Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment

Biochemistry

Volumn 45, Issue 32, 2006, Pages 9756-9766

  Hoylaerts, Marc F ^a,b   Ding, Lan ^a   Narisawa, Sonoko ^a   Van Kerckhoven, Soetkin ^b   Millán, José Luis ^a  

^a BURNHAM INSTITUTE   (United States)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBODIES; CATALYSIS; MONOMERS; STRUCTURE (COMPOSITION); SUBSTRATES; THERMODYNAMIC STABILITY;

ACTIVE SITE STRUCTURE STABILIZATION; AMINO ACID MICROENVIRONMENT; INACTIVE ENZYME; MECHANISTIC INTERPRETATION;

ENZYMES;

ALKALINE PHOSPHATASE; ALKALINE PHOSPHATASE PLACENTA ISOENZYME; AMINO ACID; ARGININE; DIMER; ENZYME ANTIBODY; GLUTAMIC ACID; ISOENZYME; MONOMER; PHOSPHATASE; TISSUE NONSPECIFIC ALKALINE PHOSPHATASE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE MUTATION; HUMAN; HYPOPHOSPHATASIA; MAMMAL; MICHAELIS CONSTANT; MICROENVIRONMENT; MOLECULAR INTERACTION; PLACENTA; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION;

ALKALINE PHOSPHATASE; AMINO ACID SUBSTITUTION; AMINO ACIDS; BINDING SITES; CATALYSIS; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; HUMANS; ISOENZYMES; KINETICS; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION; STRUCTURE-ACTIVITY RELATIONSHIP;

MAMMALIA;

EID: 33747475602     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052471+     Document Type: Article

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