The 3′-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysis

Journal of Biological Chemistry

Volumn 284, Issue 33, 2009, Pages 22184-22194

  Finger, L David ^a,f   Blanchard, M Suzette ^a   Theimer, Carla A ^b   Sengerová, Blanka ^c,d   Singh, Pumiroa ^a   Chavez, Valerie ^a,e   Liu, Fei ^b   Grasby, Jane A ^c   Shen, Binghui ^a,f  

^a CITY OF HOPE NATIONAL MEDICAL CENTER   (United States)

^b STATE UNIVERSITY OF NEW YORK   (United States)

^c UNIVERSITY OF SHEFFIELD   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

^e CEDARS SINAI MEDICAL CENTER   (United States)

^f NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL; BINDING POCKETS; CLEAVAGE SITES; DNA REPLICATIONS; DNA SUBSTRATES; ENZYME PRODUCTS; FLAP ENDONUCLEASE-1; KINETIC STUDY; PHYSIOLOGICAL SALT CONCENTRATIONS; STRUCTURAL STUDIES; SUBSTRATE BINDING; SUBSTRATE RECOGNITION; TURNOVER RATE;

CATALYSIS; DNA; ENZYME INHIBITION; GENES; HYDROLYSIS; NUCLEIC ACIDS; REACTION RATES;

SUBSTRATES;

FLAP ENDONUCLEASE; FLAP ENDONUCLEASE 1; SODIUM CHLORIDE; UNCLASSIFIED DRUG; POTASSIUM CHLORIDE;

ARTICLE; CATALYSIS; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME METABOLISM; ENZYME MODIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HUMAN; MOLECULAR RECOGNITION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN HYDROLYSIS; CHEMISTRY; CONFORMATION; ENZYME SPECIFICITY; GENETICS; HYDROLYSIS; KINETICS; MOLECULAR GENETICS; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS;

ARCHAEA; EUKARYOTA; MUS;

BASE SEQUENCE; CATALYSIS; FLAP ENDONUCLEASES; HUMANS; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PHOSPHORYLATION; POTASSIUM CHLORIDE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 69249114613     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.015065     Document Type: Article

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