The C-terminal domain of Escherichia coli dihydrodipicolinate synthase (DHDPS) is essential for maintenance of quaternary structure and efficient catalysis.
作者： Belinda B.B. Guo , Sean R.A. Devenish , Renwick C.J. Dobson , Andrew C. Muscroft-Taylor , Juliet A. Gerrard
DOI: 10.1016/J.BBRC.2009.01.169
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摘要: Abstract Dihydrodipicolinate synthase (DHDPS) catalyses the first committed step in biosynthesis of (S)-lysine, an essential constituent bacterial cell walls. Escherichia coli DHDPS is homotetrameric, and each monomer contains N-terminal (β/α)8-barrel, responsible for catalysis regulation, three C-terminal α-helices, function which unknown. This study investigated domain E. by characterising a truncated (DHDPS-H225∗). DHDPS-H225∗ was unable to complement (S)-lysine auxotroph, showed significantly reduced solubility, stability, maximum catalytic activity (kcat = 1.20 ± 0.01 s−1), only 1.6% wild type (DHDPS-WT). The affinity substrates feedback inhibitor, remained comparable DHDPS-WT. These changes were accompanied disruption quaternary structure, has previously been shown be efficient this enzyme.
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