Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 9, 2011, Pages 3554-3559

  Due, Anne V ^a,c   Kuper, Jochen ^a,d   Geerlof, Arie ^a,e   Von Kries, Jens Peter ^b   Wilmanns, Matthias ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d UNIVERSITY OF WÜRZBURG   (Germany)

^e INSTITUTE OF EPIDEMIOLOGY   (Germany)

Author keywords

Active site substrate adaptability; Amino acid biosynthesis; Enzyme evolution; Mycobacteria; Protein structure symmetry

Indexed keywords

BACTERIAL ENZYME; HISTIDINE; ISOMERASE; ISOMERASE INHIBITOR; PROTEIN PRIA; PROTEIN TRPF; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SYNTHESIS; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ISOMERIZATION; METAMORPHOSIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; ENZYME INHIBITORS; HISTIDINE; ISOMERASES; ISOMERISM; LIGANDS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

ACTINOBACTERIA; CORYNEBACTERINEAE; MYCOBACTERIUM TUBERCULOSIS;

EID: 79952769611     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1015996108     Document Type: Article

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