In:
Applied and Environmental Microbiology, American Society for Microbiology, Vol. 75, No. 17 ( 2009-09), p. 5496-5500
Kurzfassung:
A novel esterase gene, pytH , encoding a pyrethroid-hydrolyzing carboxylesterase was cloned from Sphingobium sp. strain JZ-1. The gene contained an open reading frame of 840 bp. Sequence identity searches revealed that the deduced enzyme shared the highest similarity with many α/β-hydrolase fold proteins (20 to 24% identities). PytH was expressed in Escherichia coli BL21 and purified using Ni-nitrilotriacetic acid affinity chromatography. It was a monomeric structure with a molecular mass of approximately 31 kDa and a pI of 4.85. PytH was able to transform p -nitrophenyl esters of short-chain fatty acids and a wide range of pyrethroid pesticides, and isomer selectivity was not observed. No cofactors were required for enzyme activity.
Materialart:
Online-Ressource
ISSN:
0099-2240
,
1098-5336
DOI:
10.1128/AEM.01298-09
Sprache:
Englisch
Verlag:
American Society for Microbiology
Publikationsdatum:
2009
ZDB Id:
223011-2
ZDB Id:
1478346-0
SSG:
12
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