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. 2006 Apr;72(4):2905–2917. doi: 10.1128/AEM.72.4.2905-2917.2006

TABLE 4.

Substrate ranges of cloned bacterial epoxide hydrolases

Enzyme Activity toward indicated epoxide substrate numbera:
Aromatic substrates
Aliphatic substrates
Cyclic substrates
1 2 4 5 6 7 8 10 11 12 13 14 16 17 19 20 21 22 23 24 25
AraEchAc ++ ++ ++ ++ ++ ++ ++ ++ ++ ++ ++ ++ + +
Bsuehb ++ ++
Bfuehlc ++ ++ ++ ++ ++ ++ ++ ++ ++ ++ ++ ++ +
Corehb ++ ++ ++ ++ ++ + + + ++ + ++ ++ ++ +
Draehb ++ ++ ++ ++ + ++ ++ ++ ++ ++ ++ ++ ++
MtuEphFc
Npueh1b ++ ++ ++ ++ + ++ ++ ++ ++ ++ ++ ++ +
Npueh2c +
Ppuehc
Rpaeh2c ++ ++ ++ ++ ++ ++ ++ ++ ++ + + ++ ++ ++ +
Scoeh6c
Tfuehc
a

All assays were done with the adrenaline test (46), with the exception of that for epoxide 10, for which conversion was monitored spectroscopically. Activities were scored as follows: −, <3 nmol mg−1 min−1; +, >3 nmol mg−1 min−1; and ++, >10 nmol mg−1 min−1. Epoxide structures are shown in Fig. 2.

b

Measurements were performed with purified protein.

c

Measurements were performed with desalted cell extracts.