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Volumn 7, Issue 2, 1999, Pages 205-216

A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: Why urea hydrolysis costs two nickels

Author keywords

Bacillus pasteurii; Diamidophosphate; Phenylphosphorodiamidate; Urease; X ray structure

Indexed keywords

UREA; UREASE;

EID: 0033081891     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80026-4     Document Type: Article
Times cited : (445)

References (61)
  • 1
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • 1. Jabri, E., Carr, M.B., Hausinger, R.P. & Karplus, P.A. (1995). The crystal structure of urease from Klebsiella aerogenes. Science 268, 998-1004.
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 2
    • 0001849211 scopus 로고    scopus 로고
    • 70 Years of crystalline urease: What have we learned?
    • 2. Karplus, P.A., Pearson, M.A. & Hausinger, R.P. (1997). 70 years of crystalline urease: what have we learned? Acc. Chem. Res. 30, 330-337.
    • (1997) Acc. Chem. Res. , vol.30 , pp. 330-337
    • Karplus, P.A.1    Pearson, M.A.2    Hausinger, R.P.3
  • 3
    • 0001346276 scopus 로고
    • Structure of the dinuclear active site of urease. X-ray absorption spectroscopic study of native and 2-mercaptoethanol-inhibited bacterial and plant enzymes
    • 3. Wang, S., Lee, M.H., Hausinger, R.P., Clark, P.A., Wilcox, D.E. & Scott, R.A. (1994). Structure of the dinuclear active site of urease. X-ray absorption spectroscopic study of native and 2-mercaptoethanol-inhibited bacterial and plant enzymes. Inorg. Chem. 33, 1589-1593.
    • (1994) Inorg. Chem. , vol.33 , pp. 1589-1593
    • Wang, S.1    Lee, M.H.2    Hausinger, R.P.3    Clark, P.A.4    Wilcox, D.E.5    Scott, R.A.6
  • 4
    • 0001215177 scopus 로고
    • Jack bean urease. VII. Light scattering and nickel(II) spectrum. Thiolate-nickel(II) charge transfer peaks in the spectrum of the β-mercaptoethanol-urease complex
    • 4. Biakeley, R.L., Dixon, N.E. & Zerner, B. (1983). Jack bean urease. VII. Light scattering and nickel(II) spectrum. Thiolate-nickel(II) charge transfer peaks in the spectrum of the β-mercaptoethanol-urease complex. Biochim. Biophys. Acta 744, 219-229.
    • (1983) Biochim. Biophys. Acta , vol.744 , pp. 219-229
    • Biakeley, R.L.1    Dixon, N.E.2    Zerner, B.3
  • 5
    • 0021103904 scopus 로고
    • An EXAFS study of jack bean urease, a nickel metalloenzyme
    • 5. Hasnain, S.S. & Piggot, B. (1983). An EXAFS study of jack bean urease, a nickel metalloenzyme. Biochem. Biophys. Res. Commun. 112, 279-283.
    • (1983) Biochem. Biophys. Res. Commun. , vol.112 , pp. 279-283
    • Hasnain, S.S.1    Piggot, B.2
  • 7
    • 0001028488 scopus 로고
    • Magnetic properties of the nickel enzyme urease, nickel-substituted carboxypeptidase A, and nickel-substituted carbonic anhydrase
    • 7. Clark, P.A. & Wilcox, D.E. (1989). Magnetic properties of the nickel enzyme urease, nickel-substituted carboxypeptidase A, and nickel-substituted carbonic anhydrase. Inorg. Chem. 28, 1326-1333.
    • (1989) Inorg. Chem. , vol.28 , pp. 1326-1333
    • Clark, P.A.1    Wilcox, D.E.2
  • 8
    • 0039246590 scopus 로고
    • X-ray absorption spectroscopic evidence for binding of the competitive inhibitor 2-mercaptoethanol to the nickel sites of jack bean urease. A new Ni-Ni interaction in the inhibited enzyme
    • 8. Clark, P.A., Wilcox, D.E. & Scott, R.A. (1990). X-ray absorption spectroscopic evidence for binding of the competitive inhibitor 2-mercaptoethanol to the nickel sites of jack bean urease. A new Ni-Ni interaction in the inhibited enzyme. Inorg. Chem. 29, 579-581.
    • (1990) Inorg. Chem. , vol.29 , pp. 579-581
    • Clark, P.A.1    Wilcox, D.E.2    Scott, R.A.3
  • 9
    • 0000202838 scopus 로고
    • Variable temperature magnetic circular dichroism spectroscopy as a probe of the electronic and magnetic properties of nickel in jack bean urease
    • 9. Finnegan, M.G., Kowal, A.T., Werth, M.T., Clark, P.A., Wilcox, D.E. & Johnson, M.K. (1991). Variable temperature magnetic circular dichroism spectroscopy as a probe of the electronic and magnetic properties of nickel in jack bean urease. J. Am. Chem. Soc. 113, 4030-4032.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4030-4032
    • Finnegan, M.G.1    Kowal, A.T.2    Werth, M.T.3    Clark, P.A.4    Wilcox, D.E.5    Johnson, M.K.6
  • 10
    • 0029984803 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy study of native and phenylphosphorodiamidate-inhibited Bacillus pasteurii urease
    • 10. Benini, S., Ciurli, S., Nolting, H.F. & Mangani, S. (1996). X-ray absorption spectroscopy study of native and phenylphosphorodiamidate-inhibited Bacillus pasteurii urease. Eur. J. Biochem. 239, 61-66.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 61-66
    • Benini, S.1    Ciurli, S.2    Nolting, H.F.3    Mangani, S.4
  • 11
    • 0026023106 scopus 로고
    • Recent advances in the chemistry of an old enzyme, urease
    • 11. Zerner, B. (1991). Recent advances in the chemistry of an old enzyme, urease. Bioorg. Chem. 19, 116-131.
    • (1991) Bioorg. Chem. , vol.19 , pp. 116-131
    • Zerner, B.1
  • 12
    • 0030848288 scopus 로고    scopus 로고
    • Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease
    • 12. Pearson, M.A., Overbye Michel, L., Hausinger, R.P. & Karplus, P.A. (1997). Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease. Biochemistry 36, 8164-8172.
    • (1997) Biochemistry , vol.36 , pp. 8164-8172
    • Pearson, M.A.1    Overbye Michel, L.2    Hausinger, R.P.3    Karplus, P.A.4
  • 13
    • 0030160824 scopus 로고    scopus 로고
    • Bacillus pasteurii urease: An heteropolymeric enzyme with a binuclear nickel active site
    • 13. Benini, S., Cessa, C. & Ciurli, S. (1996). Bacillus pasteurii urease: an heteropolymeric enzyme with a binuclear nickel active site. Soil Biol. Biochem. 28, 819-821.
    • (1996) Soil Biol. Biochem. , vol.28 , pp. 819-821
    • Benini, S.1    Cessa, C.2    Ciurli, S.3
  • 14
    • 0032078093 scopus 로고    scopus 로고
    • Crystallization and preliminary high resolution X-ray diffraction analysis of native and β-mercaptoethanol-inhibited urease from Bacillus pasteurii
    • 14. Benini, S., Ciurli, S., Rypniewski, W., Wilson, K.S. & Mangani, S. (1998). Crystallization and preliminary high resolution X-ray diffraction analysis of native and β-mercaptoethanol-inhibited urease from Bacillus pasteurii. Acta Crystallogr. D 54, 409-412.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 409-412
    • Benini, S.1    Ciurli, S.2    Rypniewski, W.3    Wilson, K.S.4    Mangani, S.5
  • 16
    • 0025106239 scopus 로고
    • Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation
    • 16. Mulrooney, S.B. & Hausinger, R.P. (1990). Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation. J. Bacteriol. 172, 5837-5843.
    • (1990) J. Bacteriol. , vol.172 , pp. 5837-5843
    • Mulrooney, S.B.1    Hausinger, R.P.2
  • 17
    • 0031808511 scopus 로고    scopus 로고
    • The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65 Å resolution
    • 17. Benini, S., Rypniewski, W.R., Wilson, K.S., Ciurli, S. & Mangani, S. (1998). The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65 Å resolution. J. Biol. Inorg. Chem. 3, 268-273.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 268-273
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Ciurli, S.4    Mangani, S.5
  • 18
    • 0016800324 scopus 로고
    • Inhibition of jack bean urease (EC 3.5.1.5) by acetoxydroxamic acid and by phosphoramidate. An equivalent weight for urease
    • 18. Dixon, N.E., Gazzola, C., Watters, J.J., Biakeley, R. & Zerner, B. (1975). Inhibition of jack bean urease (EC 3.5.1.5) by acetoxydroxamic acid and by phosphoramidate. An equivalent weight for urease. J. Am. Chem. Soc. 97, 4130-4131.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4130-4131
    • Dixon, N.E.1    Gazzola, C.2    Watters, J.J.3    Biakeley, R.4    Zerner, B.5
  • 19
    • 0019021670 scopus 로고
    • Jack bean urease (E.C. 3.5.1.5). III. The involvement of active-site nickel ion in inhibition by β-mercaptoethanol, phosphoramidate, and fluoride
    • 19. Dixon, N.B., Blakeley, R.L. & Zerner, B. (1980). Jack bean urease (E.C. 3.5.1.5). III. The involvement of active-site nickel ion in inhibition by β-mercaptoethanol, phosphoramidate, and fluoride. Can. J. Biochem. 58, 481-488.
    • (1980) Can. J. Biochem. , vol.58 , pp. 481-488
    • Dixon, N.B.1    Blakeley, R.L.2    Zerner, B.3
  • 20
    • 0024459370 scopus 로고
    • Competitive inhibitors of Klebsiella aerogenes urease. Mechanisms of interaction with the nickel active site
    • 20. Todd, M.J. & Hausinger, R.P. (1989). Competitive inhibitors of Klebsiella aerogenes urease. Mechanisms of interaction with the nickel active site. J. Biol. Chem. 264, 15835-15842.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15835-15842
    • Todd, M.J.1    Hausinger, R.P.2
  • 21
    • 0000030722 scopus 로고
    • Inhibition of plant and microbial ureases by phosphoramides
    • 21. McCarthy, G.W., Bremner, J.M. & Lee, J.S. (1990). Inhibition of plant and microbial ureases by phosphoramides. Plant Soil 127, 269-283.
    • (1990) Plant Soil , vol.127 , pp. 269-283
    • McCarthy, G.W.1    Bremner, J.M.2    Lee, J.S.3
  • 23
    • 0001835759 scopus 로고
    • 3D search and research using the Cambridge Structural Database
    • 23. Allen, F.H. & Kennard, O. (1993). 3D search and research using the Cambridge Structural Database. Chemical Design Automation News 8, 31-37.
    • (1993) Chemical Design Automation News , vol.8 , pp. 31-37
    • Allen, F.H.1    Kennard, O.2
  • 24
  • 25
    • 0030162098 scopus 로고    scopus 로고
    • Urease from the soil bacterium Bacillus pasteurii. 2. Immobilization on Ca-polygalacturonate
    • 25. Ciurli, S., Marzadori, C., Benini, S., Deiana, S. & Gessa, C. (1996). Urease from the soil bacterium Bacillus pasteurii. 2. Immobilization on Ca-polygalacturonate. Soil Biol. & Biochem. 28, 811-817.
    • (1996) Soil Biol. & Biochem. , vol.28 , pp. 811-817
    • Ciurli, S.1    Marzadori, C.2    Benini, S.3    Deiana, S.4    Gessa, C.5
  • 26
    • 0001142044 scopus 로고
    • Saturation magnetization of ureases from Klebsiella aerogenes and jack bean: No evidence for exchange coupling between the two active site nickel ions in the native enzymes
    • 26. Day, E.P., Peterson, J., Sendova, M.S., Todd, M.J. & Hausinger, R.P. (1993). Saturation magnetization of ureases from Klebsiella aerogenes and jack bean: no evidence for exchange coupling between the two active site nickel ions in the native enzymes. Inorg. Chem. 32, 634-638.
    • (1993) Inorg. Chem. , vol.32 , pp. 634-638
    • Day, E.P.1    Peterson, J.2    Sendova, M.S.3    Todd, M.J.4    Hausinger, R.P.5
  • 27
    • 10144255859 scopus 로고    scopus 로고
    • Characterization of the mononickel metallocenter in H134A mutant urease
    • 27. Park, I.-S., et al., & Hausinger, R.P. (1996). Characterization of the mononickel metallocenter in H134A mutant urease. J. Biol. Chem. 271, 18632-18637.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18632-18637
    • Park, I.-S.1    Hausinger, R.P.2
  • 28
    • 0032574684 scopus 로고    scopus 로고
    • Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand
    • 28. Pearson, M.A., Schaller, R.A., Michel, L.O., Karplus, P.A. & Hausinger, R.P. (1998). Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand. Biochemistry 37, 6214-6220.
    • (1998) Biochemistry , vol.37 , pp. 6214-6220
    • Pearson, M.A.1    Schaller, R.A.2    Michel, L.O.3    Karplus, P.A.4    Hausinger, R.P.5
  • 29
    • 85040110459 scopus 로고
    • Metrical Aspects of Three-and Four-Center Hydrogen bonds
    • Springer-Verlag, Berlin
    • 29. Jeffrey, G.A. & Saenger, W. (1991). Metrical Aspects of Three-and Four-Center Hydrogen bonds In Hydrogen Bonding in Biological Structures, p. 18, Springer-Verlag, Berlin.
    • (1991) Hydrogen Bonding in Biological Structures , pp. 18
    • Jeffrey, G.A.1    Saenger, W.2
  • 30
    • 0001258570 scopus 로고
    • Jack bean urease (EC 3.5.1.5). VIII. On the inhibition of urease by amides and esters of phosphoric acid
    • 30. Andrews, R.K., Dexter, A., Blakeley, R.L. & Zerner, B. (1986). Jack bean urease (EC 3.5.1.5). VIII. On the inhibition of urease by amides and esters of phosphoric acid. J. Am. Chem. Soc. 108, 7124-7125.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7124-7125
    • Andrews, R.K.1    Dexter, A.2    Blakeley, R.L.3    Zerner, B.4
  • 31
    • 0019268851 scopus 로고
    • Jack bean urease. V. On the mechanism of action of urease on urea, formamide, acetamide, N-methylurea, and related compounds
    • 31. Dixon, N.E., Riddles, P.W., Gazzola, C., Blakeley, R.L. & Zerner, B. (1980). Jack bean urease. V. On the mechanism of action of urease on urea, formamide, acetamide, N-methylurea, and related compounds. Can. J. Biochem. 58, 1335-1345.
    • (1980) Can. J. Biochem. , vol.58 , pp. 1335-1345
    • Dixon, N.E.1    Riddles, P.W.2    Gazzola, C.3    Blakeley, R.L.4    Zerner, B.5
  • 32
    • 0023644778 scopus 로고
    • Purification and characterization of the nickel-containing multicomponent urease from Klebsiella aerogenes
    • 32. Todd, M.J. & Hausinger, R.P. (1987). Purification and characterization of the nickel-containing multicomponent urease from Klebsiella aerogenes. J. Biol. Chem. 262, 5963-5967.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5963-5967
    • Todd, M.J.1    Hausinger, R.P.2
  • 33
    • 0024514293 scopus 로고
    • Microbial urease: Significance, regulation and molecular characterization
    • 33. Mobley, H.LT. & Hausinger, R.P. (1989). Microbial urease: significance, regulation and molecular characterization. Microbiol. Rev. 53, 85-108.
    • (1989) Microbiol. Rev. , vol.53 , pp. 85-108
    • Mobley, H.L.T.1    Hausinger, R.P.2
  • 34
    • 0027235376 scopus 로고
    • Site-directed mutagenesis of Klebsiella aerogenes urease: Identification of hystidine residues that appear to function in nickel ligation, substrate binding, and catalysis
    • 34. Park, I.-S. & Hausinger, R.P. (1993). Site-directed mutagenesis of Klebsiella aerogenes urease: identification of hystidine residues that appear to function in nickel ligation, substrate binding, and catalysis. Protein Sci. 2, 1034-1041.
    • (1993) Protein Sci. , vol.2 , pp. 1034-1041
    • Park, I.-S.1    Hausinger, R.P.2
  • 35
    • 0027509544 scopus 로고
    • Diethylpyrocarbonate reactivity of Klebsiella aerogenes urease: Effect of pH and active site ligands on the rate of inactivation
    • 35. Park, I.-S. & Hausinger, R.P. (1993). Diethylpyrocarbonate reactivity of Klebsiella aerogenes urease: effect of pH and active site ligands on the rate of inactivation. J. Protein Chem. 12, 51-56.
    • (1993) J. Protein Chem. , vol.12 , pp. 51-56
    • Park, I.-S.1    Hausinger, R.P.2
  • 37
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • 37. Holm, L. & Sander, C. (1997). An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 28, 72-82.
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 38
    • 0028173920 scopus 로고
    • A proposal for the catalytic mechanism in phospholipase C based on interaction energy and distance geometry calculations
    • 38. Sundell, S., Hansen, S. & Hough, E. (1994). A proposal for the catalytic mechanism in phospholipase C based on interaction energy and distance geometry calculations. Protein Eng. 7, 571-577.
    • (1994) Protein Eng. , vol.7 , pp. 571-577
    • Sundell, S.1    Hansen, S.2    Hough, E.3
  • 39
    • 0028889561 scopus 로고
    • Two-metal ion mechanism of bovine lens leucine aminopeptidase: Active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography
    • 39. Strater, N. & Lipscomb, W.N. (1995). Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography. Biochemistry 34, 14792-14800.
    • (1995) Biochemistry , vol.34 , pp. 14792-14800
    • Strater, N.1    Lipscomb, W.N.2
  • 40
    • 0029962708 scopus 로고    scopus 로고
    • Structure of a unique binuclear manganese cluster in arginase
    • 40. Kanyo, Z.F., Scolnick, L.R., Ash, D.E. & Christianson, D.W. (1996). Structure of a unique binuclear manganese cluster in arginase. Nature 283, 554-557.
    • (1996) Nature , vol.283 , pp. 554-557
    • Kanyo, Z.F.1    Scolnick, L.R.2    Ash, D.E.3    Christianson, D.W.4
  • 41
    • 0029941861 scopus 로고    scopus 로고
    • A site-directed mutagenesis study of Saccharomyces cerevisiae pyrophosphatase. Functional conservation of the active site of soluble inorganic pyrophosphatases
    • 41. Heikinheimo, P., et al., & Lahti, R. (1996). A site-directed mutagenesis study of Saccharomyces cerevisiae pyrophosphatase. Functional conservation of the active site of soluble inorganic pyrophosphatases. Eur. J. Biochem. 239, 138-143.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 138-143
    • Heikinheimo, P.1    Lahti, R.2
  • 42
    • 0029993512 scopus 로고    scopus 로고
    • Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate
    • 42. Vanhooke, J.L, Benning, M.M., Raushel, F.M. & Holden, H.M. (1996). Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate. Biochemistry 35, 6020-6025.
    • (1996) Biochemistry , vol.35 , pp. 6020-6025
    • Vanhooke, J.L.1    Benning, M.M.2    Raushel, F.M.3    Holden, H.M.4
  • 43
    • 0032584215 scopus 로고    scopus 로고
    • Structure and mechanism of a praline-specific aminopeptidase from Escherichia coli
    • 43. Wilce, M.C.J., ef al., & Wilce, J.A (1998). Structure and mechanism of a praline-specific aminopeptidase from Escherichia coli. Proc. Natl. Acad. Sci. USA 95, 3472-3477.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3472-3477
    • Wilce, M.C.J.1    Ef, A.2    Wilce, J.A.3
  • 44
    • 0029989358 scopus 로고    scopus 로고
    • X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin
    • 44. Wang, X., Randall, C.R, True, A.H. & Que, I.Jr. (1996). X-ray absorption spectroscopic studies of the FeZn derivative of uteroferrin. Biochemistry 35, 13946-13954.
    • (1996) Biochemistry , vol.35 , pp. 13946-13954
    • Wang, X.1    Randall, C.R.2    True, A.H.3    Que I., Jr.4
  • 45
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • 45. Wilcox, D.E. (1996). Binuclear metallohydrolases. Chem. Rev. 96, 2435-2458.
    • (1996) Chem. Rev. , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 46
    • 0016846997 scopus 로고
    • Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel?
    • 46. Dixon, N.E., Gazzola, C., Blakeley, R. & Zerner, B. (1975). Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel? J. Am. Chem. Soc. 97, 4131-4132.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4131-4132
    • Dixon, N.E.1    Gazzola, C.2    Blakeley, R.3    Zerner, B.4
  • 48
    • 0002935361 scopus 로고
    • Urease - A Ni(II) Metalloenzyme
    • (Lancaster, J.R., Jr., ed.), VCH Publishers, Inc., New York, NY 10010
    • 48. Andrews, R.K., Blakeley, R.L. & Zerner, B. (1989). Urease - A Ni(II) Metalloenzyme. In The Bioinorganic Chemistry of Nickel (Lancaster, J.R., Jr., ed.), pp. 141-166, VCH Publishers, Inc., New York, NY 10010.
    • (1989) The Bioinorganic Chemistry of Nickel , pp. 141-166
    • Andrews, R.K.1    Blakeley, R.L.2    Zerner, B.3
  • 50
    • 0029435465 scopus 로고
    • Recent research on problems in the use of urea as a nitrogen fertilizer
    • 50. Bremner, J.M. (1995). Recent research on problems in the use of urea as a nitrogen fertilizer. Fert. Res. 42, 321-329.
    • (1995) Fert. Res. , vol.42 , pp. 321-329
    • Bremner, J.M.1
  • 51
    • 0000862923 scopus 로고
    • Potential phytotoxicity associated with the use of soil urease inhibitors
    • 51. Krogmeier, M.J., McCarty, G.W. & Bremner, J.M. (1989). Potential phytotoxicity associated with the use of soil urease inhibitors. Proc. Natl Acad. Sci. USA 86, 1110-1112.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 1110-1112
    • Krogmeier, M.J.1    McCarty, G.W.2    Bremner, J.M.3
  • 52
    • 0018386226 scopus 로고
    • Rapid screening for urease inhibitors
    • 52. Hamilton-Miller, J.M.T. & Gargan, R.A. (1979). Rapid screening for urease inhibitors. Invest. Urol. 16, 327-328.
    • (1979) Invest. Urol. , vol.16 , pp. 327-328
    • Hamilton-Miller, J.M.T.1    Gargan, R.A.2
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • 53. Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. A 276, 307-325.
    • (1997) Methods Enzymol. A , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 54. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991 ). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 55
    • 0000071387 scopus 로고
    • A restrained-parameter structure-factor least-squares refinement procedure for large asymmetric units
    • 55. Konnert, J.H. (1976). A restrained-parameter structure-factor least-squares refinement procedure for large asymmetric units. Acta Crystallogr. A 32, 614-617.
    • (1976) Acta Crystallogr. A , vol.32 , pp. 614-617
    • Konnert, J.H.1
  • 56
    • 0001720577 scopus 로고
    • A restrained-parameter thermal-factor refinement procedure
    • 56. Konnert, J.H. & Hendrickson, W.A. (1980). A restrained-parameter thermal-factor refinement procedure. Acta Crystallogr. A 36, 344-350.
    • (1980) Acta Crystallogr. A , vol.36 , pp. 344-350
    • Konnert, J.H.1    Hendrickson, W.A.2
  • 57
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • 57. Murshudov, G.N., Vagin, A.A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D 53, 240-255.
    • (1997) Acta Cryst D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 58
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • 58. 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
  • 59
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • 59. Lamzin, V.S. & Wilson, K.S. (1997). Automated refinement for protein crystallography. Methods Enzymol. 277, 269-305.
    • (1997) Methods Enzymol. , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 60
    • 0025398721 scopus 로고
    • WHATIF: A molecular modelling and drug design program
    • 60. Vriend, G. (1990). WHATIF: a molecular modelling and drug design program. J. Molec. Graph. 8, 52-56.
    • (1990) J. Molec. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 61
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 61. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program 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


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