Evolution of enzymatic activities in the enolase superfamily: Partitioning of reactive intermediates by (D)-glucarate dehydratase from Pseudomonas putida

Biochemistry

Volumn 37, Issue 41, 1998, Pages 14350-14357

  Palmer, David R J ^a   Hubbard, Brian K ^a   Gerlt, John A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENOLASE; HYDROLYASE; SACCHARIC ACID;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CRYSTAL STRUCTURE; DEHYDRATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; EUBACTERIUM; EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE; PSEUDOMONAS PUTIDA;

CARBON ISOTOPES; CATALYSIS; DEUTERIUM; ENERGY TRANSFER; ENZYME ACTIVATION; EVOLUTION, MOLECULAR; HYDRO-LYASES; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOPYRUVATE HYDRATASE; PROTONS; PSEUDOMONAS PUTIDA; SOLVENTS; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0032514772     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981122v     Document Type: Article

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