Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C-H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 7, 2006, Pages 1268-1276

  Demidkina, T V ^a   Faleev, N G ^b   Papisova, A I ^a   Bazhulina, N P ^a   Kulikova, V V ^a   Gollnick, P D ^c   Phillips, R S ^d  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

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

^c UNIVERSITY AT BUFFALO   (United States)

^d UNIVERSITY OF GEORGIA   (United States)

Author keywords

Asp214; Citrobacter freundii tyrosine phenol lyase; Ionic form of the internal aldimine; Mutant enzymes; Rate limiting stage; Steady state kinetic

Indexed keywords

AMINO ACID; ASPARTIC ACID; BACTERIAL ENZYME; DEUTERIUM; IMINE; PHENYLALANINE; PROTON; QUINONE DERIVATIVE; TYROSINE PHENOL LYASE;

ACIDITY; ARTICLE; CATALYSIS; CHEMICAL REACTION; CITROBACTER FREUNDII; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON TRANSPORT; X RAY ANALYSIS;

ALANINE; APOENZYMES; ASPARAGINE; ASPARTIC ACID; BINDING SITES; CATALYSIS; CIRCULAR DICHROISM; CITROBACTER FREUNDII; COENZYMES; DEUTERIUM OXIDE; HOMOSERINE; KINETICS; MOLECULAR STRUCTURE; MUTATION; PHENYLALANINE; RECOMBINANT FUSION PROTEINS; SPECTROPHOTOMETRY; TYROSINE; TYROSINE PHENOL-LYASE;

CITROBACTER FREUNDII;

EID: 33746093225     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.05.001     Document Type: Article

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