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Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1

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Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1. / Szolkowy, Claudia; Eltis, Lindsay D.; Bruce, Neil C.; Grogan, Gideon.

In: Chembiochem, Vol. 10, No. 7, 04.05.2009, p. 1208-1217.

Research output: Contribution to journalArticlepeer-review

Harvard

Szolkowy, C, Eltis, LD, Bruce, NC & Grogan, G 2009, 'Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1', Chembiochem, vol. 10, no. 7, pp. 1208-1217. https://doi.org/10.1002/cbic.200900011

APA

Szolkowy, C., Eltis, L. D., Bruce, N. C., & Grogan, G. (2009). Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1. Chembiochem, 10(7), 1208-1217. https://doi.org/10.1002/cbic.200900011

Vancouver

Szolkowy C, Eltis LD, Bruce NC, Grogan G. Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1. Chembiochem. 2009 May 4;10(7):1208-1217. https://doi.org/10.1002/cbic.200900011

Author

Szolkowy, Claudia ; Eltis, Lindsay D. ; Bruce, Neil C. ; Grogan, Gideon. / Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1. In: Chembiochem. 2009 ; Vol. 10, No. 7. pp. 1208-1217.

Bibtex - Download

@article{80c0bfd0d90740cfb7d9f8ea15958633,
title = "Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1",
abstract = "Microbial genome sequences are providing a wealth of information on new enzymes that have considerable potential as biocatalysts. The recently sequenced genome of Rhodococcus jostii RHA1, for example, has revealed an impressive array of catabolic enzymes, including many putative Baeyer-Villiger monooxygenases (BVMOs). We,have cloned 23 target BVMO sequences from the genome of R. jostii RHA1 and heterologously expressed 13 of these as soluble proteins to unearth new substrate specificities and selectivities. Whole-cell biocatalysts expressing the genes were screened against seven different test substrates. Each of these catalysts displayed activity toward at least three ketones. We observed a remarkable diversity of both regio- and enantioselectivity among the BVMOs from R. jostii RHA1 for the transformation of two chiral substrates, with some enzymes displaying high enantioselectivity for the isomers of 2-methylcyclopenta none. With the notable exception of the product of gene ro03437, named MO14, the biocatalysts' sequences correlated well with their respective activities and selectivities. This correlation allowed the identification of sequence motifs specific to subgroups of the BVMOs from R. jostii and other organisms. Overall, the data improve predictive models of BVMO activity from sequence and suggest new avenues to pursue in engineering these enzymes.",
keywords = "Baeyer-Villiger reaction, enzyme catalysis, ketones, oxidoreductases, stereoselectivity, XANTHOBACTER SP ZL5, PHENYLACETONE MONOOXYGENASE, MYCOBACTERIUM-TUBERCULOSIS, BICYCLIC KETONES, BIOCATALYSTS, OXIDATION, EXPRESSION, CLONING, ENANTIOSELECTIVITY, PURIFICATION",
author = "Claudia Szolkowy and Eltis, {Lindsay D.} and Bruce, {Neil C.} and Gideon Grogan",
year = "2009",
month = may,
day = "4",
doi = "10.1002/cbic.200900011",
language = "English",
volume = "10",
pages = "1208--1217",
journal = "Chembiochem",
issn = "1439-4227",
publisher = "Wiley-VCH Verlag",
number = "7",

}

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TY - JOUR

T1 - Insights into Sequence-Activity Relationships amongst Baeyer-Villiger Monooxygenases as Revealed by the Intragenomic Complement of Enzymes from Rhodococcus jostii RHA1

AU - Szolkowy, Claudia

AU - Eltis, Lindsay D.

AU - Bruce, Neil C.

AU - Grogan, Gideon

PY - 2009/5/4

Y1 - 2009/5/4

N2 - Microbial genome sequences are providing a wealth of information on new enzymes that have considerable potential as biocatalysts. The recently sequenced genome of Rhodococcus jostii RHA1, for example, has revealed an impressive array of catabolic enzymes, including many putative Baeyer-Villiger monooxygenases (BVMOs). We,have cloned 23 target BVMO sequences from the genome of R. jostii RHA1 and heterologously expressed 13 of these as soluble proteins to unearth new substrate specificities and selectivities. Whole-cell biocatalysts expressing the genes were screened against seven different test substrates. Each of these catalysts displayed activity toward at least three ketones. We observed a remarkable diversity of both regio- and enantioselectivity among the BVMOs from R. jostii RHA1 for the transformation of two chiral substrates, with some enzymes displaying high enantioselectivity for the isomers of 2-methylcyclopenta none. With the notable exception of the product of gene ro03437, named MO14, the biocatalysts' sequences correlated well with their respective activities and selectivities. This correlation allowed the identification of sequence motifs specific to subgroups of the BVMOs from R. jostii and other organisms. Overall, the data improve predictive models of BVMO activity from sequence and suggest new avenues to pursue in engineering these enzymes.

AB - Microbial genome sequences are providing a wealth of information on new enzymes that have considerable potential as biocatalysts. The recently sequenced genome of Rhodococcus jostii RHA1, for example, has revealed an impressive array of catabolic enzymes, including many putative Baeyer-Villiger monooxygenases (BVMOs). We,have cloned 23 target BVMO sequences from the genome of R. jostii RHA1 and heterologously expressed 13 of these as soluble proteins to unearth new substrate specificities and selectivities. Whole-cell biocatalysts expressing the genes were screened against seven different test substrates. Each of these catalysts displayed activity toward at least three ketones. We observed a remarkable diversity of both regio- and enantioselectivity among the BVMOs from R. jostii RHA1 for the transformation of two chiral substrates, with some enzymes displaying high enantioselectivity for the isomers of 2-methylcyclopenta none. With the notable exception of the product of gene ro03437, named MO14, the biocatalysts' sequences correlated well with their respective activities and selectivities. This correlation allowed the identification of sequence motifs specific to subgroups of the BVMOs from R. jostii and other organisms. Overall, the data improve predictive models of BVMO activity from sequence and suggest new avenues to pursue in engineering these enzymes.

KW - Baeyer-Villiger reaction

KW - enzyme catalysis

KW - ketones

KW - oxidoreductases

KW - stereoselectivity

KW - XANTHOBACTER SP ZL5

KW - PHENYLACETONE MONOOXYGENASE

KW - MYCOBACTERIUM-TUBERCULOSIS

KW - BICYCLIC KETONES

KW - BIOCATALYSTS

KW - OXIDATION

KW - EXPRESSION

KW - CLONING

KW - ENANTIOSELECTIVITY

KW - PURIFICATION

UR - http://www.scopus.com/inward/record.url?scp=67650498684&partnerID=8YFLogxK

U2 - 10.1002/cbic.200900011

DO - 10.1002/cbic.200900011

M3 - Article

VL - 10

SP - 1208

EP - 1217

JO - Chembiochem

JF - Chembiochem

SN - 1439-4227

IS - 7

ER -