Dihydrodipicolinate synthase (DHDPS) from Escherichia coli displays partial mixed inhibition with respect to its first substrate, pyruvate

Biochimie

Volumn 86, Issue 4-5, 2004, Pages 311-315

  Dobson, Renwick C J ^a,b   Griffin, Michael D W ^a,b   Roberts, Sarah J ^b   Gerrard, Juliet A ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b THE NEW ZEALAND INSTITUTE FOR PLANT AND FOOD RESEARCH LIMITED   (New Zealand)

Author keywords

(S) lysine biosynthesis; (S) lysine inhibition; DAP; DHDPR; DHDPS; dihydrodipicolinate reductase; Dihydrodipicolinate synthase; dihydrodipicolinate synthase; HEPES; meso diaminopimelic acid; Partial mixed inhibition; Proton relay

Indexed keywords

ASPARTATE BETA SEMIALDEHYDE; ASPARTIC ACID DERIVATIVE; DIAMINOPIMELIC ACID; DIHYDROPICOLINATE SYNTHASE; LYSINE; PICOLINIC ACID DERIVATIVE; PROTON; PYRUVIC ACID; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; BIOSYNTHESIS; CHEMICAL REACTION; CRYSTALLOGRAPHY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME SUBSTRATE; ESCHERICHIA COLI; MICROORGANISM; PLANT; POLYMERIZATION;

ESCHERICHIA COLI; HYDRO-LYASES; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; PYRUVIC ACID; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 2942685393     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.03.008     Document Type: Article

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