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Volumn 11, Issue 2, 2007, Pages 166-171

Zinc-promoted alkyl transfer: a new role for zinc

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; LIGAND; THIOL; WATER; ZINC;

EID: 34047158876     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2007.02.038     Document Type: Review
Times cited : (49)

References (54)
  • 1
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld D.S. Zinc coordination sphere in biochemical zinc sites. Biometals 14 (2001) 271-313
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 2
    • 0028898325 scopus 로고
    • Metal dependence of transcriptional switching in Escherichia coli Ada
    • Myers L.C., Jackow F., and Verdine G.L. Metal dependence of transcriptional switching in Escherichia coli Ada. J Biol Chem 270 (1995) 6664-6670
    • (1995) J Biol Chem , vol.270 , pp. 6664-6670
    • Myers, L.C.1    Jackow, F.2    Verdine, G.L.3
  • 3
    • 0028041809 scopus 로고
    • Methylation dependent functional switch mechanism newly found in the Escherichia coli Ada protein
    • Ohkubo T., Sakashita H., Sakuma T., Kainosho M., Sekiguchi M., and Morikawa K. Methylation dependent functional switch mechanism newly found in the Escherichia coli Ada protein. J Am Chem Soc 116 (1994) 6035-6036
    • (1994) J Am Chem Soc , vol.116 , pp. 6035-6036
    • Ohkubo, T.1    Sakashita, H.2    Sakuma, T.3    Kainosho, M.4    Sekiguchi, M.5    Morikawa, K.6
  • 4
    • 0027752816 scopus 로고
    • Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada
    • Myers L.C., Verdine G.L., and Wagner G. Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada. Biochemistry 32 (1993) 14089-14094
    • (1993) Biochemistry , vol.32 , pp. 14089-14094
    • Myers, L.C.1    Verdine, G.L.2    Wagner, G.3
  • 5
    • 0026634921 scopus 로고
    • Zinc-binding by the methylation signaling domain of the Escherichia coli Ada protein
    • Myers L.C., Terranova M.P., Nash H.M., Markus M.A., and Verdine G.L. Zinc-binding by the methylation signaling domain of the Escherichia coli Ada protein. Biochemistry 31 (1992) 4541-4547
    • (1992) Biochemistry , vol.31 , pp. 4541-4547
    • Myers, L.C.1    Terranova, M.P.2    Nash, H.M.3    Markus, M.A.4    Verdine, G.L.5
  • 6
    • 0029760593 scopus 로고    scopus 로고
    • Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme
    • Gonzalez J.C., Peariso K., PennerHahn J.E., and Matthews R.G. Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme. Biochemistry 35 (1996) 12228-12234
    • (1996) Biochemistry , vol.35 , pp. 12228-12234
    • Gonzalez, J.C.1    Peariso, K.2    PennerHahn, J.E.3    Matthews, R.G.4
  • 7
    • 0031470779 scopus 로고    scopus 로고
    • Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation
    • Goulding C.W., and Matthews R.G. Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry 36 (1997) 15749-15757
    • (1997) Biochemistry , vol.36 , pp. 15749-15757
    • Goulding, C.W.1    Matthews, R.G.2
  • 8
    • 0031017064 scopus 로고    scopus 로고
    • 2+-farnesyltransferase indicates metal coordination of the substrate thiolate
    • 2+-farnesyltransferase indicates metal coordination of the substrate thiolate. J Biol Chem 272 (1997) 20-23
    • (1997) J Biol Chem , vol.272 , pp. 20-23
    • Huang, C.C.1    Casey, P.J.2    Fierke, C.A.3
  • 9
    • 0032147170 scopus 로고    scopus 로고
    • Human betaine-homocysteine methyltransferase is a zinc metalloenzyme
    • Millian N.S., and Garrow T.A. Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys 356 (1998) 93-98
    • (1998) Arch Biochem Biophys , vol.356 , pp. 93-98
    • Millian, N.S.1    Garrow, T.A.2
  • 10
    • 0029744528 scopus 로고    scopus 로고
    • Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri - physicochemical characterization, cloning, sequence analysis, and heterologous gene expression
    • LeClerc G.M., and Grahame D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri - physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J Biol Chem 271 (1996) 18725-18731
    • (1996) J Biol Chem , vol.271 , pp. 18725-18731
    • LeClerc, G.M.1    Grahame, D.A.2
  • 11
    • 0030879503 scopus 로고    scopus 로고
    • Methanol:coenzyme M methyltransferase from Methanosarcina barkeri - zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction
    • Sauer K., and Thauer R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri - zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction. Eur J Biochem 249 (1997) 280-285
    • (1997) Eur J Biochem , vol.249 , pp. 280-285
    • Sauer, K.1    Thauer, R.K.2
  • 12
    • 0035830845 scopus 로고    scopus 로고
    • The MtsA subunit of the methylthiol: coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer
    • Tallant T.C., Paul L., and Krzycki J.A. The MtsA subunit of the methylthiol: coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer. J Biol Chem 276 (2001) 4485-4493
    • (2001) J Biol Chem , vol.276 , pp. 4485-4493
    • Tallant, T.C.1    Paul, L.2    Krzycki, J.A.3
  • 13
    • 0344823660 scopus 로고    scopus 로고
    • SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins
    • Okeley N.M., Paul M., Stasser J.P., Blackburn N., and van der Donk W.A. SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins. Biochemistry 42 (2003) 13613-13624
    • (2003) Biochemistry , vol.42 , pp. 13613-13624
    • Okeley, N.M.1    Paul, M.2    Stasser, J.P.3    Blackburn, N.4    van der Donk, W.A.5
  • 14
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • This article describes a novel Zn site that promotes several ring closure reactions required in nisin biosynthesis and that appears to be the first example of an alkyl-transfer site with a displaceable water.
    • Li B., Yu J.P.J., Brunzelle J.S., Moll G.N., van der Donk W.A., and Nair S.K. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science 311 (2006) 1464-1467. This article describes a novel Zn site that promotes several ring closure reactions required in nisin biosynthesis and that appears to be the first example of an alkyl-transfer site with a displaceable water.
    • (2006) Science , vol.311 , pp. 1464-1467
    • Li, B.1    Yu, J.P.J.2    Brunzelle, J.S.3    Moll, G.N.4    van der Donk, W.A.5    Nair, S.K.6
  • 15
    • 0031466229 scopus 로고    scopus 로고
    • Purification to homogeneity and reconstitution of the individual components of the epoxide carboxylase multiprotein enzyme complex from Xanthobacter strain Py2
    • Allen J.R., and Ensign S.A. Purification to homogeneity and reconstitution of the individual components of the epoxide carboxylase multiprotein enzyme complex from Xanthobacter strain Py2. J Biol Chem 272 (1997) 32121-32128
    • (1997) J Biol Chem , vol.272 , pp. 32121-32128
    • Allen, J.R.1    Ensign, S.A.2
  • 16
    • 27944438100 scopus 로고    scopus 로고
    • Function of domains of human O-6-alkylguanine-DNA alkyltransferase
    • Report on an unexpected guanine dealkylation reaction catalyzed by the Zn site (previously thought to have only a structural role). It suggests the possibility that this site could have a regulatory role similar to that found in Ada.
    • Fang Q., Kanugula S., and Pegg A.E. Function of domains of human O-6-alkylguanine-DNA alkyltransferase. Biochemistry 44 (2005) 15396-15405. Report on an unexpected guanine dealkylation reaction catalyzed by the Zn site (previously thought to have only a structural role). It suggests the possibility that this site could have a regulatory role similar to that found in Ada.
    • (2005) Biochemistry , vol.44 , pp. 15396-15405
    • Fang, Q.1    Kanugula, S.2    Pegg, A.E.3
  • 17
    • 0000816291 scopus 로고    scopus 로고
    • Alkyl transfer to metal thiolates: kinetics, active species identification, and relevance to the DNA methyl phosphotriester repair center of Escherichia coli Ada
    • Wilker J.J., and Lippard S.J. Alkyl transfer to metal thiolates: kinetics, active species identification, and relevance to the DNA methyl phosphotriester repair center of Escherichia coli Ada. Inorg Chem 36 (1997) 969-978
    • (1997) Inorg Chem , vol.36 , pp. 969-978
    • Wilker, J.J.1    Lippard, S.J.2
  • 18
    • 0001657218 scopus 로고
    • Modeling the DNA methylphosphotriester repair site in Escherichia coli Ada. Why zinc and 4 cysteines?
    • Wilker J.J., and Lippard S.J. Modeling the DNA methylphosphotriester repair site in Escherichia coli Ada. Why zinc and 4 cysteines?. J Am Chem Soc 117 (1995) 8682-8683
    • (1995) J Am Chem Soc , vol.117 , pp. 8682-8683
    • Wilker, J.J.1    Lippard, S.J.2
  • 20
    • 0023893331 scopus 로고
    • Functional domains and methyl acceptor sites of the Escherichia coli Ada protein
    • Sedgwick B., Robins P., Totty N., and Lindahl T. Functional domains and methyl acceptor sites of the Escherichia coli Ada protein. J Biol Chem 263 (1988) 4430-4433
    • (1988) J Biol Chem , vol.263 , pp. 4430-4433
    • Sedgwick, B.1    Robins, P.2    Totty, N.3    Lindahl, T.4
  • 21
    • 33644560000 scopus 로고    scopus 로고
    • The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein
    • Identification of Cys38 as the methyl acceptor by NMR and mass spectrometry; absence of H-bonds to Cys38.
    • Takinowaki H., Matsuda Y., Yoshida T., Kobayashi Y., and Ohkubo T. The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein. Protein Sci 15 (2006) 487-497. Identification of Cys38 as the methyl acceptor by NMR and mass spectrometry; absence of H-bonds to Cys38.
    • (2006) Protein Sci , vol.15 , pp. 487-497
    • Takinowaki, H.1    Matsuda, Y.2    Yoshida, T.3    Kobayashi, Y.4    Ohkubo, T.5
  • 22
    • 25844499232 scopus 로고    scopus 로고
    • A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli Ada
    • NMR and crystallographic structures of Ada, demonstrating that H bonding is important in directing reactivity to Cys38, and suggesting an electrostatic mechanism for controlling DNA affinity.
    • He C., Hus J.C., Sun L.J., Zhou P., Norman D.P.G., Dotsch V., Wei H., Gross J.D., Lane W.S., Wagner G., et al. A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli Ada. Mol Cell 20 (2005) 117-129. NMR and crystallographic structures of Ada, demonstrating that H bonding is important in directing reactivity to Cys38, and suggesting an electrostatic mechanism for controlling DNA affinity.
    • (2005) Mol Cell , vol.20 , pp. 117-129
    • He, C.1    Hus, J.C.2    Sun, L.J.3    Zhou, P.4    Norman, D.P.G.5    Dotsch, V.6    Wei, H.7    Gross, J.D.8    Lane, W.S.9    Wagner, G.10
  • 23
    • 0027440878 scopus 로고
    • Repair Of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile
    • Myers L.C., Terranova M.P., Ferentz A.E., Wagner G., and Verdine G.L. Repair Of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile. Science 261 (1993) 1164-1167
    • (1993) Science , vol.261 , pp. 1164-1167
    • Myers, L.C.1    Terranova, M.P.2    Ferentz, A.E.3    Wagner, G.4    Verdine, G.L.5
  • 24
    • 0035949452 scopus 로고    scopus 로고
    • Chemical communication across the zinc tetrathiolate cluster in Escherichia coli Ada, a metalloactivated DNA repair protein
    • Sun L.J., Yim C.K., and Verdine G.L. Chemical communication across the zinc tetrathiolate cluster in Escherichia coli Ada, a metalloactivated DNA repair protein. Biochemistry 40 (2001) 11596-11603
    • (2001) Biochemistry , vol.40 , pp. 11596-11603
    • Sun, L.J.1    Yim, C.K.2    Verdine, G.L.3
  • 25
    • 15944366485 scopus 로고    scopus 로고
    • H-bonding interactions and control of thiolate nucleophilicity and specificity in model complexes of zinc metalloproteins
    • Demonstration that a single NH ⋯ S hydrogen bond can confer regiospecificity in thiolate alkylation.
    • Smith J.N., Hoffman J.T., Shirin Z., and Carrano C.J. H-bonding interactions and control of thiolate nucleophilicity and specificity in model complexes of zinc metalloproteins. Inorg Chem 44 (2005) 2012-2017. Demonstration that a single NH ⋯ S hydrogen bond can confer regiospecificity in thiolate alkylation.
    • (2005) Inorg Chem , vol.44 , pp. 2012-2017
    • Smith, J.N.1    Hoffman, J.T.2    Shirin, Z.3    Carrano, C.J.4
  • 26
    • 26444526880 scopus 로고    scopus 로고
    • Intramolecular N-H ⋯ S hydrogen bonding in the zinc thiolate complex [Tm-Ph]ZnSCH2C(O)NHPh: a mechanistic investigation of thiolate alkylation as probed by kinetics studies and by kinetic isotope effects
    • Detailed mechanistic investigation of the reactivity of model complexes, including a thorough analysis of the limitations to the interpretation of kinetic isotope effects.
    • Morlok M.M., Janak K.E., Zhu G., Quarless D.A., and Parkin G. Intramolecular N-H ⋯ S hydrogen bonding in the zinc thiolate complex [Tm-Ph]ZnSCH2C(O)NHPh: a mechanistic investigation of thiolate alkylation as probed by kinetics studies and by kinetic isotope effects. J Am Chem Soc 127 (2005) 14039-14050. Detailed mechanistic investigation of the reactivity of model complexes, including a thorough analysis of the limitations to the interpretation of kinetic isotope effects.
    • (2005) J Am Chem Soc , vol.127 , pp. 14039-14050
    • Morlok, M.M.1    Janak, K.E.2    Zhu, G.3    Quarless, D.A.4    Parkin, G.5
  • 27
    • 33745384266 scopus 로고    scopus 로고
    • Thiolate exchange in [TMR]ZnSR′ complexes and relevance to the mechanisms of thiolate alkylation reactions involving zinc enzymes and proteins
    • NMR demonstration of facile thiolate exchange in a neutral complex of Zn with thiolate + a tripodal ligand.
    • Melnick J.G., Zhu G., Buccella D., and Parkin G. Thiolate exchange in [TMR]ZnSR′ complexes and relevance to the mechanisms of thiolate alkylation reactions involving zinc enzymes and proteins. J Inorg Biochem 100 (2006) 1147-1154. NMR demonstration of facile thiolate exchange in a neutral complex of Zn with thiolate + a tripodal ligand.
    • (2006) J Inorg Biochem , vol.100 , pp. 1147-1154
    • Melnick, J.G.1    Zhu, G.2    Buccella, D.3    Parkin, G.4
  • 28
    • 0037389593 scopus 로고    scopus 로고
    • Synthetic modeling of zinc thiolates: quantitative assessment of hydrogen bonding in modulating sulfur alkylation rates
    • Chiou S.J., Riordan C.G., and Rheingold A.L. Synthetic modeling of zinc thiolates: quantitative assessment of hydrogen bonding in modulating sulfur alkylation rates. Proc Natl Acad Sci USA 100 (2003) 3695-3700
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3695-3700
    • Chiou, S.J.1    Riordan, C.G.2    Rheingold, A.L.3
  • 29
    • 0032569165 scopus 로고    scopus 로고
    • Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: the role of zinc in the methylation of homocysteine
    • Peariso K., Goulding C.W., Huang S., Matthews R.G., and Penner-Hahn J.E. Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: the role of zinc in the methylation of homocysteine. J Am Chem Soc 120 (1998) 8410-8416
    • (1998) J Am Chem Soc , vol.120 , pp. 8410-8416
    • Peariso, K.1    Goulding, C.W.2    Huang, S.3    Matthews, R.G.4    Penner-Hahn, J.E.5
  • 30
    • 0033619734 scopus 로고    scopus 로고
    • Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli
    • Zhou Z.S., Peariso K., Penner-Hahn J.E., and Matthews R.G. Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli. Biochemistry 38 (1999) 15915-15926
    • (1999) Biochemistry , vol.38 , pp. 15915-15926
    • Zhou, Z.S.1    Peariso, K.2    Penner-Hahn, J.E.3    Matthews, R.G.4
  • 31
  • 33
    • 0034599723 scopus 로고    scopus 로고
    • Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding
    • Daniels D.S., Mol C.D., Arvai A.S., Kanugula S., Pegg A.E., and Tainer J.A. Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding. EMBO J 19 (2000) 1719-1730
    • (2000) EMBO J , vol.19 , pp. 1719-1730
    • Daniels, D.S.1    Mol, C.D.2    Arvai, A.S.3    Kanugula, S.4    Pegg, A.E.5    Tainer, J.A.6
  • 34
    • 25444451577 scopus 로고    scopus 로고
    • Evidence for a metal-thiolate intermediate in alkyl group transfer from epoxypropane to coenzyme M and cooperative metal. Ion binding in epoxyalkane: CoM transferase
    • 2+-substituted epoxide carboxylase.
    • 2+-substituted epoxide carboxylase.
    • (2005) Biochemistry , vol.44 , pp. 13151-13162
    • Boyd, J.M.1    Ensign, S.A.2
  • 35
    • 0035969951 scopus 로고    scopus 로고
    • Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy
    • Peariso K., Zhou Z.H.S., Smith A.E., Matthews R.G., and Penner-Hahn J.E. Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy. Biochemistry 40 (2001) 987-993
    • (2001) Biochemistry , vol.40 , pp. 987-993
    • Peariso, K.1    Zhou, Z.H.S.2    Smith, A.E.3    Matthews, R.G.4    Penner-Hahn, J.E.5
  • 36
    • 1942457281 scopus 로고    scopus 로고
    • Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding
    • Evidence that tyrosine is the displaceable ligand in BHMT.
    • Gonzalez B., Pajares M.A., Martinez-Ripoll M., Blundell T.L., and Sanz-Aparicio J. Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding. J Mol Biol 338 (2004) 771-782. Evidence that tyrosine is the displaceable ligand in BHMT.
    • (2004) J Mol Biol , vol.338 , pp. 771-782
    • Gonzalez, B.1    Pajares, M.A.2    Martinez-Ripoll, M.3    Blundell, T.L.4    Sanz-Aparicio, J.5
  • 38
    • 15744394930 scopus 로고    scopus 로고
    • Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication
    • Evidence that the displaceable ligand in MetE is an endogenous glutamate. The low pH form that was crystallized suggests that the Zn site inverts when substrate binds.
    • Pejchal R., and Ludwig M.L. Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication. PLoS Biol 3 (2005) 254-265. Evidence that the displaceable ligand in MetE is an endogenous glutamate. The low pH form that was crystallized suggests that the Zn site inverts when substrate binds.
    • (2005) PLoS Biol , vol.3 , pp. 254-265
    • Pejchal, R.1    Ludwig, M.L.2
  • 39
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 Å resolution
    • Park H.-W., Boduluri S.R., Moomaw J.F., Casey P.J., and Beese L.S. Crystal structure of protein farnesyltransferase at 2.25 Å resolution. Science 275 (1997) 1800-1804
    • (1997) Science , vol.275 , pp. 1800-1804
    • Park, H.-W.1    Boduluri, S.R.2    Moomaw, J.F.3    Casey, P.J.4    Beese, L.S.5
  • 41
    • 0035818587 scopus 로고    scopus 로고
    • The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics
    • Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., and Beese L.S. The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. Proc Natl Acad Sci USA 98 (2001) 12948-12953
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12948-12953
    • Long, S.B.1    Hancock, P.J.2    Kral, A.M.3    Hellinga, H.W.4    Beese, L.S.5
  • 42
    • 0032493317 scopus 로고    scopus 로고
    • Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
    • Long S.B., Casey P.J., and Beese L.S. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 37 (1998) 9612-9618
    • (1998) Biochemistry , vol.37 , pp. 9612-9618
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 43
    • 0037057707 scopus 로고    scopus 로고
    • Reaction path of protein farnesyltransferase at atomic resolution
    • Long S.B., Casey P.J., and Beese L.S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 419 (2002) 645-650
    • (2002) Nature , vol.419 , pp. 645-650
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 44
    • 0032474284 scopus 로고    scopus 로고
    • Protein farnesyltransferase: structure and implications for substrate binding
    • Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., and Birktoft J. Protein farnesyltransferase: structure and implications for substrate binding. Biochemistry 37 (1998) 7907-7912
    • (1998) Biochemistry , vol.37 , pp. 7907-7912
    • Dunten, P.1    Kammlott, U.2    Crowther, R.3    Weber, D.4    Palermo, R.5    Birktoft, J.6
  • 45
    • 0034651550 scopus 로고    scopus 로고
    • The basis for K-Ras4B binding specificity to protein farnesyl transferase revealed by 2 Å resolution ternary complex structures
    • Long S.B., Casey P.J., and Beese L.S. The basis for K-Ras4B binding specificity to protein farnesyl transferase revealed by 2 Å resolution ternary complex structures. Structure 8 (2000) 209-222
    • (2000) Structure , vol.8 , pp. 209-222
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 46
    • 12944324735 scopus 로고    scopus 로고
    • Unraveling the mechanism of the farnesyltransferase enzyme
    • Sousa S.F., Fernandes P.A., and Ramos M.J. Unraveling the mechanism of the farnesyltransferase enzyme. J Biol Inorg Chem 10 (2005) 3-10
    • (2005) J Biol Inorg Chem , vol.10 , pp. 3-10
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 47
    • 11244321501 scopus 로고    scopus 로고
    • Farnesyltransferase - new insights into the zinc-coordination sphere paradigm: evidence for a carboxylate-shift mechanism
    • Computational evidence that a bidentate carboxylate (via a carboxylate shift) rather than water is the displaceable ligand in FTase.
    • Sousa S.F., Fernandes P.A., and Ramos M.J. Farnesyltransferase - new insights into the zinc-coordination sphere paradigm: evidence for a carboxylate-shift mechanism. Biophys J 88 (2005) 483-494. Computational evidence that a bidentate carboxylate (via a carboxylate shift) rather than water is the displaceable ligand in FTase.
    • (2005) Biophys J , vol.88 , pp. 483-494
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 48
    • 0001107341 scopus 로고    scopus 로고
    • Methylation of tethered thiolates in [(bme-daco)Zn](2) and [(bme-daco)Cd](2) as a model of zinc sulfur-methylation proteins
    • Grapperhaus C.A., Tuntulani T., Reibenspies J.H., and Darensbourg M.Y. Methylation of tethered thiolates in [(bme-daco)Zn](2) and [(bme-daco)Cd](2) as a model of zinc sulfur-methylation proteins. Inorg Chem 37 (1998) 4052-4058
    • (1998) Inorg Chem , vol.37 , pp. 4052-4058
    • Grapperhaus, C.A.1    Tuntulani, T.2    Reibenspies, J.H.3    Darensbourg, M.Y.4
  • 49
    • 7244220083 scopus 로고    scopus 로고
    • Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate
    • Ferrer J.L., Ravanel S., Robert M., and Dumas R. Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate. J Biol Chem 279 (2004) 44235-44238
    • (2004) J Biol Chem , vol.279 , pp. 44235-44238
    • Ferrer, J.L.1    Ravanel, S.2    Robert, M.3    Dumas, R.4
  • 50
    • 0035914908 scopus 로고    scopus 로고
    • Functional modeling of cobalamine-independent methionine synthase with pyrazolylborate-zinc-thiolate complexes
    • Brand U., Rombach M., Seebacher J., and Vahrenkamp H. Functional modeling of cobalamine-independent methionine synthase with pyrazolylborate-zinc-thiolate complexes. Inorg Chem 40 (2001) 6151-6157
    • (2001) Inorg Chem , vol.40 , pp. 6151-6157
    • Brand, U.1    Rombach, M.2    Seebacher, J.3    Vahrenkamp, H.4
  • 51
    • 0742305898 scopus 로고    scopus 로고
    • (Neocuproin)zinc thiolates: attempts at modeling cobalamin-independent methionine synthase
    • Seebacher J., Ji M., and Vahrenkamp H. (Neocuproin)zinc thiolates: attempts at modeling cobalamin-independent methionine synthase. Eur J Inorg Chem 2 (2004) 409-417
    • (2004) Eur J Inorg Chem , vol.2 , pp. 409-417
    • Seebacher, J.1    Ji, M.2    Vahrenkamp, H.3
  • 52
    • 27444435879 scopus 로고    scopus 로고
    • Biomimetic thiolate alkylation with zinc pyrazolylbis(thioimidazolyl)borate complexes
    • 2)ZnSR complexes that mimic the behavior of MetE; demonstration that these follow second-order kinetics.
    • 2)ZnSR complexes that mimic the behavior of MetE; demonstration that these follow second-order kinetics.
    • (2005) Eur J Inorg Chem , vol.20 , pp. 4070-4077
    • Ibrahim, M.M.1    He, G.2    Seebacher, J.3    Benkmil, B.4    Vahrenkamp, H.5
  • 53
    • 0034646238 scopus 로고    scopus 로고
    • Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state
    • Huang C.C., Hightower K.E., and Fierke C.A. Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state. Biochemistry 39 (2000) 2593-2602
    • (2000) Biochemistry , vol.39 , pp. 2593-2602
    • Huang, C.C.1    Hightower, K.E.2    Fierke, C.A.3
  • 54
    • 0036239341 scopus 로고    scopus 로고
    • The role of zinc in the methylation of the coenzyme M thiol group in methanol: coenzyme M methyltransferase from Methanosarcina barkeri - new insights from X-ray absorption spectroscopy
    • Kruer M., Haumann M., Meyer-Klaucke W., Thauer R.K., and Dau H. The role of zinc in the methylation of the coenzyme M thiol group in methanol: coenzyme M methyltransferase from Methanosarcina barkeri - new insights from X-ray absorption spectroscopy. Eur J Biochem 269 (2002) 2117-2123
    • (2002) Eur J Biochem , vol.269 , pp. 2117-2123
    • Kruer, M.1    Haumann, M.2    Meyer-Klaucke, W.3    Thauer, R.K.4    Dau, H.5


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