Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: Effect of the basicity of an active site his residue

Journal of Biological Chemistry

Volumn 289, Issue 12, 2014, Pages 8620-8632

  Hernandez Ortega, Aitor ^a   Quesne, Matthew G ^a   Bui, Soi ^b   Heuts, Dominic P H M ^a,c   Steiner, Roberto A ^b   Heyes, Derren J ^a   De Visser, Sam P ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b KING'S COLLEGE LONDON   (United Kingdom)

^c ROTTERDAM UNIVERSITY OF APPLIED SCIENCES   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINITY; DEPROTONATION; ISOTOPES; OXYGEN; PH EFFECTS;

CATALYTIC CYCLES; COMPUTATIONAL APPROACH; COMPUTATIONAL STUDIES; COMPUTATIONAL WORK; METABOLIC PATHWAYS; ORGANIC COFACTORS; SOLVENT ISOTOPE EFFECTS; STEADY-STATE CONDITION;

SUBSTRATES;

(1H) 3 HYDROXY 4 OXOQUINALDINE 2,4 DIOXYGENASE; ASPARTIC ACID; DIOXYGENASE; HISTIDINE; HYDROXYL GROUP; OXYGEN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BASICITY; CATALYSIS; CONTROLLED STUDY; DEPROTONATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; OXYGENATION; PH; PRIORITY JOURNAL; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; STEADY STATE;

DFT CALCULATIONS; ENZYME KINETICS; ENZYME MECHANISMS; ISOTOPE EFFECTS; MOLECULAR DYNAMICS; QUANTUM MECHANICS/MOLECULAR MECHANICS; SITE-DIRECTED MUTAGENESIS;

ARTHROBACTER; CATALYTIC DOMAIN; DIOXYGENASES; HISTIDINE; KINETICS; MOLECULAR DYNAMICS SIMULATION; PROTONS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

EID: 84896922255     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.543033     Document Type: Article

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