The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: A refined mechanism of serine protease action

Journal of Biological Chemistry

Volumn 286, Issue 5, 2011, Pages 3587-3596

  Wahlgren, Weixiao Yuan ^a   Pál, Gábor ^b   Kardos, József ^b   Porrogi, Pálma ^b   Szenthe, Borbála ^b   Patthy, András ^b   Gráf, László ^b   Katona, Gergely ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

A-DENSITY; ACTIVE SITE; ASPARTATE RESIDUE; ASPARTATES; CARBOXYL GROUPS; CATALYTIC CYCLES; CATALYTIC RESIDUE; CHARGED AMINO ACIDS; DOUBLE BONDS; ELECTRON DENSITIES; ENZYME CATALYSIS; EXPERIMENTAL OBSERVATION; HYDROGEN ATOMS; IN-VITRO; MICHAELIS COMPLEX; NEUTRAL STATE; PROTONATED; PROTONATED HISTIDINE; PROTONATION STATE; SERINE PROTEASE; SUBSTRATE-BOUND; SUBSTRATE-LIKE INHIBITORS; TETRAHEDRAL INTERMEDIATES; ULTRAHIGH RESOLUTION; X-RAY STRUCTURE;

AMINO ACIDS; CARRIER CONCENTRATION; ELECTRON DENSITY MEASUREMENT; ELECTRONS; HYDROGEN; HYDROGEN BONDS; HYDROLASES; PROTONATION; PROTONS;

DENSITY FUNCTIONAL THEORY;

ASPARAGINE; ASPARTIC ACID; HISTIDINE; SERINE; SERINE PROTEINASE; TRYPSIN; INSECT PROTEIN; PROTON; SGTI PROTEIN, SCHISTOCERCA GREGARIA;

ANISOTROPY; ARTICLE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DENSITY FUNCTIONAL THEORY; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME STABILITY; HYDROGEN BOND; IN VITRO STUDY; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; X RAY CRYSTALLOGRAPHY; ANIMAL; CHEMISTRY; GENETICS; METABOLISM; MISSENSE MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION;

ANIMALS; ASPARTIC ACID; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; INSECT PROTEINS; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTONS; SERINE PROTEASES; TRYPSIN;

EID: 79952784475     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.161604     Document Type: Article

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