메뉴 건너뛰기




Volumn , Issue , 2016, Pages 1812-1824

The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent

Author keywords

biotin; enzyme; evolution; multidomain; multifunctional; substrate channeling

Indexed keywords

ALLOPHANATE HYDROLASE; CARBOXYLASE; ENZYME; UNCLASSIFIED DRUG; UREA AMIDOLYASE; UREA CARBOXYLASE;

EID: 84988377991     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2990     Document Type: Article
Times cited : (14)

References (49)
  • 1
    • 0035843184 scopus 로고    scopus 로고
    • Modular enzymes
    • Khosla C, Harbury PB (2001) Modular enzymes. Nature 409:247–252.
    • (2001) Nature , vol.409 , pp. 247-252
    • Khosla, C.1    Harbury, P.B.2
  • 2
    • 0344631518 scopus 로고    scopus 로고
    • Substrate channeling
    • Spivey HO, Ovadi J (1999) Substrate channeling. Methods 19:306–321.
    • (1999) Methods , vol.19 , pp. 306-321
    • Spivey, H.O.1    Ovadi, J.2
  • 3
    • 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 DH, Roberts DD, Cooper JT, Atkin AL, Petro TM, Nickerson KW (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
  • 6
    • 0015496201 scopus 로고
    • Urea carboxylase and allophanate hydrolase: two components of a multienzyme complex in Saccharomyces cerevisiae
    • Whitney PA, Cooper TG (1972) Urea carboxylase and allophanate hydrolase: two components of a multienzyme complex in Saccharomyces cerevisiae. Biochem Biophys Res Commun 49:45–51.
    • (1972) Biochem Biophys Res Commun , vol.49 , pp. 45-51
    • 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, 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-dependent degradation pathway specific to urea
    • Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T (2005) Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent 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
    • 84873880153 scopus 로고    scopus 로고
    • The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family
    • Lin Y, St Maurice M (2013) The structure of allophanate 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
  • 12
    • 84880518748 scopus 로고    scopus 로고
    • Structure and function of allophanate hydrolase
    • Fan C, Li Z, Yin H, Xiang S (2013) Structure and function of allophanate hydrolase. J Biol Chem 288:21422–21432.
    • (2013) J Biol Chem , vol.288 , pp. 21422-21432
    • Fan, C.1    Li, Z.2    Yin, H.3    Xiang, S.4
  • 13
    • 84858595979 scopus 로고    scopus 로고
    • Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction
    • Fan C, Chou CY, Tong L, 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
  • 14
    • 0033594863 scopus 로고    scopus 로고
    • A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system
    • Geck MK, Kirsch JF (1999) A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Biochemistry 38:8032–8037.
    • (1999) Biochemistry , vol.38 , pp. 8032-8037
    • Geck, M.K.1    Kirsch, J.F.2
  • 15
    • 0037133537 scopus 로고    scopus 로고
    • Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway
    • James CL, Viola RE (2002) Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway. Biochemistry 41:3726–3731.
    • (2002) Biochemistry , vol.41 , pp. 3726-3731
    • James, C.L.1    Viola, R.E.2
  • 17
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu T, Koronakis E, Hughes C, Koronakis V (1998) Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore. EMBO J 17:6487–6496.
    • (1998) EMBO J , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 18
    • 77949805991 scopus 로고    scopus 로고
    • Protein–protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations
    • Ianeselli L, Zhang F, Skoda MW, Jacobs RM, Martin RA, Callow S, Prevost S, Schreiber F (2010) Protein–protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations. J Phys Chem B 114:3776–3783.
    • (2010) J Phys Chem B , vol.114 , pp. 3776-3783
    • Ianeselli, L.1    Zhang, F.2    Skoda, M.W.3    Jacobs, R.M.4    Martin, R.A.5    Callow, S.6    Prevost, S.7    Schreiber, F.8
  • 19
    • 34548427923 scopus 로고    scopus 로고
    • Patterns of protein–protein interactions in salt solutions and implications for protein crystallization
    • Dumetz AC, Snellinger-O'Brien AM, Kaler EW, Lenhoff AM (2007) Patterns of protein–protein interactions in salt solutions and implications for protein crystallization. Protein Sci 16:1867–1877.
    • (2007) Protein Sci , vol.16 , pp. 1867-1877
    • Dumetz, A.C.1    Snellinger-O'Brien, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 20
    • 0037040937 scopus 로고    scopus 로고
    • A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role
    • Hettwer S, Sterner R (2002) A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role. J Biol Chem 277:8194–8201.
    • (2002) J Biol Chem , vol.277 , pp. 8194-8201
    • Hettwer, S.1    Sterner, R.2
  • 21
    • 84857881797 scopus 로고    scopus 로고
    • Protein–protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes
    • Baker P, Hillis C, Carere J, Seah SY (2012) Protein–protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes. Biochemistry 51:1942–1952.
    • (2012) Biochemistry , vol.51 , pp. 1942-1952
    • Baker, P.1    Hillis, C.2    Carere, J.3    Seah, S.Y.4
  • 22
    • 18944379412 scopus 로고    scopus 로고
    • Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP
    • Shapir N, Sadowsky MJ, Wackett LP (2005) Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J Bacteriol 187:3731–3738.
    • (2005) J Bacteriol , vol.187 , pp. 3731-3738
    • Shapir, N.1    Sadowsky, M.J.2    Wackett, L.P.3
  • 23
    • 33947667899 scopus 로고    scopus 로고
    • Protein–protein association in polymer solutions: from dilute to semidilute to concentrated
    • Kozer N, Kuttner YY, Haran G, Schreiber G (2007) Protein–protein association in polymer solutions: from dilute to semidilute to concentrated. Biophys J 92:2139–2149.
    • (2007) Biophys J , vol.92 , pp. 2139-2149
    • Kozer, N.1    Kuttner, Y.Y.2    Haran, G.3    Schreiber, G.4
  • 25
    • 84888876092 scopus 로고    scopus 로고
    • Functional analysis of TetR-family regulator AmtRsav in Streptomyces avermitilis
    • Chen Y, Zhu H, Zheng G, Jiang W, Lu Y (2013) Functional analysis of TetR-family regulator AmtRsav in Streptomyces avermitilis. Microbiology 159:2571–2583.
    • (2013) Microbiology , vol.159 , pp. 2571-2583
    • Chen, Y.1    Zhu, H.2    Zheng, G.3    Jiang, W.4    Lu, Y.5
  • 26
    • 77649282211 scopus 로고    scopus 로고
    • Relationship between operon preference and functional properties of persistent genes in bacterial genomes
    • Bratlie MS, Johansen J, Drablos F (2010) Relationship between operon preference and functional properties of persistent genes in bacterial genomes. BMC Genom 11:71-2164-11-71.
    • (2010) BMC Genom , vol.11 , pp. 2164-2171
    • Bratlie, M.S.1    Johansen, J.2    Drablos, F.3
  • 27
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan J, Eisenberg D (2007) The origin of protein interactions and allostery in colocalization. Nature 450:983–990.
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 29
    • 37049035985 scopus 로고    scopus 로고
    • Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensis
    • Chen B, Markillie LM, Xiong Y, Mayer MU, Squier TC (2007) Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensis. Biochemistry 46:14153–14161.
    • (2007) Biochemistry , vol.46 , pp. 14153-14161
    • Chen, B.1    Markillie, L.M.2    Xiong, Y.3    Mayer, M.U.4    Squier, T.C.5
  • 30
    • 33646120110 scopus 로고    scopus 로고
    • Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth
    • Shapir N, Cheng G, Sadowsky MJ, Wackett LP (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
  • 31
    • 0015210180 scopus 로고
    • Separation of the Chlorella ATP:Urea amido-lyase into two components
    • Thompson JF, Muenster AM (1971) Separation of the Chlorella ATP:Urea amido-lyase into two components. Biochem Biophys Res Commun 43:1049–1055.
    • (1971) Biochem Biophys Res Commun , vol.43 , pp. 1049-1055
    • Thompson, J.F.1    Muenster, A.M.2
  • 32
    • 84895795810 scopus 로고    scopus 로고
    • Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site
    • Singh H, Arentson BW, Becker DF, Tanner JJ (2014) Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci USA 111:3389–3394.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 3389-3394
    • Singh, H.1    Arentson, B.W.2    Becker, D.F.3    Tanner, J.J.4
  • 33
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product
    • Thoden JB, Holden HM, Wesenberg G, Raushel FM, Rayment I (1997) Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product. Biochemistry 36:6305–6316.
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 34
    • 84893659587 scopus 로고    scopus 로고
    • Evidence for hysteretic substrate channeling in the proline dehydrogenase and Delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA)
    • Moxley MA, Sanyal N, Krishnan N, Tanner JJ, Becker DF (2014) Evidence for hysteretic substrate channeling in the proline dehydrogenase and Delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA). J Biol Chem 289:3639–3651.
    • (2014) J Biol Chem , vol.289 , pp. 3639-3651
    • Moxley, M.A.1    Sanyal, N.2    Krishnan, N.3    Tanner, J.J.4    Becker, D.F.5
  • 35
    • 0034724435 scopus 로고    scopus 로고
    • An engineered blockage within the ammonia tunnel of carbamoyl phosphate synthetase prevents the use of glutamine as a substrate but not ammonia
    • Huang X, Raushel FM (2000) An engineered blockage within the ammonia tunnel of carbamoyl phosphate synthetase prevents the use of glutamine as a substrate but not ammonia. Biochemistry 39:3240–3247.
    • (2000) Biochemistry , vol.39 , pp. 3240-3247
    • Huang, X.1    Raushel, F.M.2
  • 37
    • 33645236152 scopus 로고    scopus 로고
    • Absence of substrate channeling between active sites in the Agrobacterium tumefaciens IspDF and IspE enzymes of the methyl erythritol phosphate pathway
    • Lherbet C, Pojer F, Richard SB, Noel JP, Poulter CD (2006) Absence of substrate channeling between active sites in the Agrobacterium tumefaciens IspDF and IspE enzymes of the methyl erythritol phosphate pathway. Biochemistry 45:3548–3553.
    • (2006) Biochemistry , vol.45 , pp. 3548-3553
    • Lherbet, C.1    Pojer, F.2    Richard, S.B.3    Noel, J.P.4    Poulter, C.D.5
  • 38
    • 2442599389 scopus 로고    scopus 로고
    • Absence of NADH channeling in coupled reaction of mitochondrial malate dehydrogenase and complex I in alamethicin-permeabilized rat liver mitochondria
    • Kotlyar AB, Maklashina E, Cecchini G (2004) Absence of NADH channeling in coupled reaction of mitochondrial malate dehydrogenase and complex I in alamethicin-permeabilized rat liver mitochondria. Biochem Biophys Res Commun 318:987–991.
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 987-991
    • Kotlyar, A.B.1    Maklashina, E.2    Cecchini, G.3
  • 41
    • 78649231644 scopus 로고    scopus 로고
    • Origins, evolution, and phenotypic impact of new genes
    • Kaessmann H (2010) Origins, evolution, and phenotypic impact of new genes. Genome Res 20:1313–1326.
    • (2010) Genome Res , vol.20 , pp. 1313-1326
    • Kaessmann, H.1
  • 42
    • 0032793852 scopus 로고    scopus 로고
    • Selfish operons: the evolutionary impact of gene clustering in prokaryotes and eukaryotes
    • Lawrence J (1999) Selfish operons: the evolutionary impact of gene clustering in prokaryotes and eukaryotes. Curr Opin Genet Dev 9:642–648.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 642-648
    • Lawrence, J.1
  • 43
    • 0037079014 scopus 로고    scopus 로고
    • The structure of the protein universe and genome evolution
    • Koonin EV, Wolf YI, Karev GP (2002) The structure of the protein universe and genome evolution. Nature 420:218–223.
    • (2002) Nature , vol.420 , pp. 218-223
    • Koonin, E.V.1    Wolf, Y.I.2    Karev, G.P.3
  • 45
    • 0030703189 scopus 로고    scopus 로고
    • Yeast pseudohyphal growth is regulated by GPA2, a G protein alpha homolog
    • Lorenz MC, Heitman J (1997) Yeast pseudohyphal growth is regulated by GPA2, a G protein alpha homolog. EMBO J 16:7008–7018.
    • (1997) EMBO J , vol.16 , pp. 7008-7018
    • Lorenz, M.C.1    Heitman, J.2
  • 47
    • 0011155266 scopus 로고
    • Nutritional control of dimorphism in Ceratocystis ulmi
    • Kulkarni RK, Nickerson KW (1981) Nutritional control of dimorphism in Ceratocystis ulmi. Exp Mycol 5:148–154.
    • (1981) Exp Mycol , vol.5 , pp. 148-154
    • Kulkarni, R.K.1    Nickerson, K.W.2
  • 48
    • 0028108943 scopus 로고
    • Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase
    • Chapman-Smith A, Turner DL, Cronan JE Jr, Morris TW, Wallace JC (1994) Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochem J 302:881–887.
    • (1994) Biochem J , vol.302 , pp. 881-887
    • Chapman-Smith, A.1    Turner, D.L.2    Cronan, J.E.3    Morris, T.W.4    Wallace, J.C.5
  • 49
    • 0037304566 scopus 로고    scopus 로고
    • Enzymatic assay for determination of bicarbonate ion in plasma using urea amidolyase
    • Kimura S, Yamanishi H, Iyama S, Yamaguchi Y, Kanakura Y (2003) Enzymatic assay for determination of bicarbonate ion in plasma using urea amidolyase. Clin Chim Acta 328:179–184.
    • (2003) Clin Chim Acta , vol.328 , pp. 179-184
    • Kimura, S.1    Yamanishi, H.2    Iyama, S.3    Yamaguchi, Y.4    Kanakura, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.