Extended Data Table 1 Comparison of kinetic properties and metal loading of purified guanidinase enzymes from N. inopinata and Synechocystis

From: Growth of complete ammonia oxidizers on guanidine

  1. The Synechocystis enzyme was either overexpressed in Synechocystis15,17,18 or in E. coli18. In the latter heterologous expression experiment, Ni-loading chaperons of Synechocystis were co-overexpressed. For the N. inopinata guanidinase, three different nickel concentrations (indicated after the source species name) were used during expression. For the 20 µM nickel expression batch, nickel was present during all purification steps in the same concentration, and only removed for the ICP-MS analysis of metal loading. This was not possible for the 1 mM Ni2+ treatment as it resulted in protein denaturation during purification.
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