PMID:14580236
| Citation |
Dobson, RC, Gerrard, JA and Pearce, FG (2004) Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-aspartate beta-semialdehyde. Biochem. J. 377:757-62 |
|---|---|
| Abstract |
DHDPS (dihydrodipicolinate synthase; EC 4.2.1.52) is the enzyme that catalyses the first unique step of lysine biosynthesis in plants and micro-organisms. As such, it has attracted much attention as a target for herbicide and anti-microbial action. DHDPS has two substrates: pyruvate and ( S )-aspartate beta-semialdehyde [( S )-ASA]. There are various literature reports that suggest that high levels of ( S )-ASA inhibit the enzyme [Karsten (1997) Biochemistry 36, 1730-1739; Stahly (1969) Biochim. Biophys. Acta 191, 439-451], whereas others have not observed this phenomenon. We have resolved this long-running literature debate and shown unequivocally that this difference in reported behaviour can be attributed to differences in the preparation of ( S )-ASA used by each researcher. DHDPS is not inhibited by its substrate; rather, the inhibition is due to an, as yet, unidentified inhibitor in preparations of the substrate generated by ozonolysis. Furthermore, we demonstrate that ( R )-ASA is neither an inhibitor nor a substrate of DHDPS from Escherichia coli. |
| Links |
PubMed PMC1223910 Online version:10.1042/BJ20031389 |
| Keywords |
Aspartic Acid/analogs & derivatives; Aspartic Acid/chemical synthesis; Aspartic Acid/chemistry; Aspartic Acid/metabolism; Dihydrodipicolinate Reductase; Enzyme Inhibitors/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/antagonists & inhibitors; Escherichia coli Proteins/metabolism; Hydro-Lyases/antagonists & inhibitors; Hydro-Lyases/isolation & purification; Hydro-Lyases/metabolism; Oxidoreductases Acting on CH-CH Group Donors/isolation & purification; Stereoisomerism; Substrate Specificity |
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