1.12.98.1: coenzyme F420 hydrogenase
This is an abbreviated version!
For detailed information about coenzyme F420 hydrogenase, go to the full flat file.
Word Map on EC 1.12.98.1
-
1.12.98.1
-
methanogen
-
methanobacterium
-
thermoautotrophicum
-
methanococcus
-
hydrogenases
-
nife-hydrogenase
-
viologens
-
methanogenesis
-
heterodisulfide
-
nickel-containing
-
barkeri
-
voltae
-
fusaro
-
si-face
-
methanothermobacter
-
n5,n10-methylenetetrahydromethanopterin
-
formicicum
-
methylenetetrahydromethanopterin
-
hydrogen-dependent
-
h2-forming
- 1.12.98.1
-
methanogen
- methanobacterium
- thermoautotrophicum
-
methanococcus
- hydrogenases
- nife-hydrogenase
- viologens
-
methanogenesis
-
heterodisulfide
-
nickel-containing
- barkeri
- voltae
- fusaro
-
si-face
-
methanothermobacter
- n5,n10-methylenetetrahydromethanopterin
- formicicum
- methylenetetrahydromethanopterin
-
hydrogen-dependent
-
h2-forming
Reaction
Synonyms
8-hydroxy-5-deazaflavin-reactive hydrogenase, 8-hydroxy-5-deazaflavin-reducing hydrogenase, coenzyme F420-dependent hydrogenase, coenzyme F420-reducing dehydrogenase, deazaflavin-reducing hydrogenase, EC 1.12.99.1, F420-reducing hydrogenase, F420-reducing [NiFe] hydrogenase, F420-reducing [NiFe]-hydrogenase, F420H2 dehydrogenase, Fpo, FRH, FrhABC, FrhABG, frhAGB-encoded hydrogenase, hydrogen:(acceptor) oxidoreductase, Mbar_A0449, Mbar_A0450, Mbar_A0452, TON_1559, TON_1560, TON_1561, VhuD
ECTree
Advanced search results
Subunits
Subunits on EC 1.12.98.1 - coenzyme F420 hydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
heterotrimer
hexamer
multimer
additional information
heterotrimer
B6YTV8; B6YTV9; B6YTW0, B6YTV8; B6YTV9; B6YTW0 AND
alphabetagamma, 1 * 43000, alpha-subunit, + 1 * 30000, beta-subunit, + 1 * 25000, gamma-subunit, SDS-PAGE
2 * 48000 (alpha) + 2 * 33000 (beta) + 2 * 30000 (gamma)
-
alpha,beta,gamma 43600 + 36700 + 28000, SDS-PAGE, exact subunit composition not known, ratio 1:1:1 postulated
multimer
-
alpha,beta,gamma 42600 + 23500 + 35000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 42600 + 23500 + 35000, SDS-PAGE, exact subunit composition not known
-
multimer
-
alpha,beta,gamma 48000 + 32000 + 25000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 56000 + 42000 + 35000, SDS-PAGE, three subunit species found but exact subunit composition not known
multimer
-
alpha,beta,gamma,delta 55000 + 45000 + 37000 + 27000, SDS-PAGE, exact subunit composition not known, function of delta subunit not known
multimer
-
alpha,beta 5 * 50700 + 15 * 30700, SDS-PAGE, electron microscopy
multimer
alpha,beta,gamma,delta 44700 + 30700 + 25700 + 17600, calculated from DNA sequence, SDS-PAGE, delta subunit not visible in SDS-PAGE, exact subunit composition not known, function of delta subunit not known
multimer
-
alpha,beta,gamma 48000 + 33000 + 27000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 45000 + 31000 + 28000, SDS-PAGE, exact subunit composition not known
multimer
-
alpha,beta,gamma 8 * 47000 + 8 * 31000 + 8 * 26000, SDS-PAGE
multimer
-
ratio alpha, beta, gamma postulated to be 1:1:1
multimer
-
alpha,beta,gamma 40000 + 31000 + 26000, SDS-PAGE, exact subunit composition not known, ratio 2:2:1 leading to MW 170000
multimer
-
alpha,beta,gamma 48000 + 33000 + 27000, SDS-PAGE, exact subunit composition not known
-
the delta subunit of hydrogenase VhuD is central to the interaction of formate dehydrogenase Fdh and heterodisulfide reductase-associated hydrogenase Vhu with heterodisulfide reductase HdrA. Under conditions where both Fdh and Vhu are expressed, these enzymes compete for binding to VhuD, which in turn binds to HdrA. Under these conditions, both enzymes are fully functional and are bound to VhuD in substoichiometric quantities. Fdh copurifies specifically with VhuD in the absence of other hydrogenase subunits
additional information
-
the delta subunit of hydrogenase VhuD is central to the interaction of formate dehydrogenase Fdh and heterodisulfide reductase-associated hydrogenase Vhu with heterodisulfide reductase HdrA. Under conditions where both Fdh and Vhu are expressed, these enzymes compete for binding to VhuD, which in turn binds to HdrA. Under these conditions, both enzymes are fully functional and are bound to VhuD in substoichiometric quantities. Fdh copurifies specifically with VhuD in the absence of other hydrogenase subunits
additional information
B6YTV8; B6YTV9; B6YTW0
enzyme peptide fingerprinting using matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS) analysis
additional information
B6YTV8; B6YTV9; B6YTW0 AND
enzyme peptide fingerprinting using matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS) analysis
additional information
B6YTV8; B6YTV9; B6YTW0
the Frh enzymes are encoded by the frhAGB genes and are heterotrimers composed of an alpha-subunit (FrhA) with a binuclear [Ni-Fe] center, a beta-subunit (FrhG) with three [4Fe-4S] clusters, and a gamma-subunit (FrhB) with one [4Fe-4S] cluster and one flavin adenine dinucleotide (FAD) as a prosthetic group
additional information
B6YTV8; B6YTV9; B6YTW0 AND
the Frh enzymes are encoded by the frhAGB genes and are heterotrimers composed of an alpha-subunit (FrhA) with a binuclear [Ni-Fe] center, a beta-subunit (FrhG) with three [4Fe-4S] clusters, and a gamma-subunit (FrhB) with one [4Fe-4S] cluster and one flavin adenine dinucleotide (FAD) as a prosthetic group