1yxd

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Template:STRUCTURE 1yxd

Contents 1 Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A 2 Function 3 About this Structure 4 See Also 5 Reference

Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A

Template:ABSTRACT PUBMED 16041077

Function

[DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).^{[1] [2]}

About this Structure

1yxd is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

• Dihydrodipicolinate Synthase

Reference

• Dobson RC, Griffin MD, Jameson GB, Gerrard JA. The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1116-24. Epub 2005, Jul 20. PMID:16041077 doi:10.1107/S0907444905016318

1. ↑ Devenish SR, Blunt JW, Gerrard JA. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J Med Chem. 2010 Jun 24;53(12):4808-12. doi: 10.1021/jm100349s. PMID:20503968 doi:10.1021/jm100349s
2. ↑ Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry. 1997 Jan 7;36(1):24-33. PMID:8993314 doi:10.1021/bi962272d