The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 64, Issue 12, 2008, Pages 1092-1095

  Devenish, Sean R A ^a   Gerrard, Juliet A ^a   Jameson, Geoffrey B ^b   Dobson, Renwick C J ^c,d  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b MASSEY UNIVERSITY   (New Zealand)

^c UNIVERSITY OF MELBOURNE   (Australia)

^d UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

(S) lysine biosynthesis; Dihydrodipicolinate synthase; Substrate specificity

Indexed keywords

DIHYDRODIPICOLINATE SYNTHASE; ESCHERICHIA COLI PROTEIN; HYDROLYASE; OXALOACETIC ACID; PYRUVIC ACID;

ARTICLE; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; KINETICS; METABOLISM; PROTEIN DATABASE; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DATABASES, PROTEIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDRO-LYASES; KINETICS; OXALOACETATE; PYRUVIC ACID; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 57349158095     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309108033654     Document Type: Article

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