Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.12.98.1 extracted from

  • Baron, S.F.; Brown, D.P.; Ferry, J.G.
    Locations of the hydrogenases of Methanobacterium formicicum after subcellular fractionation of cell extract (1987), J. Bacteriol., 169, 3823-3825.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
FAD restores activity after depletion of FAD in hydrophobic interaction chromatography Methanobacterium formicicum

General Stability

General Stability Organism
0.03 mM FAD stabilizes enzyme Methanobacterium formicicum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane associated Methanobacterium formicicum 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
790000
-
biggest enzyme species, aggregate Methanobacterium formicicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2 + coenzyme F420 Methanobacterium formicicum enzyme of methanogenesis pathway reduced coenzyme F420
-
?

Organism

Organism UniProt Comment Textmining
Methanobacterium formicicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanobacterium formicicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + coenzyme F420
-
Methanobacterium formicicum reduced coenzyme F420
-
?
H2 + coenzyme F420 enzyme of methanogenesis pathway Methanobacterium formicicum reduced coenzyme F420
-
?
H2 + methyl viologen
-
Methanobacterium formicicum ?
-
?

Cofactor

Cofactor Comment Organism Structure
FAD bound to protein, depleted by hydrophobic interaction chromatography Methanobacterium formicicum
FAD FAD depleted enzyme reduces methyl viologen but not F420 Methanobacterium formicicum