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Volumn 48, Issue 42, 2009, Pages 10098-10105

Structural basis of the hydride transfer mechanism in F420- dependent methylenetetrahydromethanopterin dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATALYTIC EFFICIENCIES; CONFORMATIONAL CHANGE; CURRENT RESOLUTION; FACE TO FACE; HYDRIDE TRANSFERS; PHENYL RINGS; PLANAR CONFORMATIONS; REVERSIBLE HYDRIDES; STRUCTURAL BASIS;

EID: 70350247728     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901104d     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture
    • Thauer, R. K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture. Microbiology 144 (Part 9), 2377-2406.
    • (1998) Microbiology , vol.144 , Issue.PART 9 , pp. 2377-2406
    • Thauer, R.K.1
  • 2
    • 0021382362 scopus 로고
    • Elucidation of the structure of methanopterin, a coenzyme from Methanobacterium thermoautotrophicum, using two-dimensional nuclear-magnetic- resonance techniques
    • van Beelen, P., Stassen, A. P., Bosch, J. W., Vogels, G. D., Guijt, W., and Haasnoot, C. A. (1984) Elucidation of the structure of methanopterin, a coenzyme from Methanobacterium thermoautotrophicum, using two-dimensional nuclear-magnetic-resonance techniques. Eur. J. Biochem. 138, 563-571.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 563-571
    • Van Beelen, P.1    Stassen, A.P.2    Bosch, J.W.3    Vogels, G.D.4    Guijt, W.5    Haasnoot, C.A.6
  • 4
    • 0022273052 scopus 로고
    • Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum
    • Hartzell, P. L., Zvilius, G., Escalante-Semerena, J. C., and Donnelly, M. I. (1985) Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 133, 884-890.
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 884-890
    • Hartzell, P.L.1    Zvilius, G.2    Escalante-Semerena, J.C.3    Donnelly, M.I.4
  • 5
    • 0041384391 scopus 로고    scopus 로고
    • Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: A methanogenic enzyme with an unusual quarternary structure
    • Hagemeier, C. H., Shima, S., Thauer, R. K., Bourenkov, G., Bartunik, H. D., and Ermler, U. (2003) Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary structure. J. Mol. Biol. 332, 1047-1057.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1047-1057
    • Hagemeier, C.H.1    Shima, S.2    Thauer, R.K.3    Bourenkov, G.4    Bartunik, H.D.5    Ermler, U.6
  • 7
    • 0036046380 scopus 로고    scopus 로고
    • Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1
    • DOI 10.1016/S0969-2126(02)00802-X, PII S096921260200802X
    • Ermler, U., Hagemeier, C. H., Roth, A., Demmer, U., Grabarse, W., Warkentin, E., and Vorholt, J. A. (2002) Structure of methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1. Structure 10, 1127-1137. (Pubitemid 34908037)
    • (2002) Structure , vol.10 , Issue.8 , pp. 1127-1137
    • Ermler, U.1    Hagemeier, C.H.2    Roth, A.3    Demmer, U.4    Grabarse, W.5    Warkentin, E.6    Vorholt, J.A.7
  • 8
    • 0035800892 scopus 로고    scopus 로고
    • Re-face stereospecificity of methylene-tetrahydromethanopterin and methylenetetrahydrofolate dehydrogenases is predetermined by intrinsic properties of the substrate
    • Bartoschek, S., Buurman, G., Thauer, R. K., Geierstanger, B. H., Weyrauch, J. P., Griesinger, C., Nilges, M., Hutter, M. C., and Helms, V. (2001) Re-face stereospecificity of methylenetetrahydromethan opterin and methylenetetrahydrofolate dehydrogenases is predetermined by intrinsic properties of the substrate. ChemBioChem 2, 530-541. (Pubitemid 33728999)
    • (2001) ChemBioChem , vol.2 , Issue.7-8 , pp. 530-541
    • Bartoschek, S.1    Buurman, G.2    Thauer, R.K.3    Geierstanger, B.H.4    Weyrauch, J.P.5    Griesinger, C.6    Nilges, M.7    Hutter, M.C.8    Helms, V.9
  • 9
    • 0032520234 scopus 로고    scopus 로고
    • The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 Å resolution
    • Allaire, M., Li, Y., MacKenzie, R. E., and Cygler, M. (1998) The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A ̊ resolution. Structure 6, 173-182. (Pubitemid 28153881)
    • (1998) Structure , vol.6 , Issue.2 , pp. 173-182
    • Allaire, M.1    Li, Y.2    MacKenzie, R.E.3    Cygler, M.4
  • 10
    • 0034664991 scopus 로고    scopus 로고
    • Tetrahydrofolate and tetrahydromethanopterin compared: Functionally distinct carriers in C1 metabolism
    • Maden, B. E. (2000) Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism. Biochem. J. 350 (Part 3), 609-629.
    • (2000) Biochem. J. , vol.350 , Issue.PART 3 , pp. 609-629
    • Maden, B.E.1
  • 12
    • 0027338277 scopus 로고
    • Two N5,N10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: Characterization of the coenzyme F420-dependent enzyme
    • Klein, A. R., Koch, J., Stetter, K. O., and Thauer, R. K. (1993) Two N5,N10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: characterization of the coenzyme F420-dependent enzyme. Arch. Microbiol. 160, 186-192.
    • (1993) Arch. Microbiol. , vol.160 , pp. 186-192
    • Klein, A.R.1    Koch, J.2    Stetter, K.O.3    Thauer, R.K.4
  • 13
    • 0024651916 scopus 로고
    • Aerobic purification of N5,N10-methylenetetrahydromethanopterin dehydrogenase, separated from N5,N10-methylenetetrahydromethanopterin cyclohydrolase, from Methanobacterium thermoautotrophicum strain Marburg
    • Mukhopadhyay, B., and Daniels, L. (1989) Aerobic purification of N5,N10-methylenetetrahydromethanopterin dehydrogenase, separated from N5,N10-methylenetetrahydromethanopterin cyclohydrolase, from Methanobacterium thermoautotrophicum strain Marburg. Can. J. Microbiol. 35, 499-507.
    • (1989) Can. J. Microbiol. , vol.35 , pp. 499-507
    • Mukhopadhyay, B.1    Daniels, L.2
  • 14
    • 0025740617 scopus 로고
    • Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri
    • Te Brommelstroet, B. W., Geerts, W. J., Keltjens, J. T., van der Drift, C., and Vogels, G. D. (1991) Purification and properties of 5,10- methylenetetrahydromethanopterin dehydrogenase and 5,10- methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079, 293-302.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 293-302
    • Te Brommelstroet, B.W.1    Geerts, W.J.2    Keltjens, J.T.3    Van Der Drift, C.4    Vogels, G.D.5
  • 15
    • 0030610167 scopus 로고    scopus 로고
    • Overexpression of the coenzyme-F420-dependent N5,N10- methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri
    • Klein, A. R., and Thauer, R. K. (1997) Overexpression of the coenzyme-F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri. Eur. J. Biochem. 245, 386-391.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 386-391
    • Klein, A.R.1    Thauer, R.K.2
  • 16
    • 0024421234 scopus 로고
    • Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: Substrate crystal structures at 2 a ° resolution
    • Karplus, P. A., and Schulz, G. E. (1989) Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A ° resolution. J. Mol. Biol. 210, 163-180.
    • (1989) J. Mol. Biol. , vol.210 , pp. 163-180
    • Karplus, P.A.1    Schulz, G.E.2
  • 17
    • 23944498570 scopus 로고    scopus 로고
    • 4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a Spartan strategy for a ping-pong reaction
    • DOI 10.1021/bi050533q
    • Pejchal, R., Sargeant, R., and Ludwig, M. L. (2005) Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction. Biochemistry 44, 11447-11457. (Pubitemid 41209080)
    • (2005) Biochemistry , vol.44 , Issue.34 , pp. 11447-11457
    • Pejchal, R.1    Sargeant, R.2    Ludwig, M.L.3
  • 19
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M. R., and Kraut, J. (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36, 586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 20
    • 0043233418 scopus 로고    scopus 로고
    • Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri: The selenomethionine-labelled and non-labelled enzyme crystallized in two different forms
    • Hagemeier, C. H., Shima, S., Warkentin, E., Thauer, R. K., and Ermler, U. (2003) Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri: the selenomethionine-labelled and non-labelled enzyme crystallized in two different forms. Acta Crystallogr., Sect. D: Biol. Crystallogr. 59, 1653-1655.
    • (2003) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.59 , pp. 1653-1655
    • Hagemeier, C.H.1    Shima, S.2    Warkentin, E.3    Thauer, R.K.4    Ermler, U.5
  • 21
    • 0035087922 scopus 로고    scopus 로고
    • Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri
    • Shima, S., and Thauer, R. K. (2001) Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri. Methods Enzymol. 331, 317-353.
    • (2001) Methods Enzymol. , vol.331 , pp. 317-353
    • Shima, S.1    Thauer, R.K.2
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • W.
    • Otwinowski, Z. M., W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. 276, 10.
    • (1997) Macromol. Crystallogr. , vol.276 , pp. 10
    • Otwinowski, Z.M.1
  • 23
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 28
    • 0027169515 scopus 로고
    • Mainchain bond lengths and bond angles in protein structures
    • Laskowski, R. A., Moss, D. S., and Thornton, J. M. (1993) Mainchain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 29
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 30
    • 17144399884 scopus 로고    scopus 로고
    • How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1
    • Acharya, P., Goenrich, M., Hagemeier, C. H., Demmer, U., Vorholt, J. A., Thauer, R. K., and Ermler, U. (2005) How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1. J. Biol. Chem. 280, 13712-13719.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13712-13719
    • Acharya, P.1    Goenrich, M.2    Hagemeier, C.H.3    Demmer, U.4    Vorholt, J.A.5    Thauer, R.K.6    Ermler, U.7
  • 31
    • 0030991713 scopus 로고    scopus 로고
    • Use of strain in a stereospecific catalytic mechanism: Crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate
    • DOI 10.1021/bi962936j
    • Hyatt, D. C., Maley, F., and Montfort, W. R. (1997) Use of strain in a stereospecific catalytic mechanism: crystal structures of Escherichia coli thymidylate synthase bound to FdUMP and methylenetetrahydrofolate. Biochemistry 36, 4585-4594. (Pubitemid 27180307)
    • (1997) Biochemistry , vol.36 , Issue.15 , pp. 4585-4594
    • Hyatt, D.C.1    Maley, F.2    Montfort, W.R.3
  • 32
    • 0035967514 scopus 로고    scopus 로고
    • Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: Roles for aspartate 120 and glutamate 28
    • Trimmer, E. E., Ballou, D. P., Ludwig, M. L., and Matthews, R. G. (2001) Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry 40, 6216-6226.
    • (2001) Biochemistry , vol.40 , pp. 6216-6226
    • Trimmer, E.E.1    Ballou, D.P.2    Ludwig, M.L.3    Matthews, R.G.4
  • 33
    • 6044276851 scopus 로고    scopus 로고
    • 420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family
    • DOI 10.1016/j.str.2004.02.010, PII S0969212604000528
    • Aufhammer, S. W., Warkentin, E., Berk, H., Shima, S., Thauer, R. K., and Ermler, U. (2004) Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure 12, 361-370. (Pubitemid 38353057)
    • (2004) Structure , vol.12 , Issue.3 , pp. 361-370
    • Aufhammer, S.W.1    Warkentin, E.2    Berk, H.3    Shima, S.4    Thauer, R.K.5    Ermler, U.6
  • 34
    • 22244459552 scopus 로고    scopus 로고
    • 420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family
    • DOI 10.1110/ps.041289805
    • Aufhammer, S. W., Warkentin, E., Ermler, U., Hagemeier, C. H., Thauer, R. K., and Shima, S. (2005) Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family. Protein Sci. 14, 1840-1849. (Pubitemid 40994154)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1840-1849
    • Aufhammer, S.W.1    Warkentin, E.2    Ermler, U.3    Hagemeier, C.H.4    Thauer, R.K.5    Shima, S.6
  • 35
    • 0028815489 scopus 로고
    • Re-face specificity at C14a of methylenetetrahydromethanopterin and Si-face specificity at C5 of coenzyme F420 for coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea
    • Klein, A. R., and Thauer, R. K. (1995) Re-face specificity at C14a of methylenetetrahydromethanopterin and Si-face specificity at C5 of coenzyme F420 for coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea. Eur. J. Biochem. 227, 169-174.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 169-174
    • Klein, A.R.1    Thauer, R.K.2
  • 36
    • 34047242540 scopus 로고    scopus 로고
    • Tunneling and classical paths for proton transfer in an enzyme reaction dominated by tunneling: Oxidation of tryptamine by aromatic amine dehydrogenase
    • Masgrau, L., Ranaghan, K. E., Scrutton, N. S., Mulholland, A. J., and Sutcliffe, M. J. (2007) Tunneling and classical paths for proton transfer in an enzyme reaction dominated by tunneling: oxidation of tryptamine by aromatic amine dehydrogenase. J. Phys. Chem. B 111, 3032-3047.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 3032-3047
    • Masgrau, L.1    Ranaghan, K.E.2    Scrutton, N.S.3    Mulholland, A.J.4    Sutcliffe, M.J.5
  • 37
    • 33748601471 scopus 로고    scopus 로고
    • Tunneling and dynamics in enzymatic hydride transfer
    • Nagel, Z. D., and Klinman, J. P. (2006) Tunneling and dynamics in enzymatic hydride transfer. Chem. Rev. 106, 3095-3118.
    • (2006) Chem. Rev. , vol.106 , pp. 3095-3118
    • Nagel, Z.D.1    Klinman, J.P.2
  • 38
    • 0242330829 scopus 로고    scopus 로고
    • Measurement and ab initio calculation of CSA/dipole-dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase
    • Bartoschek, S., Buurman, G., Geierstanger, B. H., Lapham, J., and Griesinger, C. (2003) Measurement and ab initio calculation of CSA/dipole-dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase. J. Am. Chem. Soc. 125, 13308-13309.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13308-13309
    • Bartoschek, S.1    Buurman, G.2    Geierstanger, B.H.3    Lapham, J.4    Griesinger, C.5
  • 39
    • 50049107805 scopus 로고    scopus 로고
    • Catalytic cycle of human glutathione reductase near 1 Å resolution
    • Berkholz, D. S., Faber, H. R., Savvides, S. N., and Karplus, P. A. (2008) Catalytic cycle of human glutathione reductase near 1 Å resolution. J. Mol. Biol. 382, 371-384.
    • (2008) J. Mol. Biol. , vol.382 , pp. 371-384
    • Berkholz, D.S.1    Faber, H.R.2    Savvides, S.N.3    Karplus, P.A.4


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