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Volumn 95, Issue 3, 1999, Pages 125-132

Vitamin B12 joins the club: A review of structural studies and implications for mechanisms of enzymatic reactions

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EID: 0033020514     PISSN: 00382353     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (1)

References (50)
  • 4
    • 0032526407 scopus 로고    scopus 로고
    • Conformational changes on substrate binding to methylmalonyl Co A mutase and new insights into the free radical mechanism
    • Mancia F. and Evans P.R. (1998). Conformational changes on substrate binding to methylmalonyl Co A 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
  • 8
    • 0004115728 scopus 로고
    • Academic Press, London
    • 12. Academic Press, London.
    • (1972) 12
    • Pratt, J.M.1
  • 12
    • 0022430394 scopus 로고
    • 12-dependent rearrangements
    • 12-dependent rearrangements. Science 227, 869-875.
    • (1985) Science , vol.227 , pp. 869-875
    • Halpern, J.1
  • 13
    • 0025228772 scopus 로고
    • Cobalamin-dependent methionine synthase
    • Banerjee R.V. and Matthews R.G. (1990). Cobalamin-dependent methionine synthase. FASEB J. 4, 1450-1459.
    • (1990) FASEB J. , vol.4 , pp. 1450-1459
    • Banerjee, R.V.1    Matthews, R.G.2
  • 14
    • 0031104774 scopus 로고    scopus 로고
    • The Yin-Yang of cobalamin biochemistry
    • Banerjee R.V. (1997). The Yin-Yang of cobalamin biochemistry. Chem. Biol. 4, 175-186.
    • (1997) Chem. Biol. , vol.4 , pp. 175-186
    • Banerjee, R.V.1
  • 15
    • 0028597893 scopus 로고
    • Binding site revealed of nature's most beautiful cofactor
    • Stubbe J-A. (1994). Binding site revealed of nature's most beautiful cofactor. Science 266, 1663-1664.
    • (1994) Science , vol.266 , pp. 1663-1664
    • Stubbe, J.-A.1
  • 16
    • 0030829339 scopus 로고    scopus 로고
    • Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin and adenosylmethionine
    • Goulding C.W., Postigo D. and Matthews R.G. (1997). Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin and adenosylmethionine. Biochemistry 36, 8082-8091.
    • (1997) Biochemistry , vol.36 , pp. 8082-8091
    • Goulding, C.W.1    Postigo, D.2    Matthews, R.G.3
  • 17
    • 33748218119 scopus 로고
    • 12 dependent methylmalonyl-CoA mutase reaction shown by ESR spectroscopy
    • 12 dependent methylmalonyl-CoA mutase reaction shown by ESR spectroscopy. Angew. Chem. Int. Ed. Engl. 31, 215-216.
    • (1992) Angew. Chem. Int. Ed. Engl. , vol.31 , pp. 215-216
    • Zhao, Y.1    Such, P.2    Rétey, J.3
  • 18
    • 0027488863 scopus 로고
    • The synthetic substrate succinyl(carbadethia)-Co A generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-Co a mutase
    • Keep N.H., Smith G.A., Evans M.C.W., Diakun G.P. and Leadlay P.F. (1993). The synthetic substrate succinyl(carbadethia)-Co A generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-Co A mutase. Biochem. J. 295, 387-392.
    • (1993) Biochem. J. , vol.295 , pp. 387-392
    • Keep, N.H.1    Smith, G.A.2    Evans, M.C.W.3    Diakun, G.P.4    Leadlay, P.F.5
  • 19
    • 0000549033 scopus 로고
    • ed. D. Dolphin, chap. 13, Wiley, New York
    • 12 ed. D. Dolphin, vol. 2, chap. 13, pp. 357-379. Wiley, New York.
    • (1982) 12 , vol.2 , pp. 357-379
    • Rétey, J.1
  • 21
    • 14844320887 scopus 로고    scopus 로고
    • The mechanistic and evolutionary basis of stereospecificity for hydrogen transfers in enzyme-catalysed processes
    • Reynolds K.A. and Holland K.A. (1997). The mechanistic and evolutionary basis of stereospecificity for hydrogen transfers in enzyme-catalysed processes. Chem. Soc. Rev. 26, 337-343.
    • (1997) Chem. Soc. Rev. , vol.26 , pp. 337-343
    • Reynolds, K.A.1    Holland, K.A.2
  • 22
    • 0023040108 scopus 로고
    • On the mechanism of action of methylmalonyl-Co A mutase. Change of the steric course on isotopic substitution
    • Wölfle K., Michenfelder M., König A., Hull W.E. and Rétey J. (1986). On the mechanism of action of methylmalonyl-Co A mutase. Change of the steric course on isotopic substitution. Eur. J. Biochem. 156, 545-554.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 545-554
    • Wölfle, K.1    Michenfelder, M.2    König, A.3    Hull, W.E.4    Rétey, J.5
  • 23
    • 0024674237 scopus 로고
    • Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-Co A mutase from Propionibacterium shermanii
    • Marsh E.N.G., McKie N., Davis N.K. and Leadlay P.F. (1989). Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-Co A mutase from Propionibacterium shermanii. Biochem. J. 260, 345-352.
    • (1989) Biochem. J. , vol.260 , pp. 345-352
    • Marsh, E.N.G.1    McKie, N.2    Davis, N.K.3    Leadlay, P.F.4
  • 24
    • 0028088469 scopus 로고
    • Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum
    • Holloway D.E. and Marsh E.N.G. (1994). Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. J. Biol. Chem. 269, 20425-20430.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20425-20430
    • Holloway, D.E.1    Marsh, E.N.G.2
  • 25
    • 0026776985 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli
    • Luchinsky C.L., Drummond J.T., Matthews R.G. and Ludwig M.L. (1992). Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli. J. Mol. Biol. 225, 557-560.
    • (1992) J. Mol. Biol. , vol.225 , pp. 557-560
    • Luchinsky, C.L.1    Drummond, J.T.2    Matthews, R.G.3    Ludwig, M.L.4
  • 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    Keller, W.2    Kratky, C.3
  • 30
    • 0025114388 scopus 로고
    • Evidence for a super-reduced cobamide as the major corrinoid fraction in vivo and a histidine residue as a cobalt ligand of the p-cresolyl cobamide in the acetogenic bacterium Sporomusa ovata
    • Stupperich E., Eisinger H.J. and Albracht S.P.J. (1990). Evidence for a super-reduced cobamide as the major corrinoid fraction in vivo and a histidine residue as a cobalt ligand of the p-cresolyl cobamide in the acetogenic bacterium Sporomusa ovata. Eur. J. Biochem. 193, 105-109.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 105-109
    • Stupperich, E.1    Eisinger, H.J.2    Albracht, S.P.J.3
  • 31
    • 0029846834 scopus 로고    scopus 로고
    • The corrinoid-containing 23-kDa subunit Mtra of the energy-conserving NT-methyltetrahydromethanopterin: Coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum EPR spectroscopic evidence for a histidine residue as a cobalt ligand of the cobamide
    • Harms U. and Thauer R.K. (1996). The corrinoid-containing 23-kDa subunit MtrA of the energy-conserving NT-methyltetrahydromethanopterin: coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum EPR spectroscopic evidence for a histidine residue as a cobalt ligand of the cobamide. Eur. J. Biochem. 241, 149-154.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 149-154
    • Harms, U.1    Thauer, R.K.2
  • 32
    • 0032079887 scopus 로고    scopus 로고
    • Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Identification of the active-site histidine in the corrinoid-harboring subunit MtaC by site-directed mutagenesis
    • Sauer K. and Thauer R.K. (1998). Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Identification of the active-site histidine in the corrinoid-harboring subunit MtaC by site-directed mutagenesis. Eur. J. Biochem. 253, 698-705.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 698-705
    • Sauer, K.1    Thauer, R.K.2
  • 34
    • 0029950708 scopus 로고    scopus 로고
    • Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: Deductions from the structure of methionine synthase
    • Drennan C.L., Matthews R.G., Rosenblatt D.S., Ledley F.D., Fenton W.A. and Ludwig M.L. (1996). Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: deductions from the structure of methionine synthase. Proc. Natl. Acad. Sci. USA 93, 5550-5555.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5550-5555
    • Drennan, C.L.1    Matthews, R.G.2    Rosenblatt, D.S.3    Ledley, F.D.4    Fenton, W.A.5    Ludwig, M.L.6
  • 35
    • 0030048121 scopus 로고    scopus 로고
    • A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of Escherichia coli methionine synthase: Initial characterization of seven mutant proteins
    • Amaratunga M., Fluhr K., Jarrett J.T., Drennan C.E., Ludwig M.L., Matthews R.G. and Scholten J.D. (1996). A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of Escherichia coli methionine synthase: Initial characterization of seven mutant proteins. Biochemistry 35, 2453-2463.
    • (1996) Biochemistry , vol.35 , pp. 2453-2463
    • Amaratunga, M.1    Fluhr, K.2    Jarrett, J.T.3    Drennan, C.E.4    Ludwig, M.L.5    Matthews, R.G.6    Scholten, J.D.7
  • 37
    • 0026701740 scopus 로고
    • Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes
    • Marsh E.N.G. and 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
  • 38
    • 0028345427 scopus 로고
    • 12-dependent 2-methylene-glutarate mutase from Clostridium barkeri in Escherichia coli
    • 12-dependent 2-methylene-glutarate mutase from Clostridium barkeri in Escherichia coli. Eur. J. Biochem. 221, 101-109.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 101-109
    • Beatrix, B.1    Zelder, O.2    Linder, D.3    Buckel, W.4
  • 39
    • 0029828907 scopus 로고    scopus 로고
    • Carboxymethylation of mutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase
    • Holloway D.E., Chen H-P. and Marsh E.N.G. (1996). Carboxymethylation of mutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. J. Biol. Chem. 271, 29121-29125.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29121-29125
    • Holloway, D.E.1    Chen, H.-P.2    Marsh, E.N.G.3
  • 40
    • 0030800149 scopus 로고    scopus 로고
    • How enzymes control the reactivity of adenosylcobalamin: Effect on coenzyme binding and catalysis of mutations in the conserved histidine-aspartate pair of glutamate mutase
    • Chen H-P. and Marsh E.N.G. (1997). How enzymes control the reactivity of adenosylcobalamin: effect on coenzyme binding and catalysis of mutations in the conserved histidine-aspartate pair of glutamate mutase. Biochemistry 36, 7884-7889.
    • (1997) Biochemistry , vol.36 , pp. 7884-7889
    • Chen, H.-P.1    Marsh, E.N.G.2
  • 41
    • 0031574070 scopus 로고    scopus 로고
    • Identification of the active site histidine in the corrinoid protein MtrA of the energy-conserving methyltransferase complex from Methanobacterium thermoantotrophicum
    • Harms U. and Thauer R.K. (1997). Identification of the active site histidine in the corrinoid protein MtrA of the energy-conserving methyltransferase complex from Methanobacterium thermoantotrophicum. Eur. J. Biochem. 250, 783-788.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 783-788
    • Harms, U.1    Thauer, R.K.2
  • 42
    • 0023656557 scopus 로고
    • Mossbauer, EPR and optical studies of the corrinoid/iron-sulfur protein involved in the synthesis of acetyl coenzyme A by Clostridium thermoaceticum
    • Ragsdale S.W., Lindahl P.A. and Münck E. (1987). Mossbauer, EPR and optical studies of the corrinoid/iron-sulfur protein involved in the synthesis of acetyl coenzyme A by Clostridium thermoaceticum. J. Biol. Chem. 262, 14289-14297.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14289-14297
    • Ragsdale, S.W.1    Lindahl, P.A.2    Münck, E.3
  • 43
    • 0030899596 scopus 로고    scopus 로고
    • 12-dependent glycerol dehydratase and diol dehydratase
    • 12-dependent glycerol dehydratase and diol dehydratase. Eur. J. Biochem. 245, 398-401.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 398-401
    • Poppe, L.1    Rétey, J.2
  • 44
    • 0031466511 scopus 로고    scopus 로고
    • 1H-NMR structure analysis and kinetic studies with (R)-methylmalonyl-CoA mutase, glycerol dehydratase and diol dehydratase
    • 1H-NMR structure analysis and kinetic studies with (R)-methylmalonyl-CoA mutase, glycerol dehydratase and diol dehydratase. Eur. J. Biochem. 250, 303-307.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 303-307
    • Poppe, E.1    Stupperich, E.2    Hull, W.E.3    Buckel, T.4    Rétey, J.5
  • 46
    • 0031471024 scopus 로고    scopus 로고
    • Changes in protonation associated with substrate binding and cob(I)alamin formation in cobalamin-dependent methionine synthase
    • Jarrett J.T., Choi C.Y. and Matthews R.G. (1997). Changes in protonation associated with substrate binding and cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry 36, 15739-15748.
    • (1997) Biochemistry , vol.36 , pp. 15739-15748
    • Jarrett, J.T.1    Choi, C.Y.2    Matthews, R.G.3
  • 47
    • 2742589922 scopus 로고
    • Thermolysis of the Co-C bond in adenosylcorrins.3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon bond homolysis
    • Hay B.P. and Finke R.G. (1987). Thermolysis of the Co-C bond in adenosylcorrins.3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon bond homolysis. J. Am. Chem. Soc. 109, 8012-8018.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 8012-8018
    • Hay, B.P.1    Finke, R.G.2
  • 48
    • 0030896265 scopus 로고    scopus 로고
    • Evidence that cobalt-carbon bond homolysis is coupled to hydrogen atom abstraction from substrate in methylmalonyl-Co A mutase
    • Padmakumar R, Padmakumar R and Banerjee R. (1997). Evidence that cobalt-carbon bond homolysis is coupled to hydrogen atom abstraction from substrate in methylmalonyl-Co A mutase. Biochemistry 36, 3713-3718.
    • (1997) Biochemistry , vol.36 , pp. 3713-3718
    • Padmakumar, R.1    Padmakumar, R.2    Banerjee, R.3
  • 49
    • 0020715576 scopus 로고
    • 12-dependent enzymatic reactions: How the protein exploits the organometallic chemistry of cobalt corrinoids
    • 12-dependent enzymatic reactions: how the protein exploits the organometallic chemistry of cobalt corrinoids. J. Mol. Catal. 23, 187-193.
    • (1984) J. Mol. Catal. , vol.23 , pp. 187-193
    • Pratt, J.M.1
  • 50
    • 37049104246 scopus 로고
    • 12-dependent isomerase enzymes; how the protein controls the active site
    • 12-dependent isomerase enzymes; how the protein controls the active site. Chem. Soc. Rev. 14, 161-170.
    • (1985) Chem. Soc. Rev. , vol.14 , pp. 161-170
    • Pratt, J.M.1


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