Literature summary for 1.17.98.4 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.

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Protein Variants

Protein Variants	Comment	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Oxidation Stability

Oxidation Stability	Organism
enzyme is extremely oxygen-sensitive	Escherichia coli

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
formate dehydrogenase H	-	Escherichia coli

Cofactor

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

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Release 2023.1 (January 2023)