Skip to main content
. Author manuscript; available in PMC: 2009 Jul 1.
Published in final edited form as: Mol Microbiol. 2008 Jul;69(2):453–465. doi: 10.1111/j.1365-2958.2008.06296.x

Table 3.

Autodephosphorylation rates of Spo0F mutants

Substitution Position(s) Amino Acid At Position
Fold Change From Wildtype
‘14’ ‘59’ ‘89’ kdephos (min-1)a
Wildtype Q K Y 0.0039b ± 0.0011 NA
‘59’ Q E Y 0.24 ± 0.01 +62
Q N Y 0.093b ± 0.005 +24
‘89’ Q K E 0.031 ± 0.001 +7.9
Q K L 0.015 ± 0.002 +3.8
Q K H 0.0051± 0.0001 +1.3
‘59’/‘89’ Q E L 0.42 ± 0.04 +110
Q N E 0.42 ± 0.05 +110
Q N L 0.33 ± 0.02 +85
Q N H 0.17 ± 0.01 +44
‘14’/‘59’/‘89’ S E L 0.49 ± 0.10 +130
F N E 0.29 ± 0.03 +74
H N H 0.13 ± 0.00 +33
a

Mean ± standard deviation. Wildtype Spo0F was measured 4 times and each mutant Spo0F was measured 2-3 times.

b

Rates reported by Zapf et al. (Zapf et al., 1998) were 0.0039 and 0.087 min-1 for wildtype and ‘59’KN substitution, respectively.