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Volumn 288, Issue 29, 2013, Pages 21422-21432

Structure and function of allophanate hydrolase

Author keywords

[No Author keywords available]

Indexed keywords

C-DOMAIN; CATALYTIC MECHANISMS; DECARBOXYLATION REACTIONS; KLUYVEROMYCES LACTIS; MECHANISTIC STUDIES; SEQUENTIAL REACTION;

EID: 84880518748     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.453837     Document Type: Article
Times cited : (20)

References (46)
  • 2
    • 77957744758 scopus 로고    scopus 로고
    • The evolution and future of Earth's nitrogen cycle
    • Canfield, D. E., Glazer, A. N., and Falkowski, P. G. (2010) The evolution and future of Earth's nitrogen cycle. Science 330,192-196
    • (2010) Science , vol.330 , pp. 192-196
    • Canfield, D.E.1    Glazer, A.N.2    Falkowski, P.G.3
  • 3
    • 0024514293 scopus 로고
    • Microbial ureases: Significance, regulation, and molecular characterization
    • Mobley, H. L., and Hausinger, R. P. (1989) Microbial ureases: significance, regulation, and molecular characterization. Microbiol. Rev. 53, 85-108
    • (1989) Microbiol. Rev. , vol.53 , pp. 85-108
    • Mobley, H.L.1    Hausinger, R.P.2
  • 5
    • 0034585129 scopus 로고    scopus 로고
    • Plant ureases: Roles and regulation
    • Sirko, A., and Brodzik, R. (2000) Plant ureases: roles and regulation. Acta Biochim. Pol. 47,1189-1195
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 1189-1195
    • Sirko, A.1    Brodzik, R.2
  • 6
    • 0014409976 scopus 로고
    • An adenosine triphosphate-depen-dent, avidin-sensitive enzymatic cleavage of urea in yeast and green algae
    • Roon, R. J., and Levenberg, B. (1968) An adenosine triphosphate-depen- dent, avidin-sensitive enzymatic cleavage of urea in yeast and green algae. J. Biol. Chem. 243, 5213-5215
    • (1968) J. Biol. Chem. , vol.243 , pp. 5213-5215
    • Roon, R.J.1    Levenberg, B.2
  • 7
    • 0015500594 scopus 로고
    • Urea carboxylase and allopha-nate hydrolase. Two components of adenosine triphosphate:urea amido-lyase in Saccharomyces cerevisiae
    • Whitney, P. A., and Cooper, T. G. (1972) Urea carboxylase and allopha-nate hydrolase. Two components of adenosine triphosphate:urea amido-lyase in Saccharomyces cerevisiae. J. Biol. Chem. 247, 1349 -1353
    • (1972) J. Biol. Chem. , vol.247 , pp. 1349-1353
    • Whitney, P.A.1    Cooper, T.G.2
  • 8
    • 1942476071 scopus 로고    scopus 로고
    • Enzymatic characterization of a prokaryotic urea carboxylase
    • Kanamori, T., Kanou, N., Atomi, H., and Imanaka, T. (2004) Enzymatic characterization of a prokaryotic urea carboxylase. J. Bacteriol. 186, 2532-2539
    • (2004) J. Bacteriol. , vol.186 , pp. 2532-2539
    • Kanamori, T.1    Kanou, N.2    Atomi, H.3    Imanaka, T.4
  • 9
    • 15744397833 scopus 로고    scopus 로고
    • Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-de-pendent degradation pathway specific to urea
    • Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H., and Imanaka, T. (2005) Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-de-pendent degradation pathway specific to urea. FEMS Microbiol. Lett. 245, 61-65
    • (2005) FEMS Microbiol. Lett. , vol.245 , pp. 61-65
    • Kanamori, T.1    Kanou, N.2    Kusakabe, S.3    Atomi, H.4    Imanaka, T.5
  • 11
    • 79953090712 scopus 로고    scopus 로고
    • Molecular evolution of urea amidolyase and urea carboxylase in fungi
    • Strope, P. K., Nickerson, K. W., Harris, S. D., and Moriyama, E. N. (2011) Molecular evolution of urea amidolyase and urea carboxylase in fungi. BMC Evol. Biol. 11, 80
    • (2011) BMC Evol. Biol. , vol.11 , pp. 80
    • Strope, P.K.1    Nickerson, K.W.2    Harris, S.D.3    Moriyama, E.N.4
  • 12
    • 0015797031 scopus 로고
    • Urease and ATP:urea amidolyase activity in unicellular algae
    • Leftley, J. W., and Syrett, P. J. (1973) Urease and ATP:urea amidolyase activity in unicellular algae. J. Gen. Microbiol. 77, 109 -115
    • (1973) J. Gen. Microbiol. , vol.77 , pp. 109-115
    • Leftley, J.W.1    Syrett, P.J.2
  • 14
    • 63149099843 scopus 로고    scopus 로고
    • Arginine-induced germ tube formation in Candida albicans is essential for escape from murine macrophage line RAW 264.7
    • Ghosh, S., Navarathna, D. H., Roberts, D. D., Cooper, J. T., Atkin, A. L., Petro, T. M., and Nickerson, K. W. (2009) Arginine-induced germ tube formation in Candida albicans is essential for escape from murine macrophage line RAW 264.7. Infect. Immun. 77,1596 -1605
    • (2009) Infect. Immun. , vol.77 , pp. 1596-1605
    • Ghosh, S.1    Navarathna, D.H.2    Roberts, D.D.3    Cooper, J.T.4    Atkin, A.L.5    Petro, T.M.6    Nickerson, K.W.7
  • 15
    • 84855199285 scopus 로고    scopus 로고
    • The fungal pathogen Candida albicans autoinduces hyphal morphogenesis by raising extracellular pH
    • Vylkova, S., Carman, A. J., Danhof, H. A., Collette, J. R., Zhou, H., and Lorenz, M. C. (2011) The fungal pathogen Candida albicans autoinduces hyphal morphogenesis by raising extracellular pH. MBio 2, e00055-00011
    • (2011) MBio , vol.2
    • Vylkova, S.1    Carman, A.J.2    Danhof, H.A.3    Collette, J.R.4    Zhou, H.5    Lorenz, M.C.6
  • 17
    • 23744510357 scopus 로고    scopus 로고
    • Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism
    • Cheng, G., Shapir, N., Sadowsky, M. J., and Wackett, L. P. (2005) Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71, 4437- 4445
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4437-4445
    • Cheng, G.1    Shapir, N.2    Sadowsky, M.J.3    Wackett, L.P.4
  • 18
    • 18944379412 scopus 로고    scopus 로고
    • Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp
    • Shapir, N., Sadowsky, M. J., and Wackett, L. P. (2005) Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J.Bacteriol. 187, 3731-3738
    • (2005) Strain ADP. J.Bacteriol. , vol.187 , pp. 3731-3738
    • Shapir, N.1    Sadowsky, M.J.2    Wackett, L.P.3
  • 19
    • 33646120110 scopus 로고    scopus 로고
    • Purification and characterization of TrzF: Biuret hydrolysis by allophanate hydrolase supports growth
    • Shapir, N., Cheng, G., Sadowsky, M. J., and Wackett, L. P. (2006) Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72, 2491-2495
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2491-2495
    • Shapir, N.1    Cheng, G.2    Sadowsky, M.J.3    Wackett, L.P.4
  • 20
    • 79952125790 scopus 로고    scopus 로고
    • The structure of TTHA0988 from Thermus ther-mophilus, a Kipl-KipA homologue incorrectly annotated as an allophanate hydrolase
    • Jacques, D. A., Langley, D. B., Kuramitsu, S., Yokoyama, S., Trewhella, J., and Guss, J. M. (2011) The structure of TTHA0988 from Thermus ther-mophilus, a Kipl-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallogr. D Biol. Crystallogr. 67, 105-111
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 105-111
    • Jacques, D.A.1    Langley, D.B.2    Kuramitsu, S.3    Yokoyama, S.4    Trewhella, J.5    Guss, J.M.6
  • 22
    • 84858595979 scopus 로고    scopus 로고
    • Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction
    • Fan, C., Chou, C. Y., Tong, L., and Xiang, S. (2012) Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction. J. Biol. Chem. 287, 9389-9398
    • (2012) J. Biol. Chem. , vol.287 , pp. 9389-9398
    • Fan, C.1    Chou, C.Y.2    Tong, L.3    Xiang, S.4
  • 23
    • 0029916726 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9
    • Doublie, S., Kapp, U., Aberg, A., Brown, K., Strub, K., and Cusack, S. (1996) Crystallization and preliminary x-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9. FEBS Lett. 384, 219-221
    • (1996) FEBS Lett. , vol.384 , pp. 219-221
    • Doublie, S.1    Kapp, U.2    Aberg, A.3    Brown, K.4    Strub, K.5    Cusack, S.6
  • 24
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenstrom, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 29
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling
    • Bracey, M. H., Hanson, M. A., Masuda, K. R., Stevens, R. C., and Cravatt, B. F. (2002) Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling. Science 298,1793-1796
    • (2002) Science , vol.298 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 30
    • 0037013923 scopus 로고    scopus 로고
    • Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature
    • Shin, S., Lee, T. H., Ha, N. C., Koo, H. M., Kim, S. Y., Lee, H. S., Kim, Y. S., and Oh, B. H. (2002) Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature. EMBO J. 21, 2509-2516
    • (2002) EMBO J , vol.21 , pp. 2509-2516
    • Shin, S.1    Lee, T.H.2    Ha, N.C.3    Koo, H.M.4    Kim, S.Y.5    Lee, H.S.6    Kim, Y.S.7    Oh, B.H.8
  • 31
    • 33745596803 scopus 로고    scopus 로고
    • Ammonia channel couples glutaminase with transamidase reactions in GatCAB
    • Nakamura, A., Yao, M., Chimnaronk, S., Sakai, N., and Tanaka, I. (2006) Ammonia channel couples glutaminase with transamidase reactions in GatCAB. Science 312,1954-1958
    • (2006) Science , vol.312 , pp. 1954-1958
    • Nakamura, A.1    Yao, M.2    Chimnaronk, S.3    Sakai, N.4    Tanaka, I.5
  • 32
    • 68149137734 scopus 로고    scopus 로고
    • Insights into tRNA-dependent amidotransferase evolution and catalysis from the structure of the Aquifex aeolicus enzyme
    • Wu, J., Bu, W., Sheppard, K., Kitabatake, M., Kwon, S. T., Soll, D., and Smith, J. L. (2009) Insights into tRNA-dependent amidotransferase evolution and catalysis from the structure of the Aquifex aeolicus enzyme. J. Mol. Biol. 391, 703-716
    • (2009) J. Mol. Biol. , vol.391 , pp. 703-716
    • Wu, J.1    Bu, W.2    Sheppard, K.3    Kitabatake, M.4    Kwon, S.T.5    Soll, D.6    Smith, J.L.7
  • 33
    • 77957334080 scopus 로고    scopus 로고
    • Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions
    • Ito, T., and Yokoyama, S. (2010) Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions. Nature 467, 612-616
    • (2010) Nature , vol.467 , pp. 612-616
    • Ito, T.1    Yokoyama, S.2
  • 35
    • 0036409093 scopus 로고    scopus 로고
    • An alternative mechanism for amidase signature enzymes
    • Labahn, J., Neumann, S., Biildt, G., Kula, M. R., and Granzin, J. (2002) An alternative mechanism for amidase signature enzymes. J. Mol. Biol. 322, 1053-1064
    • (2002) J. Mol. Biol. , vol.322 , pp. 1053-1064
    • Labahn, J.1    Neumann, S.2    Biildt, G.3    Kula, M.R.4    Granzin, J.5
  • 36
    • 74049115832 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the 6-aminohexano-ate cyclic dimer hydrolase: Catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation
    • Yasuhira, K., Shibata, N., Mongami, G., Uedo, Y., Atsumi, Y., Kawashima, Y., Hibino, A., Tanaka, Y., Lee, Y. H., Kato, D., Takeo, M., Higuchi, Y., and Negoro, S. (2010) X-ray crystallographic analysis of the 6-aminohexano-ate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation. J. Biol. Chem. 285, 1239-1248
    • (2010) J. Biol. Chem. , vol.285 , pp. 1239-1248
    • Yasuhira, K.1    Shibata, N.2    Mongami, G.3    Uedo, Y.4    Atsumi, Y.5    Kawashima, Y.6    Hibino, A.7    Tanaka, Y.8    Lee, Y.H.9    Kato, D.10    Takeo, M.11    Higuchi, Y.12    Negoro, S.13
  • 37
    • 71649107994 scopus 로고    scopus 로고
    • Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition
    • Ohtaki, A., Murata, K., Sato, Y., Noguchi, K., Miyatake, H., Dohmae, N., Yamada, K., Yohda, M., and Odaka, M. (2010) Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition. Biochim. Biophys. Acta 1804, 184-192
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 184-192
    • Ohtaki, A.1    Murata, K.2    Sato, Y.3    Noguchi, K.4    Miyatake, H.5    Dohmae, N.6    Yamada, K.7    Yohda, M.8    Odaka, M.9
  • 38
    • 0043092112 scopus 로고    scopus 로고
    • Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad
    • Shin, S., Yun, Y. S., Koo, H. M., Kim, Y. S., Choi, K. Y., and Oh, B. H. (2003) Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad. J. Biol. Chem. 278, 24937-24943
    • (2003) J. Biol. Chem. , vol.278 , pp. 24937-24943
    • Shin, S.1    Yun, Y.S.2    Koo, H.M.3    Kim, Y.S.4    Choi, K.Y.5    Oh, B.H.6
  • 39
    • 84892432934 scopus 로고
    • Thermal decomposition ofsodium car-bamate
    • Abe, S., and Takahashi, S. (1959) Thermal decomposition ofsodium car-bamate. Nippon Kagaku Zasshi 80, 92-94
    • (1959) Nippon Kagaku Zasshi , vol.80 , pp. 92-94
    • Abe, S.1    Takahashi, S.2
  • 40
    • 52049115466 scopus 로고    scopus 로고
    • The identification and structural characterization of C7orf24 as 7-glutamyl cyclotransferase. An essential enzyme in the 7-glutamyl cycle
    • Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., and Board, P. G. (2008) The identification and structural characterization of C7orf24 as 7-glutamyl cyclotransferase. An essential enzyme in the 7-glutamyl cycle. J.Biol. Chem. 283, 22031-22042
    • (2008) J.Biol. Chem. , vol.283 , pp. 22031-22042
    • Oakley, A.J.1    Yamada, T.2    Liu, D.3    Coggan, M.4    Clark, A.G.5    Board, P.G.6
  • 41
    • 77951218927 scopus 로고    scopus 로고
    • Identification and characterization of 7-glutamylamine cyclotransferase, an enzyme responsible for 7-glutamyl-e-lysine catabolism
    • Oakley, A. J., Coggan, M., and Board, P. G. (2010) Identification and characterization of 7-glutamylamine cyclotransferase, an enzyme responsible for 7-glutamyl-e-lysine catabolism. J. Biol. Chem. 285, 9642-9648
    • (2010) J. Biol. Chem. , vol.285 , pp. 9642-9648
    • Oakley, A.J.1    Coggan, M.2    Board, P.G.3
  • 42
    • 84864416838 scopus 로고    scopus 로고
    • Decarboxylation mechanisms in biological system
    • Li, T., Huo, L., Pulley, C., and Liu, A. (2012) Decarboxylation mechanisms in biological system. Bioorg. Chem. 43, 2-14
    • (2012) Bioorg. Chem. , vol.43 , pp. 2-14
    • Li, T.1    Huo, L.2    Pulley, C.3    Liu, A.4
  • 43
    • 27144523783 scopus 로고    scopus 로고
    • The catalytic triad of serine peptidases
    • Polgar, L. (2005) The catalytic triad of serine peptidases. Cell. Mol. Life Sci. 62, 2161-2172
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2161-2172
    • Polgar, L.1
  • 44
    • 0017102564 scopus 로고
    • Thermal adaptation in yeast: Growth temperatures, membrane lipid, and cytochrome composition of psychro-philic, mesophilic, and thermophilic yeasts
    • Arthur, H., and Watson, K. (1976) Thermal adaptation in yeast: growth temperatures, membrane lipid, and cytochrome composition of psychro-philic, mesophilic, and thermophilic yeasts. J. Bacteriol. 128, 56-68
    • (1976) J. Bacteriol. , vol.128 , pp. 56-68
    • Arthur, H.1    Watson, K.2
  • 45
    • 84873880153 scopus 로고    scopus 로고
    • The structure ofallophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family
    • Lin, Y., and St Maurice, M. (2013) The structure ofallophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family. Biochemistry 52, 690-700
    • (2013) Biochemistry , vol.52 , pp. 690-700
    • Lin, Y.1    St Maurice, M.2
  • 46
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., Pupko, T., Paz, I., Bell, R. E., Bechor-Shental, D., Martz, E., and Ben-Tal, N. (2003) ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19, 163-164
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7


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