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Literature summary for 3.4.23.51 extracted from

  • Kumarevel, T.; Tanaka, T.; Bessho, Y.; Shinkai, A.; Yokoyama, S.
    Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli (2009), Biochem. Biophys. Res. Commun., 389, 310-314.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli K-12

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 28% (w/v) polyethylene glycol 400, 0.2 M CaCl2, and 0.1 M Na-HEPES (pH 7.5), at 20°C Escherichia coli K-12

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
-
Escherichia coli K-12

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12 P0AEV9
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap HP5 column chromatography, HiPrep column chromatography, and Superdex 200 gel filtration Escherichia coli K-12

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
precursor of the large subunit of hydrogenase 3 + H2O the HycI endopeptidase is involved in the C-terminal processing of the large subunit of hydrogenase 3 (HycE) Escherichia coli K-12 ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 17000, HycI exists as a monomer in solution, X-ray crystallography Escherichia coli K-12

Synonyms

Synonyms Comment Organism
HycI endopeptidase
-
Escherichia coli K-12

pI Value

Organism Comment pI Value Maximum pI Value
Escherichia coli K-12 calculated from amino acid sequence
-
3.7