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. Author manuscript; available in PMC: 2013 May 8.
Published in final edited form as: Biochemistry. 2012 Apr 24;51(18):3933–3940. doi: 10.1021/bi201881p

Table 2.

Comparison of rates of 4NPA hydrolysis by artificial esterases.

name reference molecule type kcat (s−1) KM (mM) k2 (M−1s−1)
Zinc esterases (4NPA)
MID1-zinc (22) helix-turn-helix dimer 0.30 0.42 630
Macrocyclic amine Zn(II) complexes (33, 49, 50) small molecule -- -- < 1
[Hg(II)]s[Zn(II)(H2O/OH)]N(TRIL9CL23H)3n+ (20) trimeric peptide 0.04 1.7 23
Carbonic anhydrase II (51) natural protein,
unnatural substrate
53 21 2,550
Metal-free esterases (4NPA)
−OH (32) hydroxide ion -- -- 9.5
KO-42 (26) helix-turn-helix dimer -- -- 0.29
JNIIRO (38) peptide -- -- 0.06
S-824 (25) unselected catalytic
antibody
0.0054 3 2
ECH13 a protein monomer 0.018 0.057 320
43C9 (28) selected catalytic
antibody
25 0.05 470,000
PDZ2 (30) thioredoxin redesign 0.0005 0.17 3
a

Richter, Baker, personal communication