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Literature summary for 3.4.23.51 extracted from

  • Yang, F.; Hu, W.; Xu, H.; Li, C.; Xia, B.; Jin, C.
    Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation (2007), J. Biol. Chem., 282, 3856-3863.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
solution structure of Escherichia coli HycI determined by high resolution nuclear magnetic resonance spectroscopy. The overall structure is similar to the crystal structure of holo-HybD in the same family. HycI shows an open conformation at the putative nickel-binding site, whereas HybD adopts a closed conformation Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ HycI shows an open conformation at the putative nickel-binding site. Ni2+ has lower binding affinity with HycI than that of Cd2+, which is likely required for HycI to dissociate from HycE after the C-terminal processing Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
precursor of the large subunit of hydrogenase 3 + H2O Escherichia coli HycI is an endopeptidase that is responsible for the C-terminal cleavage of the large subunit of hydrogenase 3 in Escherichia coli (UniProt: A1AER2) ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEV9
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
precursor of the large subunit of hydrogenase 3 + H2O HycI is an endopeptidase that is responsible for the C-terminal cleavage of the large subunit of hydrogenase 3 in Escherichia coli (UniProt: A1AER2) Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
HYCI
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Escherichia coli