Abstract:
:Carboxylesterase (EII') from Arthrobacter sp. KI72 has 88% homology to 6-aminohexanoate-dimer hydrolase (EII) and possesses ca. 0.5% of the level of 6-aminohexanoate-linear dimer (Ald)-hydrolytic activity of EII. To study relationship between Ald-hydrolytic and esterolytic activities, random mutations were introduced into the gene for Hyb-24 (an EII/EII' hybrid with the majority of the sequence deriving for EII' and possessing an EII'-like level of Ald-hydrolytic activity). Either a G181D or a D370Y substitution in Hyb-24 increased the Ald-hydrolytic activity ca. 10-fold, and a G181D/D370Y double substitution increased activity ca. 100-fold. On the basis of kinetic studies and the three-dimensional structure of the enzyme, we suggest that binding of Ald is improved by these mutations. D370Y increased esterolytic activity for glycerylbutyrate ca. 30-50-fold, whereas G181D decreased the activity to 30% of the parental enzyme.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ohki T,Wakitani Y,Takeo M,Yasuhira K,Shibata N,Higuchi Y,Negoro Sdoi
10.1016/j.febslet.2006.08.031subject
Has Abstractpub_date
2006-09-18 00:00:00pages
5054-8issue
21eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01003-9journal_volume
580pub_type
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