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3pb2

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Template:STRUCTURE 3pb2

Contents

Characterisation of the first monomeric dihydrodipicolinate synthase variant reveals evolutionary insights

Template:ABSTRACT PUBMED 21803176

Function

[DAPA_THEMA] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (Probable).[1]

About this Structure

3pb2 is a 6 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

See Also

Reference

  • Pearce FG, Dobson RC, Jameson GB, Perugini MA, Gerrard JA. Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization. Biochim Biophys Acta. 2011 Jul 22. PMID:21803176 doi:10.1016/j.bbapap.2011.07.016
  1. ↑ Pearce FG, Perugini MA, McKerchar HJ, Gerrard JA. Dihydrodipicolinate synthase from Thermotoga maritima. Biochem J. 2006 Dec 1;400(2):359-66. PMID:16872276 doi:10.1042/BJ20060771

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