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Literature summary extracted from

  • Schiffels, J.; Pinkenburg, O.; Schelden, M.; Aboulnaga, e.l.-.H.A.; Baumann, M.E.; Selmer, T.
    An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from Cupriavidus necator in Escherichia coli (2013), PLoS ONE, 8, e68812.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.12.1.2 synthesis system for cloning and expression of multiple genes in Escherichia coli BL21 demonstrate tby production and maturation of the NAD+reducing soluble [NiFe]-hydrogenase from Cupriavidus necator H16. The enzyme encoded in hoxFUYHI is successfully matured by co-expression of a dedicated set of auxiliary genes, comprising seven hyp genes (hypC1D1E1A2B2F2X) along with hoxW, which encodes a specific endopeptidase. Deletion of genes involved in enzyme maturation reduces maturation efficiency substantially. Further addition of hoxN1, encoding a high-affinity nickel permease, considerably increases maturation efficiency in Escherichia coli Cupriavidus necator

Organism

EC Number Organism UniProt Comment Textmining
1.12.1.2 Cupriavidus necator
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.12.1.2 230
-
 recombinant protein, pH 8.0, temperature not specified in the publication Cupriavidus necator

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.1.2 H2 + NAD+
-
 Cupriavidus necator H+ + NADH
-
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