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Literature summary extracted from

  • Gladyshev, V.N.; Khangulov, S.V.; Axley, M.J.; Stadtman, T.C.
    Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli (1994), Proc. Natl. Acad. Sci. USA, 91, 7708-7711.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.17.98.4 Sec140Cys mutant enzyme with cysteine substituted at position 140 for the selenocysteine residue has decreased catalytic activity and exhibits a different EPR signal Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.98.4 Mo molybdopterin containg enzyme, Mo is coordinated with the Se atom of selenocysteine Escherichia coli
1.17.98.4 Se Mo of the molybdopterin is coordinated with the Se atom of selenocysteine Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.17.98.4 Escherichia coli
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.17.98.4 enzyme is extremely oxygen-sensitive Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.98.4
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.17.98.4 formate dehydrogenase H
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.98.4 molybdopterin molybdopterin containg enzyme, Mo is coordinated with the Se atom of selenocysteine Escherichia coli