Mutational analysis of 6-aminohexanoate-dimer hydrolase: relationship between nylon oligomer hydrolytic and esterolytic activities.

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 Lett

journal_title

FEBS letters

authors

Ohki T,Wakitani Y,Takeo M,Yasuhira K,Shibata N,Higuchi Y,Negoro S

doi

10.1016/j.febslet.2006.08.031

subject

Has Abstract

pub_date

2006-09-18 00:00:00

pages

5054-8

issue

21

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01003-9

journal_volume

580

pub_type

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