메뉴 건너뛰기




Volumn 7, Issue 8, 1999, Pages 891-902

Glutamate mutase from Clostridium cochlearium: The structure of a coenzyme B12-dependent enzyme provides new mechanistic insights

Author keywords

Coenzyme B12; Glutamate mutase; Radical reactions

Indexed keywords

ASPARTIC ACID DERIVATIVE; CARBON; COBALT; COBAMAMIDE; GLUTAMIC ACID; HYDROGEN; METHYLMALONYL COENZYME A MUTASE; MUTASE; NITROGEN; POLYPEPTIDE; PROTEIN; RADICAL; TARTARIC ACID;

EID: 0033566661     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80116-6     Document Type: Article
Times cited : (203)

References (59)
  • 1
    • 0000019074 scopus 로고    scopus 로고
    • Corrin-dependent reactions
    • Sinnott, M., ed. Academic Press, London
    • Golding, B.T. & Buckel, W. (1998). Corrin-dependent reactions. In Comprehensive Biological Catalysis. (Sinnott, M., ed.), Vol. 3, pp. 239-259. Academic Press, London.
    • (1998) Comprehensive Biological Catalysis , vol.3 , pp. 239-259
    • Golding, B.T.1    Buckel, W.2
  • 2
    • 0022430394 scopus 로고
    • 12-dependent rearrangements
    • 12-dependent rearrangements. Science 227, 869-875.
    • (1985) Science , vol.227 , pp. 869-875
    • Halpern, J.1
  • 4
    • 0001665934 scopus 로고
    • Reaktionsselektivität von enzymen durch negative katalyse oder wie gehen enzyme mit hochreaktiven intermediaten um?
    • Rétey, J. (1990). Reaktionsselektivität von enzymen durch negative katalyse oder wie gehen enzyme mit hochreaktiven intermediaten um? Angew. Chem. 102, 373-379.
    • (1990) Angew. Chem. , vol.102 , pp. 373-379
    • Rétey, J.1
  • 5
    • 0001171486 scopus 로고    scopus 로고
    • High-resolution crystal structures of cobalamins
    • Kräutler, B., Arigoni, D. & Golding, B.T., eds. Wiley-VCH, Weinheim
    • 12-proteins. (Kräutler, B., Arigoni, D. & Golding, B.T., eds), pp. 335-347. Wiley-VCH, Weinheim.
    • (1998) 12-proteins , pp. 335-347
    • Gruber, K.1    Jogl, G.2    Klintschar, G.3    Kratky, C.4
  • 6
    • 0001957032 scopus 로고
    • 12 and cobaloximes
    • Dolphin, D., ed. Wiley-Interscience, New York
    • 12. (Dolphin, D., ed.), Vol. 1, pp. 23-107. Wiley-Interscience, New York.
    • (1982) 12 , vol.1 , pp. 23-107
    • Glusker, J.P.1
  • 11
    • 0030584657 scopus 로고    scopus 로고
    • 12 radicals are generated: The crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution
    • 12 radicals are generated: The crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution. Structure 4, 339-350.
    • (1996) Structure , vol.4 , pp. 339-350
    • Mancia, F.1    Evans, P.R.2
  • 12
    • 0032526407 scopus 로고    scopus 로고
    • Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism
    • Mancia, F. & Evans, P.R. (1998). Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism. Structure 6, 711-720.
    • (1998) Structure , vol.6 , pp. 711-720
    • Mancia, F.1    Evans, P.R.2
  • 14
    • 0000775966 scopus 로고
    • The glutamate mutase system, assays and properties
    • Barker, H.A., Rooze, V., Suzuki, F. & Iodice, A.A. (1964). The glutamate mutase system, assays and properties. J. Biol. Chem. 239, 3260-3266.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3260-3266
    • Barker, H.A.1    Rooze, V.2    Suzuki, F.3    Iodice, A.A.4
  • 15
    • 0001479241 scopus 로고
    • Glutamate mutase
    • Dolphin, D., ed. Wiley-Interscience, New York
    • 12. Dolphin, D., ed.), Vol. 2, pp. 289-355, Wiley-Interscience, New York.
    • (1982) 12 , vol.2 , pp. 289-355
    • Switzer, R.L.1
  • 16
    • 0026588982 scopus 로고
    • Glutamate mutase from Clostridium cochlearium - Purification, cobamide content and stereospecific inhibitors
    • Leutbecher, U., Bocher, R., Linder, D. & Buckel, W. (1992). Glutamate mutase from Clostridium cochlearium - Purification, cobamide content and stereospecific inhibitors. Eur. J. Biochem. 205, 759-765.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 759-765
    • Leutbecher, U.1    Bocher, R.2    Linder, D.3    Buckel, W.4
  • 17
    • 0028172856 scopus 로고
    • 12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli
    • 12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. Eur. J. Biochem. 226, 577-585.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 577-585
    • Zelder, O.1    Beatrix, B.2    Leutbecher, U.3    Buckel, W.4
  • 18
    • 0003215482 scopus 로고
    • 12 und verwandte corrinoide
    • Ammon, R. & Dirscherl, W., eds. Thieme Verlag, Stuttgart
    • 12 und verwandte corrinoide. In Fermente, Hormone, Vitamine. (Ammon, R. & Dirscherl, W., eds.), III/2, Thieme Verlag, Stuttgart.
    • (1975) Fermente, Hormone, Vitamine , vol.3 , Issue.2
    • Friedrich, W.1
  • 22
    • 0026701740 scopus 로고
    • Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum - Homologies with other cobalamin-dependent enzymes
    • Marsh, E.N.G. & Holloway, D.E. (1992). Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum - Homologies with other cobalamin-dependent enzymes. FEBS Lett. 310, 167-170.
    • (1992) FEBS Lett. , vol.310 , pp. 167-170
    • Marsh, E.N.G.1    Holloway, D.E.2
  • 23
    • 0032167586 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium
    • Reitzer, R., Krasser, M., Jogl, G., Buckel, W., Bothe, H. & Kratky, C. (1997). Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium. Acta Crystallogr. D 54, 1039-1042.
    • (1997) Acta Crystallogr. D , vol.54 , pp. 1039-1042
    • Reitzer, R.1    Krasser, M.2    Jogl, G.3    Buckel, W.4    Bothe, H.5    Kratky, C.6
  • 25
    • 0024618232 scopus 로고
    • Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction
    • Jansen, R., Kalousek, F., Fenton, W.A., Rosenberg, L.E. & Ledley, F.D. (1989). Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. Genomics 4, 198-205.
    • (1989) Genomics , vol.4 , pp. 198-205
    • Jansen, R.1    Kalousek, F.2    Fenton, W.A.3    Rosenberg, L.E.4    Ledley, F.D.5
  • 27
    • 0024832385 scopus 로고
    • 12 chemistry - The crystal and molecular structure of cob(II)alamin
    • 12 chemistry - The crystal and molecular structure of cob(II)alamin. J. Am. Chem. Soc. 111, 8936-8938.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8936-8938
    • Kräutler, B.1    Kratky, C.2    Keller, W.3
  • 28
    • 0030595334 scopus 로고    scopus 로고
    • High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor
    • Yeh, J.I., Biemann, H.P., Prive, G.G., Pandit, J., Koshland, D.E., Jr. & Kim, S.H. (1996). High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor. J. Mol. Biol. 262, 186-201.
    • (1996) J. Mol. Biol. , vol.262 , pp. 186-201
    • Yeh, J.I.1    Biemann, H.P.2    Prive, G.G.3    Pandit, J.4    Koshland D.E., Jr.5    Kim, S.H.6
  • 29
    • 0030889913 scopus 로고    scopus 로고
    • Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone
    • Mittl, P.R., et al., & Grutter, M.G. (1997). Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone. J. Biol. Chem. 272, 6539-6547.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6539-6547
    • Mittl, P.R.1    Grutter, M.G.2
  • 30
    • 0024293450 scopus 로고
    • Crystal structure determination, refinement and molecular model of creatine amidinohydrolase from Pseudomonas putida
    • Hoeffken, H.W., Knof, S.H., Bartlett, P.A., Huber, R., Moellering, H. & Schumacher, G. (1988). Crystal structure determination, refinement and molecular model of creatine amidinohydrolase from Pseudomonas putida. J. Mol. Biol. 204, 417-433.
    • (1988) J. Mol. Biol. , vol.204 , pp. 417-433
    • Hoeffken, H.W.1    Knof, S.H.2    Bartlett, P.A.3    Huber, R.4    Moellering, H.5    Schumacher, G.6
  • 31
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • Williams, P.A., Fulop, V., Garman, E.F., Saunders, N.F., Ferguson, S.J. & Hajdu, J. (1997). Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature 389, 406-412.
    • (1997) Nature , vol.389 , pp. 406-412
    • Williams, P.A.1    Fulop, V.2    Garman, E.F.3    Saunders, N.F.4    Ferguson, S.J.5    Hajdu, J.6
  • 32
    • 0029109922 scopus 로고
    • Atomic structure of the buried catalytic pocket of Escherichia coli chorismate mutase
    • Lee, A.Y., Karplus, P.A., Ganem, B. & Clardy, J. (1995). Atomic structure of the buried catalytic pocket of Escherichia coli chorismate mutase. J. Am. Chem. Soc. 117, 3627-3628.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3627-3628
    • Lee, A.Y.1    Karplus, P.A.2    Ganem, B.3    Clardy, J.4
  • 33
    • 0027992458 scopus 로고
    • The monofunctional chorismate mutase from Bacillus subtilis
    • Chook, Y.M., Gray, J.V., Ke, H. & Lipscomb, W.N. (1994). The monofunctional chorismate mutase from Bacillus subtilis. J. Mol. Biol. 240, 476-500.
    • (1994) J. Mol. Biol. , vol.240 , pp. 476-500
    • Chook, Y.M.1    Gray, J.V.2    Ke, H.3    Lipscomb, W.N.4
  • 34
    • 0028130539 scopus 로고
    • The crystal structure of allosteric chorismate mutase at 2.2 Å resolution
    • Xue, Y., Lipscomb, W.N., Graf, R., Schnappauf, G. & Braus, G. (1994). The crystal structure of allosteric chorismate mutase at 2.2 Å resolution. Proc. Natl Acad. Sci. USA 91, 10814-10818.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10814-10818
    • Xue, Y.1    Lipscomb, W.N.2    Graf, R.3    Schnappauf, G.4    Braus, G.5
  • 35
    • 0000725566 scopus 로고
    • Structure of the 5,6-dimethylbenzimidazolylcobamide coenzyme
    • Lenhert, P.G. & Hodgkin, D.C. (1961). Structure of the 5,6-dimethylbenzimidazolylcobamide coenzyme. Nature 192, 937-938.
    • (1961) Nature , vol.192 , pp. 937-938
    • Lenhert, P.G.1    Hodgkin, D.C.2
  • 37
    • 37049111526 scopus 로고
    • Anaerobic photodecomposition of alkylaquocobaloximes in aqueous solution
    • Golding, B.T., Kemp, T.J., Sellars, P.J. & Nocci, E. (1977). Anaerobic photodecomposition of alkylaquocobaloximes in aqueous solution. J. Chem. Soc. Dalton 1266-1272.
    • (1977) J. Chem. Soc. Dalton , pp. 1266-1272
    • Golding, B.T.1    Kemp, T.J.2    Sellars, P.J.3    Nocci, E.4
  • 38
    • 0000198545 scopus 로고
    • 12 coenzyme: Theory and models
    • Dolphin, D., ed. Wiley-Interscience, New York
    • 12. (Dolphin, D., ed.), Vol. 1, pp. 23-107. Wiley-Interscience, New York.
    • (1982) 12 , vol.1 , pp. 23-107
    • Golding, B.T.1
  • 39
    • 0017171488 scopus 로고
    • On the mechanism of action of adenosylcobalamin
    • Golding, B.T. & Radom, L. (1976). On the mechanism of action of adenosylcobalamin. J. Am. Chem. Soc. 98, 6331-6338.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 6331-6338
    • Golding, B.T.1    Radom, L.2
  • 42
    • 0017878143 scopus 로고
    • Investigation of the mechanism of the methylmalonyl-CoA mutase reaction with the substrate analogue: Ethylmalonyl-CoA
    • Rétey, J., Smith, E.H. & Zagalak, B. (1978). Investigation of the mechanism of the methylmalonyl-CoA mutase reaction with the substrate analogue: Ethylmalonyl-CoA. Eur. J. Biochem. 83, 437-451.
    • (1978) Eur. J. Biochem. , vol.83 , pp. 437-451
    • Rétey, J.1    Smith, E.H.2    Zagalak, B.3
  • 43
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. & Bailey, S., eds. Daresbury Laboratory, Warrington UK
    • Otwinowsky, Z. (1993). Oscillation data reduction program. In Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 55-62. Daresbury Laboratory, Warrington UK.
    • (1993) Data Collection and Processing , pp. 55-62
    • Otwinowsky, Z.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite - Programs for protein crystallography
    • Bailey, S. (1994). The CCP4 suite - Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 46
    • 0031937561 scopus 로고    scopus 로고
    • Accelerated X-ray structure elucidation of a 36 kDa muramidase/transglycosidase using wARP
    • van Asselt, E.J., Perrakis, A., Kalk, K.H. & Lamzin, V.S. (1998). Accelerated X-ray structure elucidation of a 36 kDa muramidase/transglycosidase using wARP. Acta Crystallogr. D 54, 58-73.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 58-73
    • Van Asselt, E.J.1    Perrakis, A.2    Kalk, K.H.3    Lamzin, V.S.4
  • 47
    • 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. & 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.3    Kjeldgaard, M.4
  • 49
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R-value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 50
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination - Applications of the free R-value
    • Kleywegt, G.J. & Brünger, A.T. (1996). Checking your imagination - Applications of the free R-value. Structure 4, 897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 51
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 52
    • 11944255126 scopus 로고
    • 12: High-resolution solid-state structure of aquocobalamin perchlorate and structure analysis of the aquocobalamin ion in solution
    • 12: High-resolution solid-state structure of aquocobalamin perchlorate and structure analysis of the aquocobalamin ion in solution. J. Am. Chem. Soc. 117, 4654-4670.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4654-4670
    • Kratky, C.1    Kräutler, B.2
  • 53
    • 0001805131 scopus 로고
    • Xabs2 - An empirical absorption correction program
    • Parkin, S., Moezzi, B. & Hope, H. (1995). Xabs2 - An empirical absorption correction program. J. Appl. Crystallogr. 28, 53-56.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 53-56
    • Parkin, S.1    Moezzi, B.2    Hope, H.3
  • 54
    • 0016430638 scopus 로고
    • Refinement of the structure of carp muscle calcium binding parvalbumin by model building and difference Fourier analysis
    • Moews, P.C. & Kretsinger, R.H. (1975). Refinement of the structure of carp muscle calcium binding parvalbumin by model building and difference Fourier analysis. J. Mol. Biol. 91, 201-228.
    • (1975) J. Mol. Biol. , vol.91 , pp. 201-228
    • Moews, P.C.1    Kretsinger, R.H.2
  • 55
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 56
    • 0000243829 scopus 로고
    • PROCHECK version 2.0. Programs to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK version 2.0. Programs to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 58
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. & Bacon, D.J. (1997). Raster3D: Photorealistic molecular graphics. Methods. Enzymol. 277, 505-524.
    • (1997) Methods. Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 59
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner, M.F., Spehner, J.-C. & Olson, A.J. (1996). Reduced surface: An efficient way to compute molecular surfaces. Biopolymers 38, 305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Spehner, J.-C.2    Olson, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.