Literature summary for 1.12.99.6 extracted from

Buhrke, T.; Lenz, O.; Krauss, N.; Friedrich, B.
Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site (2005), J. Biol. Chem., 280, 23791-23796.

Search for more literature for 1.12.99.6

Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzymes expressed in Escherichia coli	Cupriavidus necator

Protein Variants

Protein Variants	Comment	Organism
F110L	18% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation	Cupriavidus necator
I62V	6% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation	Cupriavidus necator
I62V/F110L	mutant enzyme shows no H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation	Cupriavidus necator

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	-	-	-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	-	-	-

Oxidation Stability

Oxidation Stability	Organism
oxygen tolerance is based on limited access of oxygen to the active site	Cupriavidus necator

Purification (Commentary)

Purification (Comment)	Organism
-	Cupriavidus necator

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
H2 + acceptor	-	Cupriavidus necator	H+ + reduced acceptor	-	?
H2 + acceptor	-	Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1	H+ + reduced acceptor	-	?

Synonyms

Synonyms	Comment	Organism
H2-sensing [NiFe] hydrogenase	-	Cupriavidus necator

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Release 2023.1 (January 2023)