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Literature summary for 3.1.1.1 extracted from

  • Bencharit, S.; Edwards, C.C.; Morton, C.L.; Howard-Williams, E.L.; Kuhn, P.; Potter, P.M.; Redinbo, M.R.
    Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1 (2006), J. Mol. Biol., 363, 201-214.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with coenzyme A, palmitate, cholate and taurocholate. Enzyme contains two additional ligand binding sites, each exhibiting relatively non-specific ligand binding properties. Catalytic triad is formed by residues S221, H468 and E354 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform hCE1
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein crystallization data, high-mannose N-linked glycosylation at N79 Homo sapiens