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Volumn 18, Issue 10, 2011, Pages 1230-1240

Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID DERIVATIVE; ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; ENZYME INHIBITOR; METAL; PHOSPHONOACETATE HYDROLASE; PHOSPHONOACETIC ACID;

EID: 80055084842     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2011.07.019     Document Type: Article
Times cited : (36)

References (45)
  • 1
    • 79959360686 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021
    • S.A. Borisova, H.D. Christman, M.E. Metcalf, N.A. Zulkepli, J.K. Zhang, W.A. van der Donk, and W.W. Metcalf Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021 J. Biol. Chem. 286 2011 22283 22290
    • (2011) J. Biol. Chem. , vol.286 , pp. 22283-22290
    • Borisova, S.A.1    Christman, H.D.2    Metcalf, M.E.3    Zulkepli, N.A.4    Zhang, J.K.5    Van Der Donk, W.A.6    Metcalf, W.W.7
  • 2
    • 33749010624 scopus 로고    scopus 로고
    • Structure and kinetics of phosphonopyruvate hydrolase from Voriovorax sp. Pal2: New insight into the divergence of catalysis within the pep mutase/isocitrate lyase superfamily
    • DOI 10.1021/bi061208l
    • C.C. Chen, Y. Han, W. Niu, A.N. Kulakova, A. Howard, J.P. Quinn, D. Dunaway-Mariano, and O. Herzberg Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily Biochemistry 45 2006 11491 11504 (Pubitemid 44453997)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11491-11504
    • Chen, C.C.H.1    Han, Y.2    Niu, W.3    Kulakova, A.N.4    Howard, A.5    Quinn, J.P.6    Dunaway-Mariano, D.7    Herzberg, O.8
  • 3
    • 0040531889 scopus 로고    scopus 로고
    • Marine organic phosphorus cycling: Novel insights from nuclear magnetic resonance
    • L.L. Clark, E.D. Ingall, and R. Benner Marine organic phosphorus cycling: novel insights from nuclear magnetic resonance Am. J. Sci. 299 1999 724 737
    • (1999) Am. J. Sci. , vol.299 , pp. 724-737
    • Clark, L.L.1    Ingall, E.D.2    Benner, R.3
  • 4
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • J.E. Coleman Structure and mechanism of alkaline phosphatase Annu. Rev. Biophys. Biomol. Struct. 21 1992 441 483
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 5
    • 33845304328 scopus 로고    scopus 로고
    • Phosphonoacetic acid utilization by fungal isolates: Occurrence and properties of a phosphonoacetate hydrolase in some penicillia
    • DOI 10.1016/j.mycres.2006.09.006, PII S0953756206002681
    • G. Forlani, M. Klimek-Ochab, J. Jaworski, B. Lejczak, and A.M. Picco Phosphonoacetic acid utilization by fungal isolates: occurrence and properties of a phosphonoacetate hydrolase in some penicillia Mycol. Res. 110 2006 1455 1463 (Pubitemid 44880685)
    • (2006) Mycological Research , vol.110 , Issue.12 , pp. 1455-1463
    • Forlani, G.1    Klimek-Ochab, M.2    Jaworski, J.3    Lejczak, B.4    Picco, A.M.5
  • 6
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifies phosphopentomutase and cofactor- independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • M.Y. Galperin, A. Bairoch, and E.V. Koonin A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases Protein Sci. 7 1998 1829 1835 (Pubitemid 29133189)
    • (1998) Protein Science , vol.7 , Issue.8 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 7
    • 9744279773 scopus 로고    scopus 로고
    • Divergent evolution in the enolase superfamily: The interplay of mechanism and specificity
    • DOI 10.1016/j.abb.2004.07.034, PII S0003986104004059
    • J.A. Gerlt, P.C. Babbitt, and I. Rayment Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity Arch. Biochem. Biophys. 433 2005 59 70 (Pubitemid 39586583)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 59-70
    • Gerlt, J.A.1    Babbitt, P.C.2    Rayment, I.3
  • 8
    • 0033605749 scopus 로고    scopus 로고
    • A model of the transition state in the alkaline phosphatase reaction
    • DOI 10.1074/jbc.274.13.8351
    • K.M. Holtz, B. Stec, and E.R. Kantrowitz A model of the transition state in the alkaline phosphatase reaction J. Biol. Chem. 274 1999 8351 8354 (Pubitemid 29164618)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8351-8354
    • Holtz, K.M.1    Stec, B.2    Kantrowitz, E.R.3
  • 10
    • 0028901756 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase: Structure and mechanistic properties of the K166R mutant
    • A.T. Kallarakal, B. Mitra, J.W. Kozarich, J.A. Gerlt, J.G. Clifton, G.A. Petsko, and G.L. Kenyon Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant Biochemistry 34 1995 2788 2797
    • (1995) Biochemistry , vol.34 , pp. 2788-2797
    • Kallarakal, A.T.1    Mitra, B.2    Kozarich, J.W.3    Gerlt, J.A.4    Clifton, J.G.5    Petsko, G.A.6    Kenyon, G.L.7
  • 11
    • 79955411030 scopus 로고    scopus 로고
    • Divergence of chemical function in the alkaline phosphatase superfamily: Structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase
    • A. Kim, M.M. Benning, S. OkLee, J. Quinn, B.M. Martin, H.M. Holden, and D. Dunaway-Mariano Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase Biochemistry 50 2011 3481 3494
    • (2011) Biochemistry , vol.50 , pp. 3481-3494
    • Kim, A.1    Benning, M.M.2    Oklee, S.3    Quinn, J.4    Martin, B.M.5    Holden, H.M.6    Dunaway-Mariano, D.7
  • 12
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures: Two-metal ion catalysis
    • E.E. Kim, and H.W. Wyckoff Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis J. Mol. Biol. 218 1991 449 464 (Pubitemid 121003358)
    • (1991) Journal of Molecular Biology , vol.218 , Issue.2 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 13
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • DOI 10.1016/S0969-2126(96)00097-4
    • G.J. Kleywegt, and A.T. Brünger Checking your imagination: applications of the free R value Structure 4 1996 897 904 (Pubitemid 26324702)
    • (1996) Structure , vol.4 , Issue.8 , pp. 897-904
    • Kleywegt, G.J.1    Brunger, A.T.2
  • 14
    • 0036477178 scopus 로고    scopus 로고
    • Phosphonates and their degradation by microorganisms
    • S.V. Kononova, and M.A. Nesmeyanova Phosphonates and their degradation by microorganisms Biochemistry (Mosc.) 67 2002 184 195 (Pubitemid 34474091)
    • (2002) Biochemistry (Moscow) , vol.67 , Issue.1 , pp. 184-195
    • Kononova, S.V.1    Nesmeyanova, M.A.2
  • 15
    • 0030792169 scopus 로고    scopus 로고
    • Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida
    • DOI 10.1016/S0378-1119(97)00151-0, PII S0378111997001510
    • A.N. Kulakova, L.A. Kulakov, and J.P. Quinn Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida Gene 195 1997 49 53 (Pubitemid 27336960)
    • (1997) Gene , vol.195 , Issue.1 , pp. 49-53
    • Kulakova, A.N.1    Kulakov, L.A.2    P. Quinn, J.3
  • 16
    • 0037931360 scopus 로고    scopus 로고
    • The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp. Pal2
    • DOI 10.1074/jbc.M301871200
    • A.N. Kulakova, G.B. Wisdom, L.A. Kulakov, and J.P. Quinn The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2 J. Biol. Chem. 278 2003 23426 23431 (Pubitemid 36830159)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23426-23431
    • Kulakova, A.N.1    Wisdom, G.B.2    Kulakov, L.A.3    Quinn, J.P.4
  • 18
    • 57049143713 scopus 로고    scopus 로고
    • Promiscuous sulfatase activity and thio-effects in a phosphodiesterase of the alkaline phosphatase superfamily
    • J.K. Lassila, and D. Herschlag Promiscuous sulfatase activity and thio-effects in a phosphodiesterase of the alkaline phosphatase superfamily Biochemistry 47 2008 12853 12859
    • (2008) Biochemistry , vol.47 , pp. 12853-12859
    • Lassila, J.K.1    Herschlag, D.2
  • 19
    • 0028791603 scopus 로고
    • The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F
    • J.W. McGrath, G.B. Wisdom, G. McMullan, M.J. Larkin, and J.P. Quinn The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F Eur. J. Biochem. 234 1995 225 230
    • (1995) Eur. J. Biochem. , vol.234 , pp. 225-230
    • McGrath, J.W.1    Wisdom, G.B.2    McMullan, G.3    Larkin, M.J.4    Quinn, J.P.5
  • 20
    • 0026554431 scopus 로고
    • Metabolism of phosphonoacetate as the sole carbon and phosphorus source by an environmental bacterial isolate
    • G. McMullan, F. Harrington, and J.P. Quinn Metabolism of phosphonoacetate as the sole carbon and phosphorus source by an environmental bacterial isolate Appl. Environ. Microbiol. 58 1992 1364 1366
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1364-1366
    • McMullan, G.1    Harrington, F.2    Quinn, J.P.3
  • 21
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • DOI 10.1006/jsbi.1999.4094
    • D.E. McRee XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165 (Pubitemid 29402600)
    • (1999) Journal of Structural Biology , vol.125 , Issue.2-3 , pp. 156-165
    • McRee, D.E.1
  • 22
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of phosphonic and phosphinic acid natural products
    • W.W. Metcalf, and W.A. van der Donk Biosynthesis of phosphonic and phosphinic acid natural products Annu. Rev. Biochem. 78 2009 65 94
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 65-94
    • Metcalf, W.W.1    Van Der Donk, W.A.2
  • 23
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the had enzyme superfamily
    • DOI 10.1021/bi001171j
    • M.C. Morais, W. Zhang, A.S. Baker, G. Zhang, D. Dunaway-Mariano, and K.N. Allen The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily Biochemistry 39 2000 10385 10396 (Pubitemid 30655914)
    • (2000) Biochemistry , vol.39 , Issue.34 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 26
    • 21644470988 scopus 로고    scopus 로고
    • Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions
    • DOI 10.1021/ja051603j
    • I. Nikolic-Hughes, P.J. O'Brien, and D. Herschlag Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions J. Am. Chem. Soc. 127 2005 9314 9315 (Pubitemid 40934714)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.26 , pp. 9314-9315
    • Nikolic-Hughes, I.1    O'Brien, P.J.2    Herschlag, D.3
  • 27
    • 0037022815 scopus 로고    scopus 로고
    • Alkaline phosphatase revisited: Hydrolysis of alkyl phosphates
    • DOI 10.1021/bi012166y
    • P.J. O'Brien, and D. Herschlag Alkaline phosphatase revisited: hydrolysis of alkyl phosphates Biochemistry 41 2002 3207 3225 (Pubitemid 34187642)
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 3207-3225
    • O'Brien, P.J.1    Herschlag, D.2
  • 28
    • 0344823660 scopus 로고    scopus 로고
    • SpaC and NisC, the Cyclases Involved in Subtilin and Nisin Biosynthesis, Are Zinc Proteins
    • DOI 10.1021/bi0354942
    • N.M. Okeley, M. Paul, J.P. Stasser, N. Blackburn, and W.A. van der Donk SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins Biochemistry 42 2003 13613 13624 (Pubitemid 37444912)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13613-13624
    • Okeley, N.M.1    Paul, M.2    Stasser, J.P.3    Blackburn, N.4    Van Der Donk, W.A.5
  • 30
    • 33645457997 scopus 로고    scopus 로고
    • Detection of phosphonoacetate degradation and phnA genes in soil bacteria from distinct geographical origins suggest its possible biogenic origin
    • P. Panas, N.G. Ternan, J.S. Dooley, and G. McMullan Detection of phosphonoacetate degradation and phnA genes in soil bacteria from distinct geographical origins suggest its possible biogenic origin Environ. Microbiol. 8 2006 939 945
    • (2006) Environ. Microbiol. , vol.8 , pp. 939-945
    • Panas, P.1    Ternan, N.G.2    Dooley, J.S.3    McMullan, G.4
  • 31
    • 0030809260 scopus 로고    scopus 로고
    • wARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • DOI 10.1107/S0907444997005696
    • A. Perrakis, T.K. Sixma, K.S. Wilson, and V.S. Lamzin wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models Acta Crystallogr. D Biol. Crystallogr. 53 1997 448 455 (Pubitemid 27340643)
    • (1997) Acta Crystallographica Section D: Biological Crystallography , vol.53 , Issue.4 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 32
    • 34548379026 scopus 로고    scopus 로고
    • New ways to break an old bond: The bacterial carbon-phosphorus hydrolases and their role in biogeochemical phosphorus cycling
    • DOI 10.1111/j.1462-2920.2007.01397.x
    • J.P. Quinn, A.N. Kulakova, N.A. Cooley, and J.W. McGrath New ways to break an old bond: the bacterial carbon-phosphorus hydrolases and their role in biogeochemical phosphorus cycling Environ. Microbiol. 9 2007 2392 2400 (Pubitemid 47366673)
    • (2007) Environmental Microbiology , vol.9 , Issue.10 , pp. 2392-2400
    • Quinn, J.P.1    Kulakova, A.N.2    Cooley, N.A.3    McGrath, J.W.4
  • 34
    • 0000327968 scopus 로고
    • Phosphate incorporation into alkaline phosphatase of E. coli
    • J.H. Schwartz, and F. Lipmann Phosphate incorporation into alkaline phosphatase of E. coli Proc. Natl. Acad. Sci. U S A 47 1961 1996 2005
    • (1961) Proc. Natl. Acad. Sci. U S A , vol.47 , pp. 1996-2005
    • Schwartz, J.H.1    Lipmann, F.2
  • 35
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • B. Stec, K.M. Holtz, and E.R. Kantrowitz A revised mechanism for the alkaline phosphatase reaction involving three metal ions J. Mol. Biol. 299 2000 1303 1311
    • (2000) J. Mol. Biol. , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 36
    • 0033963234 scopus 로고    scopus 로고
    • Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6
    • N.G. Ternan, J.T. Hamilton, and J.P. Quinn Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6 Arch. Microbiol. 173 2000 35 41 (Pubitemid 30060678)
    • (2000) Archives of Microbiology , vol.173 , Issue.1 , pp. 35-41
    • Ternan, N.G.1    Hamilton, J.T.G.2    Quinn, J.P.3
  • 38
    • 0023101749 scopus 로고
    • Bacterial carbon-phosphorus lyase: Products, rates, and regulation of phosphonic and phosphinic acid metabolism
    • L.P. Wackett, S.L. Shames, C.P. Venditti, and C.T. Walsh Bacterial carbon-phosphorus lyase: products, rates, and regulation of phosphonic and phosphinic acid metabolism J. Bacteriol. 169 1987 710 717 (Pubitemid 17010886)
    • (1987) Journal of Bacteriology , vol.169 , Issue.2 , pp. 710-717
    • Wackett, L.P.1    Shames, S.L.2    Venditti, C.P.3    Walsh, C.T.4
  • 39
    • 20444390656 scopus 로고    scopus 로고
    • Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase
    • DOI 10.1021/bi050155p
    • J. Wang, K.A. Stieglitz, and E.R. Kantrowitz Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase Biochemistry 44 2005 8378 8386 (Pubitemid 40799918)
    • (2005) Biochemistry , vol.44 , Issue.23 , pp. 8378-8386
    • Wang, J.1    Stieglitz, K.A.2    Kantrowitz, E.R.3
  • 40
    • 35848942616 scopus 로고    scopus 로고
    • Microbial metabolism of reduced phosphorus compounds
    • DOI 10.1146/annurev.micro.61.080706.093357
    • A.K. White, and W.W. Metcalf Microbial metabolism of reduced phosphorus compounds Annu. Rev. Microbiol. 61 2007 379 400 (Pubitemid 350058214)
    • (2007) Annual Review of Microbiology , vol.61 , pp. 379-400
    • White, A.K.1    Metcalf, W.W.2
  • 41
    • 0036130777 scopus 로고    scopus 로고
    • Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity
    • DOI 10.1110/ps.4260102
    • C.L. Wojciechowski, J.P. Cardia, and E.R. Kantrowitz Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity Protein Sci. 11 2002 903 911 (Pubitemid 34241298)
    • (2002) Protein Science , vol.11 , Issue.4 , pp. 903-911
    • Wojciechowski, C.L.1    Cardia, J.P.2    Kantrowitz, E.R.3
  • 42
    • 0037184908 scopus 로고    scopus 로고
    • Altering of the metal specificity of Escherichia coli alkaline phosphatase
    • DOI 10.1074/jbc.M209326200
    • C.L. Wojciechowski, and E.R. Kantrowitz Altering of the metal specificity of Escherichia coli alkaline phosphatase J. Biol. Chem. 277 2002 50476 50481 (Pubitemid 36042202)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50476-50481
    • Wojciechowski, C.L.1    Kantrowitz, E.R.2
  • 44
    • 33747517236 scopus 로고    scopus 로고
    • Structural and functional comparisons of nucleotide pyrophosphatase/ phosphodiesterase and alkaline phosphatase: Implications for mechanism and evolution
    • DOI 10.1021/bi060847t
    • J.G. Zalatan, T.D. Fenn, A.T. Brunger, and D. Herschlag Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications for mechanism and evolution Biochemistry 45 2006 9788 9803 (Pubitemid 44257425)
    • (2006) Biochemistry , vol.45 , Issue.32 , pp. 9788-9803
    • Zalatan, J.G.1    Fenn, T.D.2    Brunger, A.T.3    Herschlag, D.4
  • 45
    • 56949087215 scopus 로고    scopus 로고
    • Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion
    • J.G. Zalatan, T.D. Fenn, and D. Herschlag Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion J. Mol. Biol. 384 2008 1174 1189
    • (2008) J. Mol. Biol. , vol.384 , pp. 1174-1189
    • Zalatan, J.G.1    Fenn, T.D.2    Herschlag, D.3


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