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Volumn 132, Issue 14, 2010, Pages 5114-5120
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An active-site phenylalanine directs substrate binding and C-H cleavage in the α-ketoglutarate-dependent dioxygenase AauD
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Author keywords
[No Author keywords available]
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Indexed keywords
ACTIVE SITE;
C-H BOND;
C-H BOND CLEAVAGE;
DEUTERIUM KINETIC ISOTOPE EFFECT;
DIOXYGENASES;
HYDROGEN DONOR;
HYDROGEN-ATOM TRANSFER;
HYDROPHOBIC CORE;
INTERNUCLEAR DISTANCES;
KETOGLUTARATE;
OXYGEN ACTIVATIONS;
SIDE CHAINS;
SUBSTRATE BINDING;
SUBSTRATE-DEPENDENT PROCESS;
WILD TYPES;
AMINO ACIDS;
DEUTERIUM;
HYDROGEN BONDS;
HYDROPHOBICITY;
OXYGEN;
SUBSTRATES;
2 OXOGLUTARIC ACID;
AMINO ACID;
CARBON;
DEUTERIUM;
DIOXYGENASE;
HYDROGEN;
OXYGEN;
PHENYLALANINE;
TAUD PROTEIN;
TAURINE;
TAURINE ALPHA KETOGLUTARATE DIOXGENASE;
UNCLASSIFIED DRUG;
VALINE;
ARTICLE;
CHEMICAL REACTION;
CHEMICAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME BINDING;
ENZYME KINETICS;
ENZYME SUBSTRATE;
HYDROPHOBICITY;
PROTEIN EXPRESSION;
QUANTUM MECHANICS;
STEADY STATE;
CARBON;
CATALYTIC DOMAIN;
FERROUS COMPOUNDS;
HYDROGEN;
KINETICS;
MIXED FUNCTION OXYGENASES;
MODELS, MOLECULAR;
PHENYLALANINE;
SUBSTRATE SPECIFICITY;
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EID: 77950817925
PISSN: 00027863
EISSN: 15205126
Source Type: Journal
DOI: 10.1021/ja909416z Document Type: Article |
Times cited : (28)
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References (33)
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