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Literature summary for 1.12.1.2 extracted from

  • van der Linden, E.; Burgdorf, T.; de Lacey, A.L.; Buhrke, T.; Scholte, M.; Fernandez, V.M.; Friedrich, B.; Albracht, S.P.
    An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties (2006), J. Biol. Inorg. Chem., 11, 247-260.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
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Cupriavidus necator
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Organism

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

Oxidation Stability Organism
air the presence of NADH leads to rapid destruction of the hexameric enzyme Cupriavidus necator
the hexameric SH preparation is both active and stable in the presence of NADPH and air Cupriavidus necator

Purification (Commentary)

Purification (Comment) Organism
improved purification procedure Cupriavidus necator

Source Tissue

Source Tissue Comment Organism Textmining
additional information cells are grown heterotrophically in a fructose-glycerol minimal medium Cupriavidus necator
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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Cupriavidus necator

Synonyms

Synonyms Comment Organism
HoxFUYHI2 hexameric enzyme form Cupriavidus necator
NAD+-reducing [NiFe]-hydrogenase
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Cupriavidus necator