Article
Probing intra- versus interchain kinetic preferences of L-Thr acylation on dimeric VibF with mass spectrometry.
Biophysical journal - 1 Oct 2006
Hicks Leslie M, Balibar Carl J, Walsh Christopher T, Kelleher Neil L, Hillson Nathan J
Abstract excerpt
We present a method to probe intra- and interchain activities within dimeric nonribosomal peptide synthetases. Utilizing domain inactivation and analytical mass mutants in conjunction with rapid-quench, mass spectrometry, and a probabilistic kinetic model, we have elucidated the pre-steady-state intra- and interchain rates and the corresponding flux of the acylation of L-Thr onto VibF. Although the intra rate is...
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