메뉴 건너뛰기




Volumn 16, Issue 6, 2007, Pages 1146-1156

High-resolution structures of formate dehydrogenase from Candida boidinii

Author keywords

Crystal structure determination; Enzyme stability; Formate dehydrogenase; NADH regeneration; Protein surface engineering

Indexed keywords

BACTERIAL ENZYME; FORMATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 34249807630     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062741707     Document Type: Article
Times cited : (96)

References (28)
  • 2
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Cryst. D50: 760-763.
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Cryst. D50: 760-763.
  • 4
    • 33748580982 scopus 로고    scopus 로고
    • Inhibition of protein crystallization by evolutionary negative design
    • Doye, J.P., Louis, A.A., and Vendruscolo, M. 2004. Inhibition of protein crystallization by evolutionary negative design. Phys. Biol. 1: 9-13.
    • (2004) Phys. Biol , vol.1 , pp. 9-13
    • Doye, J.P.1    Louis, A.A.2    Vendruscolo, M.3
  • 5
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. 2004. Coot: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60: 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 6
    • 0037666071 scopus 로고    scopus 로고
    • Practical asymmetric enzymatic reduction through discovery of a dehydrogenase-compatible biphasic reaction media
    • Groger, H., Hummel, W., Buchholz, S., Drauz, K., Nguyen, T.V., Rollmann, C., Husken, H., and Abokitse, K. 2003. Practical asymmetric enzymatic reduction through discovery of a dehydrogenase-compatible biphasic reaction media. Org. Lett. 5: 173-176.
    • (2003) Org. Lett , vol.5 , pp. 173-176
    • Groger, H.1    Hummel, W.2    Buchholz, S.3    Drauz, K.4    Nguyen, T.V.5    Rollmann, C.6    Husken, H.7    Abokitse, K.8
  • 7
    • 0035104352 scopus 로고    scopus 로고
    • A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP
    • Gul-Karaguler, N., Sessions, R.B., Clarke, A.R., and Holbrook, J.J. 2001. A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP. Biotechnol. Lett. 23: 283-287.
    • (2001) Biotechnol. Lett , vol.23 , pp. 283-287
    • Gul-Karaguler, N.1    Sessions, R.B.2    Clarke, A.R.3    Holbrook, J.J.4
  • 8
    • 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
  • 9
    • 0033769472 scopus 로고    scopus 로고
    • + binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis
    • + binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis. Eur. J. Biochem. 267: 6657-6664.
    • (2000) Eur. J. Biochem , vol.267 , pp. 6657-6664
    • Labrou, N.E.1    Rigden, D.J.2    Clonis, Y.D.3
  • 11
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk, A.M. 1995. NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5: 775-783.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 12
  • 13
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding, R., Russell, R.B., Neduva, V., and Gibson, T.J. 2003b. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res. 31: 3701-3708.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 14
    • 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. D53: 240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 15
    • 84920325457 scopus 로고
    • A MoRe: An automated package for molecular replacement
    • Navaza, J. 1994. A MoRe: An automated package for molecular replacement. Acta Crystallogr. A 50: 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 16
    • 0347899397 scopus 로고    scopus 로고
    • Microbial/enzymatic synthesis of chiral pharmaceutical intermediates
    • Patel, R.N. 2003. Microbial/enzymatic synthesis of chiral pharmaceutical intermediates. Curr. Opin. Drug Discov. Devel. 6: 902-920.
    • (2003) Curr. Opin. Drug Discov. Devel , vol.6 , pp. 902-920
    • Patel, R.N.1
  • 17
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V.S. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6: 458-463.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 19
    • 0032578179 scopus 로고    scopus 로고
    • + and the implications for the catalytic mechanism of formate dehydrogenase
    • + and the implications for the catalytic mechanism of formate dehydrogenase. J. Am. Chem. Soc. 120: 7192-7200.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 7192-7200
    • Schiott, B.1    Zheng, Y.-J.2    Bruice, T.C.3
  • 21
    • 0036845955 scopus 로고    scopus 로고
    • Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae
    • Serov, A.E., Popova, A.S., Fedorchuk, V.V., and Tishkov, V.I. 2002. Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae. Biochem. J. 367: 841-847.
    • (2002) Biochem. J , vol.367 , pp. 841-847
    • Serov, A.E.1    Popova, A.S.2    Fedorchuk, V.V.3    Tishkov, V.I.4
  • 22
    • 11144247396 scopus 로고    scopus 로고
    • Catalytic mechanism and application of formate dehydrogenase
    • Tishkov, V.I. and Popov, V.O. 2004. Catalytic mechanism and application of formate dehydrogenase. Biochemistry (Mosc.) 69: 1252-1267.
    • (2004) Biochemistry (Mosc.) , vol.69 , pp. 1252-1267
    • Tishkov, V.I.1    Popov, V.O.2
  • 24
    • 33645409623 scopus 로고    scopus 로고
    • Protein engineering of formate dehydrogenase
    • Tishkov, V.I. and Popov, V.O. 2006. Protein engineering of formate dehydrogenase. Biomol. Eng. 23: 89-110.
    • (2006) Biomol. Eng , vol.23 , pp. 89-110
    • Tishkov, V.I.1    Popov, V.O.2
  • 25
    • 0022821997 scopus 로고
    • Reconstitution of a functional electron-transfer chain from purified formate dehydrogenase and fumarate reductase complexes
    • Unden, G. and Kroger, A. 1986. Reconstitution of a functional electron-transfer chain from purified formate dehydrogenase and fumarate reductase complexes. Methods Enzymol. 126: 387-399.
    • (1986) Methods Enzymol , vol.126 , pp. 387-399
    • Unden, G.1    Kroger, A.2
  • 26
    • 0042933788 scopus 로고    scopus 로고
    • Recent developments in pyridine nucleotide regeneration
    • van der Donk, W.A. and Zhao, H. 2003. Recent developments in pyridine nucleotide regeneration. Curr. Opin. Biotechnol. 14: 421-426.
    • (2003) Curr. Opin. Biotechnol , vol.14 , pp. 421-426
    • van der Donk, W.A.1    Zhao, H.2
  • 27
    • 0027177745 scopus 로고
    • Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase
    • Vinals, C., Depiereux, E., and Feytmans, E. 1993. Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase. Biochem. Biophys. Res. Commun. 192: 182-188.
    • (1993) Biochem. Biophys. Res. Commun , vol.192 , pp. 182-188
    • Vinals, C.1    Depiereux, E.2    Feytmans, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.