|
Volumn 277, Issue 25, 2002, Pages 22168-22174
|
The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5′-monophosphate cyclohydrolase). A surprising lack of substrate channeling
|
Author keywords
[No Author keywords available]
|
Indexed keywords
BIOSYNTHESIS;
CATALYSIS;
ENZYME KINETICS;
HUMAN ENGINEERING;
PROTEINS;
CYCLOHYDROLASE REACTION;
BIOCHEMISTRY;
5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBONUCLEOTIDE TRANSFORMYLASE INOSINE 5' MONOPHOSPHATE CYCLOHYDROLASE;
CYCLOHYDROLASE;
FORMYLAMINOIMIDAZOLE CARBOXAMIDE RIBONUCLEOTIDE;
FORMYLTRANSFERASE;
HYDROLASE;
INOSINE PHOSPHATE;
PHOSPHORIBOSYLAMINOIMIDAZOLECARBOXAMIDE FORMYLTRANSFERASE;
RIBONUCLEOTIDE;
TETRAHYDROFOLIC ACID;
TRANSFERASE;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
CHEMICAL REACTION KINETICS;
COMPUTER MODEL;
COMPUTER PROGRAM;
COMPUTER SIMULATION;
CONFORMATIONAL TRANSITION;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME KINETICS;
ENZYME MECHANISM;
ENZYME SUBSTRATE COMPLEX;
FLOW KINETICS;
HUMAN;
HUMAN CELL;
PHOTOCHEMICAL QUENCHING;
PRIORITY JOURNAL;
RADIATION ABSORPTION;
REACTION ANALYSIS;
STEADY STATE;
STRUCTURE ACTIVITY RELATION;
BINDING SITES;
CATALYSIS;
HUMANS;
HYDROXYMETHYL AND FORMYL TRANSFERASES;
KINETICS;
MODELS, CHEMICAL;
MULTIENZYME COMPLEXES;
NUCLEOTIDE DEAMINASES;
PROTEIN BINDING;
PROTEIN CONFORMATION;
SPECTROPHOTOMETRY;
TETRAHYDROFOLATES;
TIME FACTORS;
ULTRAVIOLET RAYS;
|
EID: 0037151063
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M111964200 Document Type: Article |
Times cited : (39)
|
References (28)
|