ATPase rates of p97-ND1L bearing point mutations at the active site and their functional defects deduced from NMR analysis. All presented mutants form hexamers. Only N348Q fully abolishes ATP hydrolysis, and only mutations of F360 have a stimulatory effect on phosphate release. Asterisks designate ATPase inactive mutants. 'Coupled NTD position' indicates whether the mutant exhibits the same change in NTD position upon nucleotide binding as wild-type (WT) p97. 'ADP·Pi state' indicates that this state is observed during ATP turnover. Data are presented as mean values. Error bars represent s.d. for n = 4 biologically independent replicates. ATPase rates were determined in n = 2–4 replicates, as indicated by the corresponding data points. The ATPase rate of K251A at 50 °C could not be determined due to the low thermal stability.
