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. 2003 Jan;185(2):688–692. doi: 10.1128/JB.185.2.688-692.2003

TABLE 1.

Characterization of amino acid substitutions at position L111

Substitutiona Sp act (nmol of product formed/min/mg of protein)b
Urease Histidase GDH
No NAC 17 45 875
Wild type 857 326 28
L111P 597 209 335
L111K 1,080 239 431
L111R 959 219 330
L111Q 1,326 265 365
L111T 1,052 211 253
L111D 748 233 282
L111E 810 253 262
L111N 825 233 215
L111G 778 237 170
L111S 745 233 163
L111A 806 222 73
L111H 756 250 90
L111C 708 305 31
L111I 735 409 28
L111M 762 294 31
L111V 722 302 31
L111F 856 343 18
L111W 563 268 37
L111Y 17 60 695
a

All mutants were carried as cloned fragments in pCB1041. No NAC, pCB1041; Wild type, pCB1051. The background strain was KC4598 (hutC515 nac-204::λplac Mu53 srl-7012::Tn5-131).

b

Cells were grown in W4 minimal salts (18) supplemented with glucose (0.4%), ammonium sulfate (0.2%), glutamine (0.2%), 2 μM nickel sulfate, and 100 μg of ampicillin per ml. Assay values are reported as specific activities and are the mean of at least three independent experiments in which the standard error was <15% of the mean.