Abstract
A C–C hydrolase gene (bphD LA-4 ) from strain Dyella ginsengisoli LA-4 was cloned and expressed in Escherichia coli BL21 (DE3). BphDLA-4 together with another hydrolase MfphALA-4, which derived from the same strain, possessed esterase activities. p-Nitrophenyl butyrate was the best substrate for both enzymes. BphDLA-4 had high catalytic efficiency to p-nitrophenyl benzoate, whereas MfphALA-4 had no activity. Homology modeling and docking studies demonstrated that the proper hydrogen bond interaction was important for the reactivity of specific substrate.
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References
Bornscheuer UT, Kazlauskas R (2004) Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways. Angew Chem Int Ed Engl 43:6032–6040
Horsman GP, Ke J, Dai S, Seah SY, Bolin JT, Eltis LD (2006) Kinetic and structural insight into the mechanism of BphD, a C–C bond hydrolase from the biphenyl degradation pathway. Biochemistry 45:11071–11186
Hult K, Berglund P (2007) Enzyme promiscuity: mechanism and applications. Trends Biotechnol 25:231–238
Jochens H, Hesseler M, Stiba K, Padhi SK, Kazlauskas RJ, Bornscheuer UT (2011) Protein engineering of α/β-hydrolase fold enzymes. Chembiochem 12:1508–1517
Khersonsky O, Tawfik DS (2010) Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu Rev Biochem 79:471–505
Kourist R, Bartsch S, Fransson L, Hult K, Bornscheuer UT (2008) Understanding promiscuous amidase activity of an esterase from Bacillus subtilis. Chembiochem 9:87–89
Leitgeb S, Nidetzky B (2010) Enzyme catalytic promiscuity: the nonheme Fe2+ center of beta-diketone-cleaving dioxygenase Dke1 promotes hydrolysis of activated esters. Chembiochem 11:502–505
Li JJ, Bugg TD (2007) Investigation of a general base mechanism for ester hydrolysis in C–C hydrolase enzymes of the alpha/beta-hydrolase superfamily: a novel mechanism for the serine catalytic triad. Org Biomol Chem 5:507–513
Li C, Hassler M, Bugg TD (2008) Catalytic promiscuity in the alpha/beta-hydrolase superfamily: hydroxamic acid formation, C–C bond formation, ester and thioester hydrolysis in the C–C hydrolase family. Chembiochem 9:71–76
Li A, Qu YY, Zhou JT, Ma F, Zhou H, Shi SN (2010) Characterization of a novel meta-fission product hydrolase from Dyella ginsengisoli LA-4. Proc Biochem 45:94–100
Seah SY, Terracina G, Bolin JT, Riebel P, Snieckus V, Eltis LD (1998) Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls. J Biol Chem 273:22943–22949
Speare DM, Fleming SM, Beckett MN, Li JJ, Bugg TD (2004) Synthetic 6-aryl-2-hydroxy-6–ketohexa -2,4-dienoic acid substrates for C–C hydrolase BphD: investigation of a general base catalytic mechanism. Org Biomol Chem 2:2942–2950
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The authors would like to thank the National Natural Science Foundation of China (Nos. 21176040 and 51078054) for their financial supports.
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Zhou, H., Qu, Y., Kong, C. et al. Promiscuous esterase activities of the C–C hydrolases from Dyella ginsengisoli . Biotechnol Lett 34, 1107–1113 (2012). https://doi.org/10.1007/s10529-012-0880-0
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DOI: https://doi.org/10.1007/s10529-012-0880-0