Entry |
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Name |
coenzyme F420 hydrogenase;
8-hydroxy-5-deazaflavin-reducing hydrogenase;
F420-reducing hydrogenase;
coenzyme F420-dependent hydrogenase
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Class |
Oxidoreductases;
Acting on hydrogen as donor;
With other, known, physiological acceptors
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Sysname |
hydrogen:coenzyme F420 oxidoreductase
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Reaction(IUBMB) |
H2 + oxidized coenzyme F420 = reduced coenzyme F420 [RN: R03025]
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Reaction(KEGG) |
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Substrate |
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Product |
reduced coenzyme F420 [CPD: C01080]
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Comment |
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 methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
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History |
EC 1.12.98.1 created 1989 as EC 1.12.99.1, transferred 2002 to EC 1.12.98.1
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Pathway |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K00440 | coenzyme F420 hydrogenase subunit alpha |
K00441 | coenzyme F420 hydrogenase subunit beta |
K00443 | coenzyme F420 hydrogenase subunit gamma |
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Genes |
» show all
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Reference |
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Authors |
Adams MW, Mortenson LE, Chen JS. |
Title |
Hydrogenase. |
Journal |
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Reference |
|
Authors |
Yamazaki S. |
Title |
A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue. |
Journal |
J Biol Chem 257:7926-9 (1982) |
Reference |
|
Authors |
Fox JA, Livingston DJ, Orme-Johnson WH, Walsh CT. |
Title |
8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization. |
Journal |
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Sequence |
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Reference |
|
Authors |
Muth E, Morschel E, Klein A. |
Title |
Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae. |
Journal |
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Reference |
|
Authors |
Baron SF, Ferry JG. |
Title |
Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum. |
Journal |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 1.12.98.1 |
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