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. Author manuscript; available in PMC: 2010 Sep 23.
Published in final edited form as: J Am Chem Soc. 2009 Sep 23;131(37):13523–13530. doi: 10.1021/ja9054417

Figure 4.

Figure 4

MS analysis of coupled glutamic acid transfer assays. A: Incubation of KtzN with holo A*PCP3, KtzO (red trace) or KtzP (green trace) and their co-substrates yielded the transfer of glutamic acid and subsequent hydroxylation by KtzO and KtzP. No transfer of glutamic acid by KtzN was observed with a hydroxylase was not added (blue trace). B: Role of A*: The KtzN coupled assay was carried out as in A, but the single PCP was used instead of A*PCP of the third module of KtzH. In all cases, only holo-PCP was detected after the coupled assays, indicating that one hydroxylase and the A* domain is needed to allow KtzN-mediated transfer of glutamic acid on the PCP domain.