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Volumn 51, Issue 29, 2012, Pages 5831-5840

The catalytic serine of meta-cleavage product hydrolases is activated differently for C-O bond cleavage than for C-C bond cleavage

Author keywords

[No Author keywords available]

Indexed keywords

BENZOIC ACID; C-C BOND FISSION; C-C BONDS; C-O BOND CLEAVAGE; DEACYLATION; DIFFERENT MECHANISMS; ESTER HYDROLYSIS; KINETIC ANALYSIS; META-CLEAVAGE; METHANOL CONCENTRATION; METHANOLYSIS; METHYL BENZOATE; N-PROPANOL; NUCLEOPHILIC CATALYSIS; NUCLEOPHILIC MECHANISMS; ORDERS OF MAGNITUDE; PHYSIOLOGICAL SUBSTRATE; PRIMARY ALCOHOLS; PRODUCT ANALYSIS; RATE LIMITING; STEADY-STATE HYDROLYSIS;

EID: 84864268097     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300663r     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0034717267 scopus 로고    scopus 로고
    • Identification of a serine hydrolase as a key determinant in the microbial degradation of polychlorinated biphenyls
    • DOI 10.1074/jbc.275.21.15701
    • Seah, S. Y., Labbe, G., Nerdinger, S., Johnson, M. R., Snieckus, V., and Eltis, L. D. (2000) Identification of a serine hydrolase as a key determinant in the microbial degradation of polychlorinated biphenyls J. Biol. Chem. 275, 15701-15708 (Pubitemid 30366867)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15701-15708
    • Seah, S.Y.K.1    Labbe, G.2    Nerdinger, S.3    Johnson, M.R.4    Snieckus, V.5    Eltis, L.D.6
  • 3
    • 84858244926 scopus 로고    scopus 로고
    • Identification of an Acyl-Enzyme Intermediate in a meta -Cleavage Product Hydrolase Reveals the Versatility of the Catalytic Triad
    • Ruzzini, A. C., Ghosh, S., Horsman, G. P., Foster, L. J., Bolin, J. T., and Eltis, L. D. (2012) Identification of an Acyl-Enzyme Intermediate in a meta -Cleavage Product Hydrolase Reveals the Versatility of the Catalytic Triad J. Am. Chem. Soc. 134, 4615-4624
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 4615-4624
    • Ruzzini, A.C.1    Ghosh, S.2    Horsman, G.P.3    Foster, L.J.4    Bolin, J.T.5    Eltis, L.D.6
  • 5
    • 0032784276 scopus 로고    scopus 로고
    • α/β-Hydrolase fold enzymes: The family keeps growing
    • Nardini, M. and Dijkstra, B. W. (1999) α/β-Hydrolase fold enzymes: The family keeps growing Curr. Opin. Struct. Biol. 9, 732-737
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 6
    • 79952720628 scopus 로고    scopus 로고
    • Different active-site loop orientation in serine hydrolases versus acyltransferases
    • Jiang, Y., Morley, K. L., Schrag, J. D., and Kazlauskas, R. J. (2011) Different active-site loop orientation in serine hydrolases versus acyltransferases ChemBioChem 12, 768-776
    • (2011) ChemBioChem , vol.12 , pp. 768-776
    • Jiang, Y.1    Morley, K.L.2    Schrag, J.D.3    Kazlauskas, R.J.4
  • 7
    • 0034285515 scopus 로고    scopus 로고
    • α/β-Hydrolase fold enzymes: Structures, functions and mechanisms
    • Holmquist, M. (2000) α/β-Hydrolase fold enzymes: Structures, functions and mechanisms Curr. Protein Pept. Sci. 1, 209-235
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 209-235
    • Holmquist, M.1
  • 8
    • 2442485744 scopus 로고    scopus 로고
    • 236
    • DOI 10.1074/jbc.M401575200
    • Gruber, K., Gartler, G., Krammer, B., Schwab, H., and Kratky, C. (2004) Reaction mechanism of hydroxynitrile lyases of the α/β-hydrolase superfamily: The three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of Lys236 J. Biol. Chem. 279, 20501-20510 (Pubitemid 38623497)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20501-20510
    • Gruber, K.1    Gartler, G.2    Krammer, B.3    Schwab, H.4    Kratky, C.5
  • 9
    • 8544222809 scopus 로고    scopus 로고
    • Dioxygenases without requirement for cofactors and their chemical model reaction: Compulsory order ternary complex mechanism of 1H-3-hydroxy-4- oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion
    • DOI 10.1021/bi048735u
    • Frerichs-Deeken, U., Ranguelova, K., Kappl, R., Huttermann, J., and Fetzner, S. (2004) Dioxygenases without requirement for cofactors and their chemical model reaction: Compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion Biochemistry 43, 14485-14499 (Pubitemid 39491983)
    • (2004) Biochemistry , vol.43 , Issue.45 , pp. 14485-14499
    • Frerichs-Deeken, U.1    Ranguelova, K.2    Kappl, R.3    Huttermann, J.4    Fetzner, S.5
  • 10
    • 33748666189 scopus 로고    scopus 로고
    • Structural characterization of enterobactin hydrolase IroE
    • DOI 10.1021/bi060950i
    • Larsen, N. A., Lin, H., Wei, R., Fischbach, M. A., and Walsh, C. T. (2006) Structural characterization of enterobactin hydrolase IroE Biochemistry 45, 10184-10190 (Pubitemid 44384793)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10184-10190
    • Larsen, N.A.1    Lin, H.2    Wei, R.3    Fischbach, M.A.4    Walsh, C.T.5
  • 11
    • 0034673180 scopus 로고    scopus 로고
    • Catalytic mechanism of a C-C hydrolase enzyme: Evidence for a gem-diol intermediate, not an acyl enzyme
    • DOI 10.1021/bi9923095
    • Fleming, S. M., Robertson, T. A., Langley, G. J., and Bugg, T. D. (2000) Catalytic mechanism of a C-C hydrolase enzyme: Evidence for a gem-diol intermediate, not an acyl enzyme Biochemistry 39, 1522-1531 (Pubitemid 30090722)
    • (2000) Biochemistry , vol.39 , Issue.6 , pp. 1522-1531
    • Fleming, S.M.1    Robertson, T.A.2    Langley, G.J.3    Bugg, T.D.H.4
  • 13
    • 33748762789 scopus 로고    scopus 로고
    • Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway
    • DOI 10.1021/bi0611098
    • Horsman, G. P., Ke, J., Dai, S., Seah, S. Y., Bolin, J. T., and Eltis, L. D. (2006) Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway Biochemistry 45, 11071-11086 (Pubitemid 44413654)
    • (2006) Biochemistry , vol.45 , Issue.37 , pp. 11071-11086
    • Horsman, G.P.1    Ke, J.2    Dai, S.3    Seah, S.Y.K.4    Bolin, J.T.5    Eltis, L.D.6
  • 14
    • 33750066944 scopus 로고    scopus 로고
    • Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD
    • DOI 10.1021/bi061253t
    • Li, C., Li, J. J., Montgomery, M. G., Wood, S. P., and Bugg, T. D. (2006) Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD Biochemistry 45, 12470-12479 (Pubitemid 44583689)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12470-12479
    • Li, C.1    Li, J.-J.2    Montgomery, M.G.3    Wood, S.P.4    Bugg, T.D.H.5
  • 15
    • 0030776495 scopus 로고    scopus 로고
    • Purification, characterization, and stereochemical analysis of a c-c hydrolase: 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase
    • DOI 10.1021/bi971115r
    • Lam, W. W. and Bugg, T. D. (1997) Purification, characterization, and stereochemical analysis of a C-C hydrolase: 2-Hydroxy-6-keto-nona-2,4-diene-1,9- dioic acid 5,6-hydrolase Biochemistry 36, 12242-12251 (Pubitemid 27440962)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12242-12251
    • Lam, W.W.Y.1    Bugg, T.D.H.2
  • 16
    • 0030870888 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of 2-hydroxy-6-keto-nona-2,4-diene- 1,9-dioic acid 5,6-hydrolase: Kinetic evidence for enol/keto tautomerization
    • DOI 10.1021/bi971116j
    • Henderson, I. M. and Bugg, T. D. (1997) Pre-steady-state kinetic analysis of 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase: Kinetic evidence for enol/keto tautomerization Biochemistry 36, 12252-12258 (Pubitemid 27440963)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12252-12258
    • Henderson, I.M.J.1    Bugg, T.D.H.2
  • 17
    • 34547094599 scopus 로고    scopus 로고
    • The tautomeric half-reaction of BphD, a C-C bond hydrolase: Kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triad
    • DOI 10.1074/jbc.M702237200
    • Horsman, G. P., Bhowmik, S., Seah, S. Y., Kumar, P., Bolin, J. T., and Eltis, L. D. (2007) The tautomeric half-reaction of BphD, a C-C bond hydrolase. Kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triad J. Biol. Chem. 282, 19894-19904 (Pubitemid 47100080)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 19894-19904
    • Horsman, G.P.1    Bhowmik, S.2    Seah, S.Y.K.3    Kumar, P.4    Bolin, J.T.5    Eltis, L.D.6
  • 18
    • 12344275671 scopus 로고    scopus 로고
    • Catalytic mechanism of C-C hydrolase MhpC from Escherichia coli: Kinetic analysis of His263 and Ser110 site-directed mutants
    • DOI 10.1016/j.jmb.2004.11.032, PII S0022283604014809
    • Li, C., Montgomery, M. G., Mohammed, F., Li, J. J., Wood, S. P., and Bugg, T. D. (2005) Catalytic mechanism of C-C hydrolase MhpC from Escherichia coli: Kinetic analysis of His263 and Ser110 site-directed mutants J. Mol. Biol. 346, 241-251 (Pubitemid 40128318)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.1 , pp. 241-251
    • Li, C.1    Montgomery, M.G.2    Mohammed, F.3    Li, J.-J.4    Wood, S.P.5    Bugg, T.D.H.6
  • 19
    • 33846527200 scopus 로고    scopus 로고
    • Investigation of a general base mechanism for ester hydrolysis in C-C hydrolase enzymes of the α/β-hydrolase superfamily: A novel mechanism for the serine catalytic triad
    • DOI 10.1039/b615605c
    • Li, J. J. and Bugg, T. D. (2007) Investigation of a general base mechanism for ester hydrolysis in C-C hydrolase enzymes of the α/β-hydrolase superfamily: A novel mechanism for the serine catalytic triad Org. Biomol. Chem. 5, 507-513 (Pubitemid 46168256)
    • (2007) Organic and Biomolecular Chemistry , vol.5 , Issue.3 , pp. 507-513
    • Li, J.-J.1    Bugg, T.D.H.2
  • 20
    • 38149122142 scopus 로고    scopus 로고
    • Catalytic promiscuity in the α/β-hydrolase superfamily: Hydroxamic acid formation, C-C bond formation, ester and thioester hydrolysis in the C-C hydrolase family
    • Li, C., Hassler, M., and Bugg, T. D. (2008) Catalytic promiscuity in the α/β-hydrolase superfamily: Hydroxamic acid formation, C-C bond formation, ester and thioester hydrolysis in the C-C hydrolase family ChemBioChem 9, 71-76
    • (2008) ChemBioChem , vol.9 , pp. 71-76
    • Li, C.1    Hassler, M.2    Bugg, T.D.3
  • 21
    • 84862788890 scopus 로고    scopus 로고
    • Promiscuous esterase activities of the C-C hydrolases from Dyella ginsengisoli
    • Zhou, H., Qu, Y., Kong, C., Wu, Y., Zhu, K., Yang, J., and Zhou, J. (2012) Promiscuous esterase activities of the C-C hydrolases from Dyella ginsengisoli Biotechnol. Lett. 34, 1107-1113
    • (2012) Biotechnol. Lett. , vol.34 , pp. 1107-1113
    • Zhou, H.1    Qu, Y.2    Kong, C.3    Wu, Y.4    Zhu, K.5    Yang, J.6    Zhou, J.7
  • 22
    • 0032483324 scopus 로고    scopus 로고
    • Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls
    • DOI 10.1074/jbc.273.36.22943
    • Seah, S. Y., Terracina, G., Bolin, J. T., Riebel, P., Snieckus, V., and Eltis, L. D. (1998) Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls J. Biol. Chem. 273, 22943-22949 (Pubitemid 28417469)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.36 , pp. 22943-22949
    • Seah, S.Y.K.1    Terracina, G.2    Bolin, J.T.3    Riebel, P.4    Snieckus, V.5    Eltis, L.D.6
  • 24
    • 0029758922 scopus 로고    scopus 로고
    • Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi
    • DOI 10.1021/bi9605292
    • Li, J., Szittner, R., Derewenda, Z. S., and Meighen, E. A. (1996) Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi Biochemistry 35, 9967-9973 (Pubitemid 26269911)
    • (1996) Biochemistry , vol.35 , Issue.31 , pp. 9967-9973
    • Li, J.1    Szittner, R.2    Derewenda, Z.S.3    Meighen, E.A.4
  • 25
    • 26644439533 scopus 로고    scopus 로고
    • Catalytic mechanism of fungal homoserine transacetylase
    • DOI 10.1021/bi0514764
    • Nazi, I. and Wright, G. D. (2005) Catalytic mechanism of fungal homoserine transacetylase Biochemistry 44, 13560-13566 (Pubitemid 41443683)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13560-13566
    • Nazi, I.1    Wright, G.D.2
  • 26
    • 37549050177 scopus 로고    scopus 로고
    • The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in polychlorinated biphenyls degradation: Large 3-substituents prevent tautomerization
    • Bhowmik, S., Horsman, G. P., Bolin, J. T., and Eltis, L. D. (2007) The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in polychlorinated biphenyls degradation: Large 3-substituents prevent tautomerization J. Biol. Chem. 282, 36377-36385
    • (2007) J. Biol. Chem. , vol.282 , pp. 36377-36385
    • Bhowmik, S.1    Horsman, G.P.2    Bolin, J.T.3    Eltis, L.D.4
  • 27
    • 0015932715 scopus 로고
    • Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin
    • Fastrez, J. and Fersht, A. R. (1973) Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin Biochemistry 12, 2025-2034
    • (1973) Biochemistry , vol.12 , pp. 2025-2034
    • Fastrez, J.1    Fersht, A.R.2
  • 28
    • 0015811262 scopus 로고
    • Evidence for a phosphoryl-enzyme intermediate in the catalytic reaction of prostatic acid phosphatase
    • Ostrowski, W. and Barnard, E. A. (1973) Evidence for a phosphoryl-enzyme intermediate in the catalytic reaction of prostatic acid phosphatase Biochemistry 12, 3893-3898
    • (1973) Biochemistry , vol.12 , pp. 3893-3898
    • Ostrowski, W.1    Barnard, E.A.2
  • 29
    • 77956021391 scopus 로고    scopus 로고
    • Switching from an esterase to a hydroxynitrile lyase mechanism requires only two amino acid substitutions
    • Padhi, S. K., Fujii, R., Legatt, G. A., Fossum, S. L., Berchtold, R., and Kazlauskas, R. J. (2010) Switching from an esterase to a hydroxynitrile lyase mechanism requires only two amino acid substitutions Chem. Biol. 17, 863-871
    • (2010) Chem. Biol. , vol.17 , pp. 863-871
    • Padhi, S.K.1    Fujii, R.2    Legatt, G.A.3    Fossum, S.L.4    Berchtold, R.5    Kazlauskas, R.J.6
  • 30
    • 80051856617 scopus 로고    scopus 로고
    • An inserted α/β subdomain shapes the catalytic pocket of Lactobacillus johnsonii cinnamoyl esterase
    • Lai, K. K., Stogios, P. J., Vu, C., Xu, X., Cui, H., Molloy, S., Savchenko, A., Yakunin, A., and Gonzalez, C. F. (2011) An inserted α/β subdomain shapes the catalytic pocket of Lactobacillus johnsonii cinnamoyl esterase PLoS One 6, e23269
    • (2011) PLoS One , vol.6 , pp. 23269
    • Lai, K.K.1    Stogios, P.J.2    Vu, C.3    Xu, X.4    Cui, H.5    Molloy, S.6    Savchenko, A.7    Yakunin, A.8    Gonzalez, C.F.9
  • 31
    • 0000707160 scopus 로고
    • An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin
    • Corey, D. R. and Craik, C. S. (1992) An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin J. Am. Chem. Soc. 114, 1784-1790
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 1784-1790
    • Corey, D.R.1    Craik, C.S.2
  • 33
    • 73649123859 scopus 로고    scopus 로고
    • Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism
    • Lack, N. A., Yam, K. C., Lowe, E. D., Horsman, G. P., Owen, R. L., Sim, E., and Eltis, L. D. (2010) Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism J. Biol. Chem. 285, 434-443
    • (2010) J. Biol. Chem. , vol.285 , pp. 434-443
    • Lack, N.A.1    Yam, K.C.2    Lowe, E.D.3    Horsman, G.P.4    Owen, R.L.5    Sim, E.6    Eltis, L.D.7


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