Construction of a tailor-made L (2S,3S)-butanediol dehydrogenase by exchanging domains between native structural analogs.

Abstract:

:The development of a stable L-BDH chimera was attempted by exchanging whole domains between two native structural analogs, L-BDH and meso-BDH, because the S-configuration specificity of L-BDH is valuable from the standpoint of its application but its activity is unstable, whereas meso-BDH is stable. The domain chimeras obtained indicated that the leaf-like structures constituting three domains were likely to be mainly associated with chiral recognition, and the fourth domain, the basic domain, is likely to be mainly associated with enzyme stability. A combination of the leaf domains of L-BDH and the basic domain of meso-BDH attained a sufficient level of practical use as an artificial L-BDH chimera, because the resulting enzyme had both stability and S-configuration specificity. However, the levels of stability and specificity were slightly lower than those of the respective enzymes from which they were derived.

journal_name

Protein Pept Lett

authors

Shimegi T,Takusagawa Y,Ohtsuki T,Noda S,Kurisu G,Kusunoki M,Ui S

doi

10.2174/092986611795713970

subject

Has Abstract

pub_date

2011-08-01 00:00:00

pages

825-30

issue

8

eissn

0929-8665

issn

1875-5305

pii

BSP/ PPL/ E pub/0310

journal_volume

18

pub_type

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