Tryptophanase from Proteus vulgaris: The conformational rearrangement in the active site, induced by the mutation of Tyrosine 72 to Phenylalanine, and its mechanistic consequences

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 4, 2006, Pages 750-757

  Kulikova, Vitalia V ^a   Zakomirdina, Ludmila N ^a   Dementieva, Irene S ^b   Phillips, Robert S ^c   Gollnick, Paul D ^d   Demidkina, Tatyana V ^a   Faleev, Nicolai G ^e  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^b UNIVERSITY OF CHICAGO   (United States)

^c UNIVERSITY OF GEORGIA   (United States)

^d UNIVERSITY AT BUFFALO   (United States)

^e A N NESMEYANOV INSTITUTE OF ORGANOELEMENT COMPOUNDS   (Russian Federation)

Author keywords

Proteus vulgaris; Pyridoxal 5 phosphate; Site directed mutagenesis; Tryptophan indole lyase

Indexed keywords

1 (3,4 DIMETHOXYPHENYL) 3 (3 ETHYLVALERYL) 4 HYDROXY 6,7,8 TRIMETHOXY 2 NAPHTHOIC ACID METHYL ESTER; AMINO ACID; CARBON; CYSTEINE; FUNCTIONAL GROUP; PHENYLALANINE; SERINE; TRYPTOPHAN; TRYPTOPHANASE; TYROSINE;

ARTICLE; ATOM; CATALYSIS; CATALYST; CONFORMATION; COVALENT BOND; ENZYME ACTIVITY; LIVER CONGESTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEUS VULGARIS; REACTION ANALYSIS; STRUCTURE ANALYSIS; SUBSTITUTION REACTION; WILD TYPE;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PROTEIN CONFORMATION; PROTEUS VULGARIS; TRYPTOPHANASE; TYROSINE;

PROTEUS VULGARIS;

EID: 33646076726     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.12.003     Document Type: Article

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