Alternative catalytic anions differentially modulate human α-amylase activity and specificity

Biochemistry

Volumn 47, Issue 11, 2008, Pages 3332-3344

  Maurus, Robert ^a   Begum, Anjuman ^a   Williams, Leslie K ^a   Fredriksen, Jason R ^a   Zhang, Ran ^a   Withers, Stephen G ^a   Brayer, Gary D ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CATALYST ACTIVITY; METAL IONS; NEGATIVE IONS; PLASTICITY;

ANION SUBSTITUTIONS; CATALYTIC ANIONS; POLYATOMIC NATURES;

ENZYME ACTIVITY;

AMYLASE; AZIDE; CHLORIDE; NITRATE; NITRITE;

ALLOSTERISM; ARTICLE; BINDING SITE; CATALYSIS; ELECTRICITY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HUMAN; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ALLOSTERIC REGULATION; ALPHA-AMYLASE; ASPARAGINE; AZIDES; CATALYSIS; CHLORIDES; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENZYME ACTIVATION; HUMANS; HYDROGEN-ION CONCENTRATION; NITRATES; NITRITES; PICHIA; PROTEIN BINDING; RECOMBINANT PROTEINS; SERINE; SUBSTRATE SPECIFICITY;

EID: 40849087951     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701652t     Document Type: Article

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