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. 1999 Dec;181(23):7314–7322. doi: 10.1128/jb.181.23.7314-7322.1999

TABLE 3.

Rates of amino acid catabolism determined for H. pylori cells of WT and rocF mutant strains (n = 4)a

Strain Mean rate of enzyme activity (nmol/min/mg of protein) ± SD
Arginase Asparaginase Aspartase Glutaminase Serine dehydratase
26695 33 ± 4 19 ± 3 8 ± 2 66 ± 6 42 ± 7
26695 rocF::aphA3  UDb 19 ± 3 8 ± 2 62 ± 8 19 ± 3c
N6 51 ± 5 35 ± 6 11 ± 3 91 ± 10 37 ± 8
N6 rocF::aphA3 UD 20 ± 4 12 ± 3 80 ± 11 14 ± 3c
N6 236-2 UD 25 ± 4 11 ± 2 85 ± 10 25 ± 5d
SS1 54 ± 5 32 ± 3 17 ± 3 81 ± 8 50 ± 7
SS1 rocF::aphA3 UD 28 ± 5 11 ± 3 75 ± 8 17 ± 3e
SS1 236-2 UD 24 ± 3 15 ± 2 75 ± 6 32 ± 6e
a

Bacteria were suspended in a phosphate (20 mM; pH 7)–NaCl (115 mM)–KCl (15 mM) buffer plus one of the following amino acids: l-arginine (100 mM), l-asparagine (80 mM), l-aspartate (80 mM), l-glutamine (80 mM), or l-serine (80 mM) and were measured for enzyme activity by NMR (see Materials and Methods). 

b

UD, undetectable. P < 0.0001 compared with its isogenic WT strain. 

c

P < 0.005 compared with its isogenic WT strain. 

d

P < 0.05 compared with its isogenic WT strain. 

e

P < 0.01 compared with its isogenic WT strain.