Abstract:
:trans-3-Chloroacrylic acid dehalogenase (CaaD) catalyzes the hydrolytic dehalogenation of trans-3-haloacrylates to yield malonate semialdehyde by a mechanism utilizing βPro-1, αArg-8, αArg-11, and αGlu-52. These residues are implicated in a promiscuous hydratase activity where 2-oxo-3-pentynoate is processed to acetopyruvate. The roles of three nearby residues (βAsn-39, αPhe-39, and αPhe-50) are unexplored. Mutants were constructed at these positions (βN39A, αF39A, αF39T, αF50A and αF50Y) and kinetic parameters determined along with those of the αR8K and αR11K mutants. Analysis indicates that αArg-8, αArg-11, and βAsn-39 are critical for dehalogenase activity whereas αArg-11 and αPhe-50 are critical for hydratase activity. Docking studies suggest structural bases for these observations.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Poelarends GJ,Serrano H,Huddleston JP,Johnson WH Jr,Whitman CPdoi
10.1016/j.febslet.2013.07.006subject
Has Abstractpub_date
2013-09-02 00:00:00pages
2842-50issue
17eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00519-Xjournal_volume
587pub_type
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