메뉴 건너뛰기




Volumn 12, Issue 1, 2017, Pages

Structure and function of the N-terminal domain of Ralstonia eutropha polyhydroxyalkanoate synthase, and the proposed structure and mechanisms of the whole enzyme

Author keywords

3D reconstructed model; Enzyme mechanism; PHA synthase; PhaM; Polyhydroxyalkanoates

Indexed keywords

BACTERIA; DIMERS; ENZYMES; GRANULATION; THREE DIMENSIONAL COMPUTER GRAPHICS; X RAY SCATTERING;

EID: 85008956964     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201600649     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: Natural catalysts for plastics
    • Rehm, B. H., Polyester synthases: Natural catalysts for plastics. Biochem. J. 2003, 376, 15–33.
    • (2003) Biochem. J , vol.376 , pp. 15-33
    • Rehm, B.H.1
  • 2
    • 0010407860 scopus 로고    scopus 로고
    • Bacterial polyhydroxyalkanoates
    • Lee, S. Y., Bacterial polyhydroxyalkanoates. Biotechnol. Bioeng. 1996, 49, 1–14.
    • (1996) Biotechnol. Bioeng , vol.49 , pp. 1-14
    • Lee, S.Y.1
  • 3
    • 0036302861 scopus 로고    scopus 로고
    • A repressor protein, PhaR, regulates polyhydroxyalkanoate (PHA) synthesis via its direct interaction with PHA
    • Maehara, A., Taguchi, S., Nishiyama, T., Yamane, T., Doi, Y., A repressor protein, PhaR, regulates polyhydroxyalkanoate (PHA) synthesis via its direct interaction with PHA. J. Bacteriol. 2002, 184, 3992–4002.
    • (2002) J. Bacteriol , vol.184 , pp. 3992-4002
    • Maehara, A.1    Taguchi, S.2    Nishiyama, T.3    Yamane, T.4    Doi, Y.5
  • 4
    • 0024425823 scopus 로고
    • Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC)
    • Peoples, O. P., Sinskey, A. J., Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J. Biol. Chem. 1989, 264, 15298–15303.
    • (1989) J. Biol. Chem , vol.264 , pp. 15298-15303
    • Peoples, O.P.1    Sinskey, A.J.2
  • 5
    • 0002217020 scopus 로고    scopus 로고
    • PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo
    • Sim, S. J., Snell, K. D., Hogan, S. A., Stubbe, J. et al., PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo. Nat. Biotechnol. 1997, 15, 63–67.
    • (1997) Nat. Biotechnol , vol.15 , pp. 63-67
    • Sim, S.J.1    Snell, K.D.2    Hogan, S.A.3    Stubbe, J.4
  • 7
    • 33750993043 scopus 로고    scopus 로고
    • Sequence analysis and structure prediction of type II Pseudomonas sp. USM 4–55 PHA synthase and an insight into its catalytic mechanism
    • Wahab, H. A., Khairudin, N. B. A., Samian, M. R., Najimudin, N., Sequence analysis and structure prediction of type II Pseudomonas sp. USM 4–55 PHA synthase and an insight into its catalytic mechanism. BMC Struct. Biol. 2006, 6, 1.
    • (2006) BMC Struct. Biol , vol.6 , pp. 1
    • Wahab, H.A.1    Khairudin, N.B.A.2    Samian, M.R.3    Najimudin, N.4
  • 8
    • 0034636122 scopus 로고    scopus 로고
    • Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase
    • Jia, Y., Kappock, T. J., Frick, T., Sinskey, A. J., Stubbe, J., Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase. Biochemistry 2000, 39, 3927–3936.
    • (2000) Biochemistry , vol.39 , pp. 3927-3936
    • Jia, Y.1    Kappock, T.J.2    Frick, T.3    Sinskey, A.J.4    Stubbe, J.5
  • 9
    • 85008881293 scopus 로고    scopus 로고
    • Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms
    • Kim, J., Kim, Y-J., Choi, S. Y., Lee, S. Y., Kim, K-J., Crystal structure of Ralstonia eutropha polyhydroxyalkanoate synthase C-terminal domain and reaction mechanisms. Biotechnol. J. 2016, DOI: 10.1002/biot.201600648.
    • (2016) Biotechnol. J
    • Kim, J.1    Kim, Y.-J.2    Choi, S.Y.3    Lee, S.Y.4    Kim, K.-J.5
  • 10
    • 84997834600 scopus 로고    scopus 로고
    • Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator
    • Wittenborn, E. C., Jost, M., Wei, Y., Stubbe, J., Drennan, C. L., Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. J. Biol. Chem. 2016, 756833
    • (2016) J. Biol. Chem , pp. 756833
    • Wittenborn, E.C.1    Jost, M.2    Wei, Y.3    Stubbe, J.4    Drennan, C.L.5
  • 11
    • 33749166221 scopus 로고    scopus 로고
    • Mutation on N-terminus of polyhydroxybutyrate synthase of Ralstonia eutropha enhanced PHB accumulation
    • Zheng, Z., Li, M., Xue, X. J., Tian, H. L. et al., Mutation on N-terminus of polyhydroxybutyrate synthase of Ralstonia eutropha enhanced PHB accumulation. Appl. Microbiol. Biotechnol. 2006, 72, 896–905.
    • (2006) Appl. Microbiol. Biotechnol , vol.72 , pp. 896-905
    • Zheng, Z.1    Li, M.2    Xue, X.J.3    Tian, H.L.4
  • 12
    • 84862825731 scopus 로고    scopus 로고
    • Incremental truncation of PHA synthases results in altered product specificity
    • Wang, Q., Xia, Y., Chen, Q., Qi, Q., Incremental truncation of PHA synthases results in altered product specificity. Enzyme Microb. Technol. 2012, 50, 293–297.
    • (2012) Enzyme Microb. Technol , vol.50 , pp. 293-297
    • Wang, Q.1    Xia, Y.2    Chen, Q.3    Qi, Q.4
  • 13
    • 0020488703 scopus 로고
    • Calculated tyrosyl circular dichroism of proteins: Absence of tryptophan and cystine interferences in avian pancreatic polypeptide
    • Strassburger, W., Glatter, U., Wollmer, A., Fleischhauer, J. et al., Calculated tyrosyl circular dichroism of proteins: Absence of tryptophan and cystine interferences in avian pancreatic polypeptide. FEBS Lett. 1982, 139, 295–299.
    • (1982) FEBS Lett , vol.139 , pp. 295-299
    • Strassburger, W.1    Glatter, U.2    Wollmer, A.3    Fleischhauer, J.4
  • 14
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • Rambo, R. P., Tainer, J. A., Accurate assessment of mass, models and resolution by small-angle scattering. Nature 2013 496, 477–481.
    • (2013) Nature , Issue.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 15
    • 0026244044 scopus 로고
    • GNOM-a program package for small-angle scattering data processing
    • Semenyuk, A. V., Svergun, D. I., GNOM-a program package for small-angle scattering data processing. J. Appl. Crystallogr. 1991, 24, 537–540.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 16
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke, D., Svergun, D. I., DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J. Appl. Crystallogr. 2009, 42, 342–346.
    • (2009) J. Appl. Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 17
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., Svergun, D. I., Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 2003, 36, 860–864.
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 18
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C., Koch, M. H. J., CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 1995, 28, 768–773.
    • (1995) J. Appl. Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 19
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., Svergun, D. I., Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 2001, 34, 33–41.
    • (2001) J. Appl. Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 20
    • 0017145313 scopus 로고
    • Enzymatic synthesis of poly-β-hydroxybutyrate in Zoogloea ramigera
    • Fukui, T., Yoshimoto, A., Matsumoto, M., Hosokawa, S., Saito, T., Enzymatic synthesis of poly-β-hydroxybutyrate in Zoogloea ramigera. Arch. Microbiol. 1976, 110, 149–156.
    • (1976) Arch. Microbiol , vol.110 , pp. 149-156
    • Fukui, T.1    Yoshimoto, A.2    Matsumoto, M.3    Hosokawa, S.4    Saito, T.5
  • 21
    • 73949105231 scopus 로고    scopus 로고
    • Biosynthesis of polylactic acid and its copolymers using evolved propionate CoA transferase and PHA synthase
    • Yang, T. H., Kim, T. W., Kang, H. O., Lee, S. H. et al., Biosynthesis of polylactic acid and its copolymers using evolved propionate CoA transferase and PHA synthase. Biotechnol. Bioeng. 2010, 105, 150–160.
    • (2010) Biotechnol. Bioeng , vol.105 , pp. 150-160
    • Yang, T.H.1    Kim, T.W.2    Kang, H.O.3    Lee, S.H.4
  • 22
    • 73949094856 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for the production of polylactic acid and its copolymers
    • Jung, Y. K., Kim, T. Y., Park, S. J., Lee, S. Y., Metabolic engineering of Escherichia coli for the production of polylactic acid and its copolymers. Biotechnol. Bioeng. 2010, 105, 161–171.
    • (2010) Biotechnol. Bioeng , vol.105 , pp. 161-171
    • Jung, Y.K.1    Kim, T.Y.2    Park, S.J.3    Lee, S.Y.4
  • 23
    • 0018122036 scopus 로고
    • A rapid gas chromatographic method for the determination of poly-β-hydroxybutyric acid in microbial biomass
    • Braunegg, G., Sonnleitner, B. Y., Lafferty, R. M., A rapid gas chromatographic method for the determination of poly-β-hydroxybutyric acid in microbial biomass. European J. Appl. Microbiol. Biotechnol. 1978, 6, 29–37.
    • (1978) European J. Appl. Microbiol. Biotechnol , vol.6 , pp. 29-37
    • Braunegg, G.1    Sonnleitner, B.Y.2    Lafferty, R.M.3
  • 24
    • 84963516758 scopus 로고    scopus 로고
    • One-step fermentative production of poly(lactate-co-glycolate) from carbohydrates in Escherichia coli
    • Choi, S. Y., Park, S. J., Kim, W. J., Yang, J. E. et al., One-step fermentative production of poly(lactate-co-glycolate) from carbohydrates in Escherichia coli. Nat. Biotechnol. 2016, 34, 435–440.
    • (2016) Nat. Biotechnol , vol.34 , pp. 435-440
    • Choi, S.Y.1    Park, S.J.2    Kim, W.J.3    Yang, J.E.4
  • 25
    • 84863229520 scopus 로고    scopus 로고
    • Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei
    • Cai, S., Cai, L., Liu, H., Liu, X. et al., Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei. Appl. Environ. Microbiol. 2012, 78, 1946–1952.
    • (2012) Appl. Environ. Microbiol , vol.78 , pp. 1946-1952
    • Cai, S.1    Cai, L.2    Liu, H.3    Liu, X.4
  • 26
    • 18944405650 scopus 로고    scopus 로고
    • Kinetic studies of polyhydroxybutyrate granule formation in Wautersia eutropha H16 by transmission electron microscopy
    • Tian, J. M., Sinskey, A. J., Stubbe, J., Kinetic studies of polyhydroxybutyrate granule formation in Wautersia eutropha H16 by transmission electron microscopy. J. Bacteriol. 2005, 187, 3814–3824.
    • (2005) J. Bacteriol , vol.187 , pp. 3814-3824
    • Tian, J.M.1    Sinskey, A.J.2    Stubbe, J.3
  • 27
    • 9444254469 scopus 로고    scopus 로고
    • High level production of supra molecular weight poly (3-hydroxybutyrate) by metabolically engineered Escherichia coli
    • Choi, J. I., Lee, S. Y., High level production of supra molecular weight poly(3-hydroxybutyrate) by metabolically engineered Escherichia coli. Biotechnol. Bioprocess Eng. 2004, 9, 196–200.
    • (2004) Biotechnol. Bioprocess Eng , vol.9 , pp. 196-200
    • Choi, J.I.1    Lee, S.Y.2
  • 28
    • 0010407860 scopus 로고    scopus 로고
    • Bacterial polyhydroxyalkanoates
    • Lee, S. Y., Bacterial polyhydroxyalkanoates. Biotechnol. Bioeng. 1996, 49, 1–14.
    • (1996) Biotechnol. Bioeng , vol.49 , pp. 1-14
    • Lee, S.Y.1
  • 29
    • 33749166221 scopus 로고    scopus 로고
    • Mutation on N-terminus of polyhydroxybutyrate synthase of Ralstonia eutropha enhanced PHB accumulation
    • Zheng, Z., Li, M., Xue, X-J., Tian, H-L. et al., Mutation on N-terminus of polyhydroxybutyrate synthase of Ralstonia eutropha enhanced PHB accumulation. Appl. Microbiol. Biotechnol. 2006, 72, 896–905.
    • (2006) Appl. Microbiol. Biotechnol , vol.72 , pp. 896-905
    • Zheng, Z.1    Li, M.2    Xue, X.-J.3    Tian, H.-L.4
  • 30
    • 45449097050 scopus 로고    scopus 로고
    • Location of functional region at N-terminus of polyhydroxyalkanoate (PHA) synthase by N-terminal mutation and its effect of PHA synthesis
    • Ye, Z., Song, G., Chen, G., Chen, J., Location of functional region at N-terminus of polyhydroxyalkanoate (PHA) synthase by N-terminal mutation and its effect of PHA synthesis. Biochem. Eng. J. 2008, 41, 67–73.
    • (2008) Biochem. Eng. J , vol.41 , pp. 67-73
    • Ye, Z.1    Song, G.2    Chen, G.3    Chen, J.4
  • 31
    • 84892460614 scopus 로고    scopus 로고
    • PhaM is the physiological activator of poly(3-hydroxybutyrate) (PHB) synthase (PhaC1) in Ralstonia eutropha
    • Pfeiffer, D., Jendrossek, D., PhaM is the physiological activator of poly(3-hydroxybutyrate) (PHB) synthase (PhaC1) in Ralstonia eutropha. Appl. Environ. Microbiol. 2014, 80, 555–563.
    • (2014) Appl. Environ. Microbiol , vol.80 , pp. 555-563
    • Pfeiffer, D.1    Jendrossek, D.2
  • 32
    • 80855132840 scopus 로고    scopus 로고
    • Identification of a multifunctional protein, PhaM, that determines number, surface to volume ratio, subcellular localization and distribution to daughter cells of poly(3-hydroxybutyrate), PHB, granules in Ralstonia eutropha H16
    • Pfeiffer, D., Wahl, A., Jendrossek, D., Identification of a multifunctional protein, PhaM, that determines number, surface to volume ratio, subcellular localization and distribution to daughter cells of poly(3-hydroxybutyrate), PHB, granules in Ralstonia eutropha H16. Mol. Microbiol. 2011, 82, 936–951.
    • (2011) Mol. Microbiol , vol.82 , pp. 936-951
    • Pfeiffer, D.1    Wahl, A.2    Jendrossek, D.3
  • 33
    • 84869054255 scopus 로고    scopus 로고
    • PHB granules are attached to the nucleoid via PhaM in Ralstonia eutropha
    • Wahl, A., Schuth, N., Pfeiffer, D., Nussberger, S., Jendrossek, D., PHB granules are attached to the nucleoid via PhaM in Ralstonia eutropha. BMC Microbiol. 2012, 12, 262.
    • (2012) BMC Microbiol , vol.12 , pp. 262
    • Wahl, A.1    Schuth, N.2    Pfeiffer, D.3    Nussberger, S.4    Jendrossek, D.5
  • 34
    • 84952921103 scopus 로고    scopus 로고
    • Characterization of binding preference of polyhydroxyalkanoate biosynthesis-related multifunctional protein PhaM from Ralstonia eutropha
    • Ushimaru, K., Tsuge, T., Characterization of binding preference of polyhydroxyalkanoate biosynthesis-related multifunctional protein PhaM from Ralstonia eutropha. Appl. Microbiol. Biotechnol. 2016, 100, 4413–4421.
    • (2016) Appl. Microbiol. Biotechnol , vol.100 , pp. 4413-4421
    • Ushimaru, K.1    Tsuge, T.2
  • 35
    • 0027933456 scopus 로고
    • Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: Evidence for a required posttranslational modification for catalytic activity
    • Gerngross, T. U., Snell, K. D., Peoples, O. P., Sinskey A. J. et al., Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: Evidence for a required posttranslational modification for catalytic activity. Biochem. 1994, 33, 9311–9320.
    • (1994) Biochem , vol.33 , pp. 9311-9320
    • Gerngross, T.U.1    Snell, K.D.2    Peoples, O.P.3    Sinskey, A.J.4
  • 36
    • 84858680303 scopus 로고    scopus 로고
    • Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: Implications for the initiation and elongation of polymer formation in vivo
    • Cho, M., Brigham, C. J., Sinskey, A. J., Stubbe, J., Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: Implications for the initiation and elongation of polymer formation in vivo. Biochemistry 2012, 51, 2276–2288.
    • (2012) Biochemistry , vol.51 , pp. 2276-2288
    • Cho, M.1    Brigham, C.J.2    Sinskey, A.J.3    Stubbe, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.