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Volumn 7, Issue 9, 2007, Pages 901-908

Inhibition of the archaeal β-class (Cab) and γ-class (Cam) carbonic anhydrases

Author keywords

[No Author keywords available]

Indexed keywords

ACETAZOLAMIDE; ARCHAEAL PROTEIN; ARSENIC ACID DERIVATIVE; BENZENEBORONIC ACID; BICARBONATE; CARBON DIOXIDE; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE ALPHA; CARBONATE DEHYDRATASE BETA; CARBONATE DEHYDRATASE GAMMA; CARBONATE DEHYDRATASE INHIBITOR; CELECOXIB; COBALT; DORZOLAMIDE; ETHOXZOLAMIDE; HYDROGEN SULFIDE; METAL ION; METHAZOLAMIDE; SULFANILAMIDE; SULFONAMIDE; THIOCYANATE; TOPIRAMATE; UNCLASSIFIED DRUG; ZINC;

EID: 34249720676     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802607780636753     Document Type: Review
Times cited : (135)

References (57)
  • 1
    • 84908284616 scopus 로고
    • Carbonic anhydrase. Its preparation and properties
    • Meldrum, N.N. and Roughton, F.J.W. Carbonic anhydrase. Its preparation and properties. J. Physiol. 1933, 80, 113-141.
    • (1933) J. Physiol , vol.80 , pp. 113-141
    • Meldrum, N.N.1    Roughton, F.J.W.2
  • 2
    • 0029936927 scopus 로고    scopus 로고
    • Characterization of heterologously produced carbonic anhydrase from Methanosarcina thermophila
    • Alber, B.E.; Ferry, J.G. Characterization of heterologously produced carbonic anhydrase from Methanosarcina thermophila. J. Bacteriol. 1996, 178, 3270-3274.
    • (1996) J. Bacteriol , vol.178 , pp. 3270-3274
    • Alber, B.E.1    Ferry, J.G.2
  • 3
    • 0030891670 scopus 로고    scopus 로고
    • The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae
    • Chirica, L.; Elleby, B.; Jonsson, B.; Lindskog, S. The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae. Eur. J. Biochem. 1997, 244, 755-760.
    • (1997) Eur. J. Biochem , vol.244 , pp. 755-760
    • Chirica, L.1    Elleby, B.2    Jonsson, B.3    Lindskog, S.4
  • 4
    • 0035059355 scopus 로고    scopus 로고
    • Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity
    • Cronk, J.D.; Cronk, M.R.; O'Neill, J.W.; Zhang, K.Y. Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity. Protein Sci. 2001, 5, 911-922.
    • (2001) Protein Sci , vol.5 , pp. 911-922
    • Cronk, J.D.1    Cronk, M.R.2    O'Neill, J.W.3    Zhang, K.Y.4
  • 6
    • 0001113609 scopus 로고
    • The catalytic mechanism of carbonic anhydrase
    • Lindskog, S.; Coleman, J.E. The catalytic mechanism of carbonic anhydrase. Proc. Natl. Acad. Sci. 1973, 70, 2505-2508.
    • (1973) Proc. Natl. Acad. Sci , vol.70 , pp. 2505-2508
    • Lindskog, S.1    Coleman, J.E.2
  • 7
    • 0030849266 scopus 로고    scopus 로고
    • Structure and mechanism of carbonic anhydrase
    • Lindskog, S. Structure and mechanism of carbonic anhydrase. Pharmacol. Ther. 1997, 74, 1-20.
    • (1997) Pharmacol. Ther , vol.74 , pp. 1-20
    • Lindskog, S.1
  • 8
    • 0033593062 scopus 로고    scopus 로고
    • Carbonic anhydrases is an ancient enzyme widespread in prokaryotes
    • Smith, K.; Jakubzick, C.; Whittam, T.S.; Ferry, J.G. Carbonic anhydrases is an ancient enzyme widespread in prokaryotes. Proc. Natl. Acad. Sci. 1999, 96, 15184-15189.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 15184-15189
    • Smith, K.1    Jakubzick, C.2    Whittam, T.S.3    Ferry, J.G.4
  • 9
    • 0034599484 scopus 로고    scopus 로고
    • Kimber, M.; Pai, E.F. The active site architecture of Pisum sativum β-carbonic anhydrase is a mirror image of that of α-carbonic anhydrases. EMBO J. 2000, 19, 14-17-1418.
    • Kimber, M.; Pai, E.F. The active site architecture of Pisum sativum β-carbonic anhydrase is a mirror image of that of α-carbonic anhydrases. EMBO J. 2000, 19, 14-17-1418.
  • 10
    • 0029874435 scopus 로고    scopus 로고
    • A left-handed beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
    • Kisker, C.; Schindelin, H.; Alber, B.E.; Ferry, J.G.; Rees, D.C. A left-handed beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 1996, 15, 2323-2330.
    • (1996) EMBO J , vol.15 , pp. 2323-2330
    • Kisker, C.1    Schindelin, H.2    Alber, B.E.3    Ferry, J.G.4    Rees, D.C.5
  • 14
    • 33646365079 scopus 로고    scopus 로고
    • The Structure of β-carbonic anhydrase from the carboxylsomal shell reveals a distinct subclass with one active site for the price of two
    • Sawaya, M.; Cannon, G.C.; Heinhorst, S.; Tanaka, S.; Williams, E.B.; Yeates, T.O.; Kerfeld, C.A. The Structure of β-carbonic anhydrase from the carboxylsomal shell reveals a distinct subclass with one active site for the price of two. J. Biol. Chem. 2006, 281, 7546-7555.
    • (2006) J. Biol. Chem , vol.281 , pp. 7546-7555
    • Sawaya, M.1    Cannon, G.C.2    Heinhorst, S.3    Tanaka, S.4    Williams, E.B.5    Yeates, T.O.6    Kerfeld, C.A.7
  • 15
    • 0035971165 scopus 로고    scopus 로고
    • Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum
    • Strop, P.S.K.; Iverson, T.M.; Ferry, J.G.; Rees, D.C. Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum. J. Biol. Chem. 2001, 27 6, 10299-10305.
    • (2001) J. Biol. Chem , vol.27 , Issue.6 , pp. 10299-10305
    • Strop, P.S.K.1    Iverson, T.M.2    Ferry, J.G.3    Rees, D.C.4
  • 16
    • 0027317583 scopus 로고
    • Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen bond network in human carbonic anhydrase II
    • Xue, Y.F.; Liljas, A.; Jonsson, B.H.; Lindskog, S. Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen bond network in human carbonic anhydrase II. Proteins 1993, 17, 93-106
    • (1993) Proteins , vol.17 , pp. 93-106
    • Xue, Y.F.1    Liljas, A.2    Jonsson, B.H.3    Lindskog, S.4
  • 17
    • 1642500161 scopus 로고    scopus 로고
    • A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell
    • So, A.K.C.; Espie, G.S.; Williams, E.B.; Shively, J.M.; Heinhorst, S.; Cannon, G.C. A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell. J. Bacteriol. 2004, 186, 623-630.
    • (2004) J. Bacteriol , vol.186 , pp. 623-630
    • So, A.K.C.1    Espie, G.S.2    Williams, E.B.3    Shively, J.M.4    Heinhorst, S.5    Cannon, G.C.6
  • 19
    • 0028234521 scopus 로고
    • A carbonic anhydrase from the archaeon Methanosarcina thermophila
    • Alber, B.E.; Ferry, J.G. A carbonic anhydrase from the archaeon Methanosarcina thermophila. Proc. Natl. Acad. Sci. 1994, 91, 6909-6913.
    • (1994) Proc. Natl. Acad. Sci , vol.91 , pp. 6909-6913
    • Alber, B.E.1    Ferry, J.G.2
  • 21
    • 0034622565 scopus 로고    scopus 로고
    • A structure-function study of a proton transport pathway in the gamma class carbonic anhydrase from Methanosarcina thermophila
    • Tripp, B.C.; Ferry, J.G. A structure-function study of a proton transport pathway in the gamma class carbonic anhydrase from Methanosarcina thermophila. Biochemistry 2000, 39, 9232-9240.
    • (2000) Biochemistry , vol.39 , pp. 9232-9240
    • Tripp, B.C.1    Ferry, J.G.2
  • 22
    • 33646009983 scopus 로고    scopus 로고
    • Proposal for a hydrogen bond network in the active site of the prototypic gamma-class carbonic anhydrase
    • Zimmerman, S.; Ferry, J.G. Proposal for a hydrogen bond network in the active site of the prototypic gamma-class carbonic anhydrase. Biochemistry 2006, 45, 5149-5157.
    • (2006) Biochemistry , vol.45 , pp. 5149-5157
    • Zimmerman, S.1    Ferry, J.G.2
  • 24
    • 18544380806 scopus 로고    scopus 로고
    • Lane, T.S.; MA, George, G.N.; Pickering, I.J.; Prince, R.C.; Morel, F.M.M. Biochemistry, A cadmium enzyme from a marine diatom. Nature 2005, 435, 42.
    • Lane, T.S.; MA, George, G.N.; Pickering, I.J.; Prince, R.C.; Morel, F.M.M. Biochemistry, A cadmium enzyme from a marine diatom. Nature 2005, 435, 42.
  • 25
    • 0034712970 scopus 로고    scopus 로고
    • A biological function for cadmium in marine diatoms
    • Lane, T.W.; Morel, F.M.M. A biological function for cadmium in marine diatoms. Proc. Natl. Acad. Sci. 2000, 97, 4627-4631.
    • (2000) Proc. Natl. Acad. Sci , vol.97 , pp. 4627-4631
    • Lane, T.W.1    Morel, F.M.M.2
  • 26
    • 0034112264 scopus 로고    scopus 로고
    • Regulation of carbonic anhydrase expression by zinc, cobalt, and carbon dioxide in the marine diatom Thalassiosira weissflogii
    • Lane, T.W.; Morel, F.M.M. Regulation of carbonic anhydrase expression by zinc, cobalt, and carbon dioxide in the marine diatom Thalassiosira weissflogii. Plant Physiol. 2000, 123, 345-352.
    • (2000) Plant Physiol , vol.123 , pp. 345-352
    • Lane, T.W.1    Morel, F.M.M.2
  • 28
    • 2442589472 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Inhibition of the zinc and cobalt γ-class enzyme from the archaeon Methanosarcina thermophila with anions
    • Innocenti, A.; Zimmerman, S.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T. Carbonic anhydrase inhibitors. Inhibition of the zinc and cobalt γ-class enzyme from the archaeon Methanosarcina thermophila with anions. Bioorg. Med. Chem. Lett. 2004, 14, 3327-3331.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 3327-3331
    • Innocenti, A.1    Zimmerman, S.2    Ferry, J.G.3    Scozzafava, A.4    Supuran, C.T.5
  • 29
    • 3843150633 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the methanoarchaeon Methanobacterium thermoautotrophicum (Cab) with anions
    • Innocenti, A.; Zimmerman, S.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T. Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the methanoarchaeon Methanobacterium thermoautotrophicum (Cab) with anions. Bioorg. Med. Chem. Lett. 2004, 14, 4563-4567.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 4563-4567
    • Innocenti, A.1    Zimmerman, S.2    Ferry, J.G.3    Scozzafava, A.4    Supuran, C.T.5
  • 30
    • 8844286179 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Inhibition of the prokaryotic beta and gamma-class from Archaea with sulfonamides
    • Zimmerman, S.; Innocenti, A.; Casini, A.; Ferry, J.G.; Scozzafava, A.; Supuran, C.T. Carbonic anhydrase inhibitors. Inhibition of the prokaryotic beta and gamma-class from Archaea with sulfonamides. Bioorg. Med. Chem. Lett. 2004, 14, 6001-6006.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 6001-6006
    • Zimmerman, S.1    Innocenti, A.2    Casini, A.3    Ferry, J.G.4    Scozzafava, A.5    Supuran, C.T.6
  • 32
    • 0036062304 scopus 로고    scopus 로고
    • Roles of the conserved aspartate and arginine in the catalytic mechanism of an archaeal beta-class carbonic anhydrase
    • Smith, K.S.; Ingram-Smith, C.; Ferry, J.G. Roles of the conserved aspartate and arginine in the catalytic mechanism of an archaeal beta-class carbonic anhydrase. J. Bacteriol. 2002, 184, 4240-4245.
    • (2002) J. Bacteriol , vol.184 , pp. 4240-4245
    • Smith, K.S.1    Ingram-Smith, C.2    Ferry, J.G.3
  • 33
    • 0034622579 scopus 로고    scopus 로고
    • A closer look at the active site of γ-class carbonic anhydrases, High-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
    • Iverson, T.M.; Alber, B.E.; Kisker, C.; Ferry, J.G.; Rees, D.C. A closer look at the active site of γ-class carbonic anhydrases, High-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 2000, 39, 9222-9231.
    • (2000) Biochemistry , vol.39 , pp. 9222-9231
    • Iverson, T.M.1    Alber, B.E.2    Kisker, C.3    Ferry, J.G.4    Rees, D.C.5
  • 34
    • 13444269025 scopus 로고    scopus 로고
    • Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II
    • Fisher, Z.; Hernandez Prada, J.A.; Tu, C.; Duda, D.; Yoshioka, C.; An, H.; Govindasamy, L.; Silverman, D.N.; McKenna, R. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry 2005, 44, 1097-1105.
    • (2005) Biochemistry , vol.44 , pp. 1097-1105
    • Fisher, Z.1    Hernandez Prada, J.A.2    Tu, C.3    Duda, D.4    Yoshioka, C.5    An, H.6    Govindasamy, L.7    Silverman, D.N.8    McKenna, R.9
  • 35
    • 0027131280 scopus 로고
    • Kinetic studies of pea carbonic anhydrase
    • Johansson, I.; Forsman, C. Kinetic studies of pea carbonic anhydrase. Eur. J. Biochem. 1993, 218, 439-446.
    • (1993) Eur. J. Biochem , vol.218 , pp. 439-446
    • Johansson, I.1    Forsman, C.2
  • 36
    • 0015239422 scopus 로고    scopus 로고
    • Khalifah, R.G. The carbon dioxide hydration activity of carbonic anhydrase I. Stop-flow kinetic studies on the native human isoenzymes B and C. J. Biol. Chem. 1971, 246, 2561-2573.
    • Khalifah, R.G. The carbon dioxide hydration activity of carbonic anhydrase I. Stop-flow kinetic studies on the native human isoenzymes B and C. J. Biol. Chem. 1971, 246, 2561-2573.
  • 38
    • 0027283352 scopus 로고
    • Kinetic and spectroscopic studies of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II
    • Krebs, J.F.R.F.; Dluhy, R.A.; Fierke, C.A. Kinetic and spectroscopic studies of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II. Biochemistry 1993, 32, 4496-4505.
    • (1993) Biochemistry , vol.32 , pp. 4496-4505
    • Krebs, J.F.R.F.1    Dluhy, R.A.2    Fierke, C.A.3
  • 39
    • 0027418070 scopus 로고
    • Importance of the conserved active site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II
    • Liang, Z.W.; Xue, Y.F.; Behravan, G.; Jonsson, B.H.; Lindskog, S. Importance of the conserved active site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II. Eur. J. Biochem. 1993, 211, 821-827.
    • (1993) Eur. J. Biochem , vol.211 , pp. 821-827
    • Liang, Z.W.1    Xue, Y.F.2    Behravan, G.3    Jonsson, B.H.4    Lindskog, S.5
  • 40
    • 0027139195 scopus 로고
    • Carbonic anhydrase and the role of orientation in catalysis
    • Lindskog, S.; Liljas, A. Carbonic anhydrase and the role of orientation in catalysis. Curr. Opin. Struct. Biol. 1993, 3, 915-920.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 915-920
    • Lindskog, S.1    Liljas, A.2
  • 41
    • 34249673169 scopus 로고
    • Kinetics and mechanism of cobalt substituted bovine muscle carbonic anhydrase
    • Ren, X.; Lindskog, S. Kinetics and mechanism of cobalt substituted bovine muscle carbonic anhydrase. Eur. J. Biochem. 1987, 106, 430-430.
    • (1987) Eur. J. Biochem , vol.106 , pp. 430-430
    • Ren, X.1    Lindskog, S.2
  • 44
    • 0020668933 scopus 로고
    • Proton transfer in the catalytic mechanism of carbonic anhydrase
    • Silverman, D.N.; Vincent, S.H. Proton transfer in the catalytic mechanism of carbonic anhydrase. CRC Crit. Rev. Biochem. 1984, 14, 207-255.
    • (1984) CRC Crit. Rev. Biochem , vol.14 , pp. 207-255
    • Silverman, D.N.1    Vincent, S.H.2
  • 45
    • 0034462876 scopus 로고    scopus 로고
    • Structural and kinetic characterization of an archaeal beta-class carbonic anhydrase
    • Smith, K.S.; Cosper, N.J.; Stalhandske, C.; Scott, R.A.; Ferry, J.G. Structural and kinetic characterization of an archaeal beta-class carbonic anhydrase. J. Bacteriol. 2000, 182, 6605-6613.
    • (2000) J. Bacteriol , vol.182 , pp. 6605-6613
    • Smith, K.S.1    Cosper, N.J.2    Stalhandske, C.3    Scott, R.A.4    Ferry, J.G.5
  • 47
    • 0027403496 scopus 로고
    • Crystallographic studies of azide binding to human carbonic anhydrase II
    • Nair, S.K.C.D. Crystallographic studies of azide binding to human carbonic anhydrase II. Eur. J. Biochem. 1993, 213, 507-515.
    • (1993) Eur. J. Biochem , vol.213 , pp. 507-515
    • Nair, S.K.C.D.1
  • 48
    • 33746972783 scopus 로고    scopus 로고
    • Proton transfer pathways in the mutant His-64-Ala of human carbonic anhydrase II
    • Roy, A.; Taraphder, S. Proton transfer pathways in the mutant His-64-Ala of human carbonic anhydrase II. Biopolymers 2006, 82(6), 623-30.
    • (2006) Biopolymers , vol.82 , Issue.6 , pp. 623-630
    • Roy, A.1    Taraphder, S.2
  • 49
    • 0347928862 scopus 로고    scopus 로고
    • Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class
    • Tu, C.K.; Rowlett, R.S.; Tripp, B.C.; Ferry, J.G.; Silverman, D.N. Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class. Biochemistry 2002, 41, 15429-15435.
    • (2002) Biochemistry , vol.41 , pp. 15429-15435
    • Tu, C.K.1    Rowlett, R.S.2    Tripp, B.C.3    Ferry, J.G.4    Silverman, D.N.5
  • 50
    • 0025026406 scopus 로고
    • Insights into the function of the zinc hydroxide-Thr199-Glu106 hydrogen bonding network in carbonic anhydrases
    • Merz, K.M. Insights into the function of the zinc hydroxide-Thr199-Glu106 hydrogen bonding network in carbonic anhydrases. J. Mol. Biol. 1990, 214, 799-802.
    • (1990) J. Mol. Biol , vol.214 , pp. 799-802
    • Merz, K.M.1
  • 51
    • 0027752970 scopus 로고
    • Structural and functional importance of a conserved hydrogen-bond network in human carbonic anhydrase II
    • Krebs, J.F.; Ippolito, J.A.; Christianson, D.W.; Fierke, C.A. Structural and functional importance of a conserved hydrogen-bond network in human carbonic anhydrase II. J. Biol. Chem. 1993, 268, 27458-27466.
    • (1993) J. Biol. Chem , vol.268 , pp. 27458-27466
    • Krebs, J.F.1    Ippolito, J.A.2    Christianson, D.W.3    Fierke, C.A.4
  • 53
    • 0032538339 scopus 로고    scopus 로고
    • Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetozolamide
    • Huan, S.; Xue, Y.; Suaer-Eriksson, E.; Chirica, L.; Lindskog, S.; Jonsson, B. Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetozolamide. J. Mol. Biol. 1998, 283, 301-310.
    • (1998) J. Mol. Biol , vol.283 , pp. 301-310
    • Huan, S.1    Xue, Y.2    Suaer-Eriksson, E.3    Chirica, L.4    Lindskog, S.5    Jonsson, B.6
  • 54
    • 0037103151 scopus 로고    scopus 로고
    • Nonaromatic sulfonamide group as an ideal anchor for potent human carbonic anhydrase inhibitors, role of hydrogen-bonding networks in ligand binding and drug design
    • Abbate, F.; Supuran, C.T.; Scozzafava, A.; Orioli, P.; Stubbs, M.T.; Klebe, G. Nonaromatic sulfonamide group as an ideal anchor for potent human carbonic anhydrase inhibitors, role of hydrogen-bonding networks in ligand binding and drug design. J. Med. Chem. 2002, 45, 3583-3587.
    • (2002) J. Med. Chem , vol.45 , pp. 3583-3587
    • Abbate, F.1    Supuran, C.T.2    Scozzafava, A.3    Orioli, P.4    Stubbs, M.T.5    Klebe, G.6
  • 55
    • 0028935889 scopus 로고
    • Structural basis of inhibitor affinity to variants of human carbonic anhydrase II
    • Nair, S.K.; Krebs, J.F.; Christianson, D.W.; Fierke, C.A. Structural basis of inhibitor affinity to variants of human carbonic anhydrase II. Biochemistry 1995, 34, 3981-3989.
    • (1995) Biochemistry , vol.34 , pp. 3981-3989
    • Nair, S.K.1    Krebs, J.F.2    Christianson, D.W.3    Fierke, C.A.4
  • 56
    • 0032882552 scopus 로고    scopus 로고
    • Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes
    • Christianson, D.W.J.; David, C. Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes. Ann. Rev. Biochem. 1999, 68, 33-57.
    • (1999) Ann. Rev. Biochem , vol.68 , pp. 33-57
    • Christianson, D.W.J.1    David, C.2


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