Two classes of bacterial IMPDHs according to their quaternary structures and catalytic properties

PLoS ONE

Volumn 10, Issue 2, 2015, Pages

  Alexandre, Thomas ^a,b,c   Rayna, Bertrand ^a,b   Munier Lehmann, Hélène ^a,b  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

^c UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; BACTERIAL ENZYME; INOSINATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; TETRAMER; BACTERIAL PROTEIN;

ARTICLE; BIOCHEMISTRY; CATALYSIS; CLASSIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; MICHAELIS MENTEN KINETICS; NONHUMAN; PHYSICAL CHEMISTRY; PROTEIN QUATERNARY STRUCTURE; BACTERIUM; BINDING SITE; CHEMICAL STRUCTURE; METABOLISM; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS);

BACTERIA; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; IMP DEHYDROGENASE; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY;

EID: 84923833955     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0116578     Document Type: Article

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