: strain WWM85 Delta hpt::PmcrB-Phi C31int-attP, strain WWM86 Delta hpt::PmcrB-Phi C31int-attB, strain WWM71 Delta hpt::PmcrB-Phi C31int-attB, Delta fpoA-O Deletion of fpo by markerless exchange with pDK4 in WWM86, strain WWM123 Delta hpt::PmcrB-Phi C31int-attP, Delta fpoF Deletion of fpoF by markerless exchange with pDK13 in WWM85, strain WWM116 Delta hpt::PmcrB-Phi C31int-attP, Delta freAEGB Deletion of fre by markerless exchange with pGK6 in WWM85, strain WWM122 Delta hpt::PmcrB-Phi C31int-attB, Delta frhADGB::pac-hpt Deletion of frh with ApaI/NotI-digested pAMG81 in WWM86, strain WWM108 Delta hpt::PmcrB-Phi C31int-attB, Delta fpoA-O, Delta frhADGB::pac-hpt Deletion of frh with ApaI/NotI-digested pAMG81 in WWM71, strain WWM145 Delta hpt::PmcrB-Delta C31int-attP, Delta fpoF, Delta frhADGB::pac-hpt Deletion of frh with ApaI/NotI-digested pAMG81 in WWM123
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is unstable under reducing conditions
727399
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mukhopadhyay, B.; Purwantini, E.; Daniels, L.
Effect of methanogenic substrates on coenzyme f420-dependent N5,N10-methylene-H4MPT dehydrogenase, N5,N10-methenyl-H4MPT cyclohydrolase and F420-reducing hydrogenase activities in Methanosarcina barkeri
Arch. Microbiol.
159
141-146
1993
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
-
Manually annotated by BRENDA team
Michel, R.; Massanz, C.; Kostka, S.; Richter, M.; Fiebig, K.
Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro
Eur. J. Biochem.
233
727-735
1995
Methanosarcina barkeri (P80490 and P80489 and P80491), Methanosarcina barkeri DSM 804 (P80490 and P80489 and P80491)
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
Kulkarni, G.; Kridelbaugh, D.; Guss, A.; Metcalf, W.
Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri
Proc. Natl. Acad. Sci. USA
106
15915-15920
2009
Methanosarcina barkeri
Manually annotated by BRENDA team
Fiebig, K.; Friedrich, B.
Purification of the F420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro)
Eur. J. Biochem.
184
79-88
1989
Methanosarcina barkeri (P80490 and P80489 and P80491), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (P80490 and P80489 and P80491)
Manually annotated by BRENDA team