Specificity versus catalytic potency: The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis

Biochimie

Volumn 91, Issue 8, 2009, Pages 1036-1044

  Dobson, Renwick C J ^a,b   Perugini, Matthew A ^a   Jameson, Geoffrey B ^c   Gerrard, Juliet A ^d  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c MASSEY UNIVERSITY   (New Zealand)

^d UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

(S) Lysine biosynthesis; Catalysis; Dihydrodipicolinate synthase; Protein dynamics; Site directed mutagenesis

Indexed keywords

2 OXOGLUTARIC ACID; DIHYDRODIPICOLINATE SYNTHASE; ESCHERICHIA COLI PROTEIN; PYRUVIC ACID DERIVATIVE; SERINE; THREONINE; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PREDICTION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDRO-LYASES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THREONINE;

ESCHERICHIA COLI;

EID: 67649444194     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.05.013     Document Type: Article

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