Enzyme

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     1. Oxidoreductases
        1.12 Acting on hydrogen as donor
            1.12.98 With other, known, physiological acceptors
ID:1.12.98.3
Description:Methanosarcina-phenazine hydrogenase.
Alternative Name: Methylviologen-reducing hydrogenase.
Methanophenazine hydrogenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.12.98.3
BRENDA Enzyme Link: BRENDA 1.12.98.3
KEGG Enzyme Link: KEGG1.12.98.3
BioCyc Enzyme Link: BioCyc 1.12.98.3
ExPASy Enzyme Link: ExPASy1.12.98.3
EC2PDB Enzyme Link: EC2PDB 1.12.98.3
ExplorEnz Enzyme Link: ExplorEnz 1.12.98.3
PRIAM enzyme-specific profiles Link: PRIAM 1.12.98.3
IntEnz Enzyme Link: IntEnz 1.12.98.3
MEDLINE Enzyme Link: MEDLINE 1.12.98.3
MSA:

1.12.98.3;

Phylogenetic Tree:

1.12.98.3;

Uniprot:
M-CSA:
RHEA:24436 H2 + methanophenazine = dihydromethanophenazine
RULE(radius=1) [*:1]1:[*:2]:[n;H0;+0:3]:[*:4]:[*:5]:[n;H0;+0:6]:1.[H;H0;+0:7]-[H;H0;+0:8]>>[*:1]1:[*:2]-[NH;+0:3]-[*:4]:[*:5]-[NH;+0:6]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1.Abken HJ, Tietze M, Brodersen J, Bäumer S, Beifuss U, Deppenmeier U1998 Apr9555882
Methanophenazine: Structure, Total Synthesis, and Function of a New Cofactor from Methanogenic Archaea This work was supported by the Deutsche Forschungsgemeinschaft (Sonderforschungsbereich 416; grants De 488/6-1 and De 488/4-2) and the Fonds der Chemischen Industrie. We are grateful to Drs. J. Paust and H. Jaedicke (BASF AG, Ludwigshafen) and Dr. R. K. Müller (Hoffmann-La Roche Ltd., Basel) for generously providing chemicals.Beifuss U, Tietze M, Bäumer S, Deppenmeier U2000 Jul 1710941105
Novel reactions involved in energy conservation by methanogenic archaea.Deppenmeier U, Lienard T, Gottschalk G1999 Sep 310471795