The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site- directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity

Biochemistry

Volumn 36, Issue 21, 1997, Pages 6502-6510

  Sundararaju, Bakthavatsalam ^a   Antson, Alfred A ^b   Phillips, Robert S ^a   Demidkina, Tatyana V ^c   Barbolina, Maria V ^c   Gollnick, Paul ^d   Dodson, G Guy ^b   Wilson, Keith S ^b  

^a UNIVERSITY OF GEORGIA   (United States)

^b UNIVERSITY OF YORK   (United Kingdom)

^c ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^d UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROPIONIC ACID DERIVATIVE; TYROSINE PHENOL LYASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL TISSUE; ARTICLE; CITROBACTER FREUNDII; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; RABBIT; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

ARGININE; CATALYSIS; CITROBACTER FREUNDII; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ISOLEUCINE; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PHENYLPROPIONATES; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPTOPHAN; TYROSINE; TYROSINE PHENOL-LYASE; VALINE;

EID: 0030982177     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962917+     Document Type: Article

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