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Volumn 2, Issue 2, 1998, Pages 222-234

Zinc enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; CARBONATE DEHYDRATASE; METALLOPROTEINASE; PHOSPHOLIPASE C; PROTEINASE; ZINC;

EID: 0032041818     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80064-1     Document Type: Article
Times cited : (354)

References (47)
  • 1
    • 0001119497 scopus 로고
    • Carbonic anhydrase. Purification and nature of the enzyme
    • Keilin D, Mann T: Carbonic anhydrase. Purification and nature of the enzyme. Biochem J 1940, 34:1163-1176.
    • (1940) Biochem J , vol.34 , pp. 1163-1176
    • Keilin, D.1    Mann, T.2
  • 2
    • 0343349776 scopus 로고
    • Carboxypeptidase, a zinc metalloprotein
    • Vallee BL, Neurath H: Carboxypeptidase, a zinc metalloprotein. J. Am. Chem Soc 1954, 76:5006-5006.
    • (1954) J. Am. Chem Soc , vol.76 , pp. 5006-5006
    • Vallee, B.L.1    Neurath, H.2
  • 3
    • 0026463503 scopus 로고
    • Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
    • Hakansson K, Carlsson M, Svensson LA, Liljas A: Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J Mol Biol 1992, 227:1192-1204.
    • (1992) J Mol Biol , vol.227 , pp. 1192-1204
    • Hakansson, K.1    Carlsson, M.2    Svensson, L.A.3    Liljas, A.4
  • 4
    • 0014217388 scopus 로고
    • Mechanism of action of carbonic anhydrase. Substrate, sulfonamide and anion binding
    • Coleman JE: Mechanism of action of carbonic anhydrase. Substrate, sulfonamide and anion binding. J Biol Chem 1967, 242:5212-5219.
    • (1967) J Biol Chem , vol.242 , pp. 5212-5219
    • Coleman, J.E.1
  • 5
    • 0001113609 scopus 로고
    • The catalytic mechanism of carbonic anhydrase
    • Lindskog S, Coleman JE: The catalytic mechanism of carbonic anhydrase. Proc Nat Acad Sci USA 1973, 70:2505-2508.
    • (1973) Proc Nat Acad Sci USA , vol.70 , pp. 2505-2508
    • Lindskog, S.1    Coleman, J.E.2
  • 6
    • 0028932267 scopus 로고
    • Proton transfer in carbonic anhydrase measured by equilibrium isotope exchange
    • Silverman DN: Proton transfer in carbonic anhydrase measured by equilibrium isotope exchange. Methods Enzymol 1995, 249:479-503.
    • (1995) Methods Enzymol , vol.249 , pp. 479-503
    • Silverman, D.N.1
  • 7
    • 0029057703 scopus 로고
    • Human carbonic anhydrases and carbonic anhydrase deficiencies
    • Sly WS, Hu PY: Human carbonic anhydrases and carbonic anhydrase deficiencies. Annu Rev Biochem 1995, 64:375-401.
    • (1995) Annu Rev Biochem , vol.64 , pp. 375-401
    • Sly, W.S.1    Hu, P.Y.2
  • 9
    • 0028867081 scopus 로고    scopus 로고
    • Structure determination of murine mitochondrial carbonic anhydrase V at 2.45 Å resolution: Implications for catalytic proton transfer and inhibitor design
    • Boriack-Sjodin PA, Heck RW, Laipis PJ, Silverman DN, Christianson DW: Structure determination of murine mitochondrial carbonic anhydrase V at 2.45 Å resolution: Implications for catalytic proton transfer and inhibitor design. Proc Natl Acad Sci USA 1996, 92:10949-10953.
    • (1996) Proc Natl Acad Sci USA , vol.92 , pp. 10949-10953
    • Boriack-Sjodin, P.A.1    Heck, R.W.2    Laipis, P.J.3    Silverman, D.N.4    Christianson, D.W.5
  • 10
    • 0028590042 scopus 로고
    • Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites
    • Kiefer LL, Fierke CA: Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites. Biochemistry 1994, 33:15233-15240.
    • (1994) Biochemistry , vol.33 , pp. 15233-15240
    • Kiefer, L.L.1    Fierke, C.A.2
  • 11
    • 0028589527 scopus 로고
    • Structural consequences of redesigning a protein-zinc binding site
    • Ippolito JA, Cristianson DW: Structural consequences of redesigning a protein-zinc binding site. Biochemistry 1994, 33:15241-15249.
    • (1994) Biochemistry , vol.33 , pp. 15241-15249
    • Ippolito, J.A.1    Cristianson, D.W.2
  • 12
    • 0028873117 scopus 로고
    • Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
    • Kiefer LL, Paterno SA, Fierke CA: Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency. J Am Chem Soc 1995, 117:6831-6837.
    • (1995) J am Chem Soc , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 13
    • 0028796822 scopus 로고
    • X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
    • Lesburg C, Christianson DW: X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site. J Am Chem Soc 1995, 117:6838-6844.
    • (1995) J am Chem Soc , vol.117 , pp. 6838-6844
    • Lesburg, C.1    Christianson, D.W.2
  • 14
    • 0002873247 scopus 로고
    • Proteolytic enzymes: Aspartic and metallo peptidases
    • Barrett AJ (Ed): Proteolytic enzymes: aspartic and metallo peptidases. Methods Enzymol 1995, 248:183-787.
    • (1995) Methods Enzymol , vol.248 , pp. 183-787
    • Barrett, A.J.1
  • 15
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews BW: Structural basis of the action of thermolysin and related zinc peptidases. Accounts Chem Res 1988, 21:333-340.
    • (1988) Accounts Chem Res , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 19
    • 0021095532 scopus 로고
    • Refined crystal structure of carboxypeptidase a at 1.54 Å resolution
    • Rees DC, Lewis M, Lipscomb WN: Refined crystal structure of carboxypeptidase A at 1.54 Å resolution. J Mol Biol 1983, 168:367-373.
    • (1983) J Mol Biol , vol.168 , pp. 367-373
    • Rees, D.C.1    Lewis, M.2    Lipscomb, W.N.3
  • 21
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures
    • Kim EE, Wyckoff HW: Reaction mechanism of alkaline phosphatase based on crystal structures. J Mol Biol 1991, 218:449-464.
    • (1991) J Mol Biol , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 23
    • 0025763145 scopus 로고
    • Crystal structure of Penicillium citrinum P1 nuclease at 2.8 Å resolution
    • Volbeda A, Lahm A, Sakiyama F, Suck D: Crystal structure of Penicillium citrinum P1 nuclease at 2.8 Å resolution. EMBO J 1991, 10:1607-1618.
    • (1991) EMBO J , vol.10 , pp. 1607-1618
    • Volbeda, A.1    Lahm, A.2    Sakiyama, F.3    Suck, D.4
  • 24
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman JE: Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct 1992, 21:441-483.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 25
    • 0020536591 scopus 로고
    • Synthesis and configurational anlysis of dinucleoside phosphate isotopically chiral at phosphorous. Stereochemical course of Penicillium citrum nuclease P1 reaction
    • Potter BVL, Connolly BA, Eckstein F: Synthesis and configurational anlysis of dinucleoside phosphate isotopically chiral at phosphorous. Stereochemical course of Penicillium citrum nuclease P1 reaction. Biochemistry 1983, 22:1369-1377.
    • (1983) Biochemistry , vol.22 , pp. 1369-1377
    • Bvl, P.1    Connolly, B.A.2    Eckstein, F.3
  • 27
    • 0026740977 scopus 로고
    • Crystal structures of phosphate, iodide and iodate-inhibited phospholipase C from Bacillus cereus and structural investigations of the binding of reaction products and a substrate analogue
    • Hansen S, Hansen SH, Hough E: Crystal structures of phosphate, iodide and iodate-inhibited phospholipase C from Bacillus cereus and structural investigations of the binding of reaction products and a substrate analogue. J Mol Biol 1992, 225:543-549.
    • (1992) J Mol Biol , vol.225 , pp. 543-549
    • Hansen, S.1    Hansen, S.H.2    Hough, E.3
  • 28
    • 0027379581 scopus 로고
    • Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analog
    • Hansen S, Hough E, Svensson LA, Wong Y-L, Martin SF: Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analog. J Mol Biol 1993, 234:179-187.
    • (1993) J Mol Biol , vol.234 , pp. 179-187
    • Hansen, S.1    Hough, E.2    Svensson, L.A.3    Wong, Y.-L.4    Martin, S.F.5
  • 29
    • 0028173920 scopus 로고
    • A proposal for the catalytic mechanism in phospholiipase C bases on interaction energy and distance geometry calculations
    • Sundell S, Hansen S, Hough E: A proposal for the catalytic mechanism in phospholiipase C bases on interaction energy and distance geometry calculations. Protein Eng 1994, 7:571-577.
    • (1994) Protein Eng , vol.7 , pp. 571-577
    • Sundell, S.1    Hansen, S.2    Hough, E.3
  • 30
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
    • Concha NO, Rasmussen BA, Bush K, Herzberg O: Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 1996, 4:823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 31
    • 0031569353 scopus 로고    scopus 로고
    • 2, a bacterial enzyme with applications in cancer therapy
    • 2 is a structurally and functionally interesting member of the group of enzymes containing binuclear zinc complexes at their active centers. This paper points out an interesting conservation of overall protein fold between proteases containing both binuclear and mononuclear zinc sites.
    • (1997) Structure , vol.5 , pp. 337-347
    • Rowsell, S.1    Pauptit, R.A.2    Tucker, A.D.3    Melton, R.G.4    Blow, D.M.5    Brick, P.6
  • 32
    • 0029761259 scopus 로고    scopus 로고
    • Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase
    • Blom NS, Tetreault S, Coulombe R, Sygusch J: Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat Struct Biol 1996, 3:856-862.
    • (1996) Nat Struct Biol , vol.3 , pp. 856-862
    • Blom, N.S.1    Tetreault, S.2    Coulombe, R.3    Sygusch, J.4
  • 33
    • 0027458881 scopus 로고
    • Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase
    • Zhang Y, Liang J-Y, Huang S, Ke H, Lipscomb WN: Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry 1993, 32:1844-1857.
    • (1993) Biochemistry , vol.32 , pp. 1844-1857
    • Zhang, Y.1    Liang, J.-Y.2    Huang, S.3    Ke, H.4    Lipscomb, W.N.5
  • 35
    • 0029918891 scopus 로고    scopus 로고
    • Crystallographic identification of metal-binding sites in E. coli inorganic pyrophosphatase
    • Kankare J, Salminen T, Lahti R, Cooperman BS, Baykov AA, Goldman A: Crystallographic identification of metal-binding sites in E. coli inorganic pyrophosphatase. Biochemistry 1996, 35:4670-4677.
    • (1996) Biochemistry , vol.35 , pp. 4670-4677
    • Kankare, J.1    Salminen, T.2    Lahti, R.3    Cooperman, B.S.4    Baykov, A.A.5    Goldman, A.6
  • 36
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi A, Pares S, Duée E, Galleni M, Duex C, Frère JM, Dideberg O: The 3-D structure of a zinc metallo-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 1995, 14:4919-4921.
    • (1995) EMBO J , vol.14 , pp. 4919-4921
    • Carfi, A.1    Pares, S.2    Duée, E.3    Galleni, M.4    Duex, C.5    Frère, J.M.6    Dideberg, O.7
  • 37
    • 0031440226 scopus 로고    scopus 로고
    • Crystal structures of the cadmium- And mercury-substituted metallo-lactamase from Bacteroids fragilis
    • Concha NO, Rasmussen BA, Bush K, Herzberg O: Crystal structures of the cadmium- and mercury-substituted metallo-lactamase from Bacteroids fragilis. Protein Sci 1997, 6:2671-2676. This is a significant documentation of the structural changes that may or may not occur when the zincs at a binuclear site are exchanged with other IIB metal ions.
    • (1997) Protein Sci , vol.6 , pp. 2671-2676
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 38
    • 0029116127 scopus 로고
    • Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution of a new crystal form
    • Sträter N, Lipscomb WN: Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution of a new crystal form. Biochemistry 1995, 34:9200-9210.
    • (1995) Biochemistry , vol.34 , pp. 9200-9210
    • Sträter, N.1    Lipscomb, W.N.2
  • 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
    • Sträter N, Lipscomb WN: 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 1995, 34:14792-14800.
    • (1995) Biochemistry , vol.34 , pp. 14792-14800
    • Sträter, N.1    Lipscomb, W.N.2
  • 40
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevier B, Schalk C, D'Orchymont H, Rondeau J-M, Moras D, Tarnus C: Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure 1994, 2:283-291.
    • (1994) Structure , vol.2 , pp. 283-291
    • Chevier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.-M.4    Moras, D.5    Tarnus, C.6
  • 41
    • 0029960042 scopus 로고    scopus 로고
    • The structure of aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit
    • Chevier B, D'Orchymont H, Schalk C, Tarnus C, Moras D: The structure of aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit Eur J Biochem 1996, 237:393-398.
    • (1996) Eur J Biochem , vol.237 , pp. 393-398
    • Chevier, B.1    D'Orchymont, H.2    Schalk, C.3    Tarnus, C.4    Moras, D.5
  • 43
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from E. coli: A new type of proteolytic enzyme
    • Roderick SL, Matthews BW:Structure of the cobalt-dependent methionine aminopeptidase from E. coli: a new type of proteolytic enzyme. Biochemistry 1993, 32:3907-3912.
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 44
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox DE, Binuclear metallohydrolases. Chem Rev 1996, 96:2435-2458. This is a concise review of the many enzymes containing binuclear metal ion complexes at their active centers.
    • (1996) Chem Rev , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 45
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
    • Park H-W, Boduluri SR, Moomaw JF, Casey PJ, Beese LS: Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science 1997, 275:1800-1804. This enzyme has a complex structure, but topological features of the protein clearly seem to establish the binding modes of the two large substrates and their relationship to the zinc ion.
    • (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
  • 46
    • 0031017064 scopus 로고    scopus 로고
    • Evidence for a catalytic role of zinc in protein farnesyltransferase
    • Huang C-C, Casey PJ, Fierke CA: Evidence for a catalytic role of zinc in protein farnesyltransferase. J Biol Chem 1997, 272:20-23.
    • (1997) J Biol Chem , vol.272 , pp. 20-23
    • Huang, C.-C.1    Casey, P.J.2    Fierke, C.A.3
  • 47
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon SF, Rodgers KK, Schatz DG, Coleman JE, Steitz TA: Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat Struct Biol 1997, 4:586-591.
    • (1997) Nat Struct Biol , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.