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. Author manuscript; available in PMC: 2014 Feb 12.
Published in final edited form as: Biochemistry. 2013 Jan 30;52(6):1101–1112. doi: 10.1021/bi301496p

Table 3.

Kinetic parameters of l-histidinol phosphatases from cog 1387.

Locus tag Organism kcat (s−1) Km (mM) kcat/Km
(M−1s−1)
Metal content per
enzyme monomer
MCCL_0344 Macrococcus caseolyticus JCSC5402 30 ± 2 1.5 ± 0.3 (2.0 ± 0.2) × 104 Mn (0.9); Fe (0.6); Zn (0.3)
BBR47_00270 Brevibacillus brevis NBRC 100599 7.2 ± 0.4 2.6 ± 0.3 (2.8 ± 0.2) × 103 Zn (1.6); Mn (0.3)
BCE_1533 Bacillus cereus ATCC10987 8.1 ± 0.1 1.5 ± 0.1 (5.6 ± 0.2) × 103 Mn (1.4); Zn (0.4)
BcerKBAB4_1335a Bacillus weihenstephanensis KBAB4 1.2 ± 0.1 4.9 ± 0.3 (2.5 ± 0.2) × 102 Zn (1.5); Fe (1.2)
BcerKBAB4_1335 34 ± 2 1.3 ± 0.2 (2.6 ± 0.2) × 104 Mn (1.0); Zn (0.6)
BSU29620a Bacillus subtilis subsp. subtilis str. 168 0.37 ± 0.01 0.10 ± 0.01 (3.7 ± 0.6) × 103 Fe (2.6); Zn (0.4)
BH3206 Bacillus halodurans C-125 28 ± 1 0.64 ± 0.08 (4.4 ± 0.5) × 104 Mn (1.1); Zn (0.3)
GK2799 Geobacillus kaustophilus HTA426 7.6 ± 1.4 8 ± 3 (9.0 ± 1.1) × 102 Mn (1.0); Zn (0.4); Fe (0.3)
SMU_1486c Streptococcus mutans UA159 0.31 ± 0.01 0.58 ± 0.07 (5.3 ± 0.8) × 102 Zn (0.4); Fe (0.3)
a

Enzymes were over-expressed without the addition of 2,2’-bipyridyl in the growth medium.