Literature summary for 1.12.99.6 extracted from

Sasaki, D.; Watanabe, S.; Kanai, T.; Atomi, H.; Imanaka, T.; Miki, K.
Characterization and in vitro interaction study of a [NiFe] hydrogenase large subunit from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (2012), Biochem. Biophys. Res. Commun., 417, 192-196.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermococcus kodakarensis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Thermococcus kodakarensis	5829	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	contains 0.23 Fe atoms per molecule of large subunit HyhL	Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
48300	-	and 96600, gel filtration	Thermococcus kodakarensis
96600	-	and 48300, gel filtration	Thermococcus kodakarensis

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	Q8NKS2	alpha subunit	-

Purification (Commentary)

Purification (Comment)	Organism
cytosolic [NiFe] hydrogenase large subunit HyhL	Thermococcus kodakarensis

Subunits

Subunits	Comment	Organism
dimer	2 * 48300, calculated, 2 * 48300, gel filtration. Enzyme exists in equilibrium between dimer and monomer	Thermococcus kodakarensis
monomer	1 * 48300, calculated, 1 * 48300, gel filtration. Enzyme exists in equilibrium between dimer and monomer	Thermococcus kodakarensis
More	subunit HyhL forms a tight 1:1 binary complex with hydrogenase HypA and weakly interacts with HypC	Thermococcus kodakarensis

Synonyms

Synonyms	Comment	Organism
HyhL	large subunit	Thermococcus kodakarensis
[NiFe] hydrogenase	-	Thermococcus kodakarensis

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Release 2023.1 (January 2023)