Mostrando 1 - 5 Resultados de 5 Para Buscar 'Clan Casalesi~', tiempo de consulta: 2.05s Limitar resultados
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    “…GHs’ active sites may be described as a combination of subsites dedicated to the binding of individual sugar residues and to catalysis. The three-dimensional structure of GH:carbohydrate complexes has demonstrated that carbohydrate ring conformation changes in an ordered manner during catalysis. …”
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    Intrinsic dynamic behavior of enzyme:substrate complexes govern the catalytic action of β-galactosidases across clan GH-A
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    Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites
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    Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases
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    A Parasite Cysteine Protease Is Key to Host Protein Degradation and Iron Acquisition
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    “…[Image: see text] Retaining glycoside hydrolases use acid/base catalysis with an enzymatic acid/base protonating the glycosidic bond oxygen to facilitate leaving-group departure alongside attack by a catalytic nucleophile to form a covalent intermediate. …”
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    Reaction Mechanism of Glycoside Hydrolase Family 116 Utilizes Perpendicular Protonation
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