메뉴 건너뛰기




Volumn 22, Issue 1, 2009, Pages 141-148

The ins and outs of biological zinc sites

Author keywords

Alcohol dehydrogenase; Carbonic anhydrase; Carboxypeptidase; Chelation; Chelators; D pencillamine; Matrix metalloproteinase; Metalloenzymes; Thionein; X ray structure; Zinc; Zinc enzymes

Indexed keywords

ALCOHOL DEHYDROGENASE; CARBONATE DEHYDRATASE; GELATINASE A; INTERSTITIAL COLLAGENASE; MUTANT PROTEIN; PENICILLAMINE; PROMATRIX METALLOPROTEASE; PROTEIN PRECURSOR; PROTEINASE; UNCLASSIFIED DRUG; ZINC; ZINC BINDING PROTEIN; ZINC PROTEASE;

EID: 59449107552     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-008-9184-1     Document Type: Conference Paper
Times cited : (74)

References (35)
  • 1
    • 30744471169 scopus 로고    scopus 로고
    • Counting the zinc-proteins encoded in the human genome
    • 10.1021/pr050361j
    • C Andreini L Banci I Bertini A Rosato 2006 Counting the zinc-proteins encoded in the human genome J Proteome Res 5 196 201 10.1021/pr050361j
    • (2006) J Proteome Res , vol.5 , pp. 196-201
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 2
    • 33750998488 scopus 로고    scopus 로고
    • Zinc through the three domains of life
    • 10.1021/pr0603699
    • C Andreini L Banci I Bertini A Rosato 2006 Zinc through the three domains of life J Proteome Res 5 3173 3178 10.1021/pr0603699
    • (2006) J Proteome Res , vol.5 , pp. 3173-3178
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 3
    • 0018232814 scopus 로고
    • Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases
    • 10.1016/0022-2836(78)90356-X
    • P Argos RM Garavito W Eventoff MG Rossmann CI Branden 1978 Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases J Mol Biol 126 141 158 10.1016/0022-2836(78)90356-X
    • (1978) J Mol Biol , vol.126 , pp. 141-158
    • Argos, P.1    Garavito, R.M.2    Eventoff, W.3    Rossmann, M.G.4    Branden, C.I.5
  • 4
    • 0023704559 scopus 로고
    • Use of chelating agents to inhibit enzymes
    • 10.1016/0076-6879(88)58051-5
    • DS Auld 1988 Use of chelating agents to inhibit enzymes Methods Enzymol 158 110 114 10.1016/0076-6879(88)58051-5
    • (1988) Methods Enzymol , vol.158 , pp. 110-114
    • Auld, D.S.1
  • 5
    • 0029062905 scopus 로고
    • Removal and replacement of metal ions in metallopeptidases
    • 10.1016/0076-6879(95)48016-1
    • DS Auld 1995 Removal and replacement of metal ions in metallopeptidases Methods Enzymol 248 228 242 10.1016/0076-6879(95)48016-1
    • (1995) Methods Enzymol , vol.248 , pp. 228-242
    • Auld, D.S.1
  • 6
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • 10.1023/A:1012976615056
    • DS Auld 2001 Zinc coordination sphere in biochemical zinc sites Biometals 14 271 313 10.1023/A:1012976615056
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 11
    • 58149136238 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: The role of zinc for alcohol dehydrogenase structure and function
    • DS Auld T Bergman 2008 Medium- and short-chain dehydrogenase/reductase gene and protein families: the role of zinc for alcohol dehydrogenase structure and function Cell Mol Life Sci 65 3961 3970
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3961-3970
    • Auld, D.S.1    Bergman, T.2
  • 12
    • 58149116809 scopus 로고    scopus 로고
    • Zinc binding to peptide Analogs of the structural zinc site in alcohol dehydrogenase: Implications for an entatic state
    • 10.1007/s00018-008-8379-5
    • T Bergman K Zhang C Palmberg H Jörnvall DS Auld 2008 Zinc binding to peptide Analogs of the structural zinc site in alcohol dehydrogenase: implications for an entatic state Cell Mol Life Sci 65 4019 4027 10.1007/s00018-008-8379-5
    • (2008) Cell Mol Life Sci , vol.65 , pp. 4019-4027
    • Bergman, T.1    Zhang, K.2    Palmberg, C.3    Jörnvall, H.4    Auld, D.S.5
  • 13
    • 0034720771 scopus 로고    scopus 로고
    • Inhibition of carboxypeptidase A by d-pencillamine: Mechanism and implications for drug design
    • 10.1021/bi000101+
    • CR Chong DS Auld 2000 Inhibition of carboxypeptidase A by d-pencillamine: mechanism and implications for drug design Biochemistry 39 7580 7588 10.1021/bi000101+
    • (2000) Biochemistry , vol.39 , pp. 7580-7588
    • Chong, C.R.1    Auld, D.S.2
  • 14
    • 35848931030 scopus 로고    scopus 로고
    • Catalysis of zinc transfer by d-penicillamine to secondary chelators
    • 10.1021/jm070803y
    • CR Chong DS Auld 2007 Catalysis of zinc transfer by d-penicillamine to secondary chelators J Med Chem 50 5524 5527 10.1021/jm070803y
    • (2007) J Med Chem , vol.50 , pp. 5524-5527
    • Chong, C.R.1    Auld, D.S.2
  • 15
    • 0000726701 scopus 로고    scopus 로고
    • Carbonic anhydrase: Evolution of the design of the zinc binding site by nature and by design
    • 10.1021/ar9501232
    • DW Christianson CA Fierke 1996 Carbonic anhydrase: evolution of the design of the zinc binding site by nature and by design Acc Chem Res 29 331 339 10.1021/ar9501232
    • (1996) Acc Chem Res , vol.29 , pp. 331-339
    • Christianson, D.W.1    Fierke, C.A.2
  • 17
    • 15744362065 scopus 로고    scopus 로고
    • X-ray structure of human proMMP-1: New insights into procollagenase activation and collagen binding
    • 10.1074/jbc.M411084200
    • D Jozic G Bourenkov NH Lim R Visse H Nagase W Bode K Maskos 2005 X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding J Biol Chem 280 9578 9585 10.1074/jbc.M411084200
    • (2005) J Biol Chem , vol.280 , pp. 9578-9585
    • Jozic, D.1    Bourenkov, G.2    Lim, N.H.3    Visse, R.4    Nagase, H.5    Bode, W.6    Maskos, K.7
  • 18
    • 0023781524 scopus 로고
    • Biochemistry of metallothionein
    • 10.1021/bi00423a001
    • JH Kagi A Schaffer 1988 Biochemistry of metallothionein Biochemistry 27 8509 8515 10.1021/bi00423a001
    • (1988) Biochemistry , vol.27 , pp. 8509-8515
    • Kagi, J.H.1    Schaffer, A.2
  • 19
    • 0028873117 scopus 로고
    • Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
    • 10.1021/ja00131a004
    • LL Kiefer SA Paterno CA Fierke 1995 Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency J Am Chem Soc 117 6831 6837 10.1021/ja00131a004
    • (1995) J Am Chem Soc , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 20
    • 33947276403 scopus 로고    scopus 로고
    • Different redox states of metallothionein/thionein in biological tissue
    • 10.1042/BJ20061044
    • A Krezel W Maret 2007 Different redox states of metallothionein/thionein in biological tissue Biochem J 402 551 558 10.1042/BJ20061044
    • (2007) Biochem J , vol.402 , pp. 551-558
    • Krezel, A.1    Maret, W.2
  • 21
    • 0028796822 scopus 로고
    • X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
    • 10.1021/ja00131a005
    • CA Lesburg DW Christianson 1995 X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site J Am Chem Soc 117 6838 6844 10.1021/ja00131a005
    • (1995) J Am Chem Soc , vol.117 , pp. 6838-6844
    • Lesburg, C.A.1    Christianson, D.W.2
  • 23
    • 0033523040 scopus 로고    scopus 로고
    • Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed
    • 10.1126/science.284.5420.1667 see comments
    • E Morgunova A Tuuttila U Bergmann M Isupov Y Lindqvist G Schneider K Tryggvason 1999 Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed Science 284 1667 1670 10.1126/science.284.5420.1667 see comments
    • (1999) Science , vol.284 , pp. 1667-1670
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Isupov, M.4    Lindqvist, Y.5    Schneider, G.6    Tryggvason, K.7
  • 24
    • 0346195665 scopus 로고    scopus 로고
    • Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
    • 10.1038/nature01370
    • R Natesh SL Schwager ED Sturrock KR Acharya 2003 Crystal structure of the human angiotensin-converting enzyme-lisinopril complex Nature 421 551 554 10.1038/nature01370
    • (2003) Nature , vol.421 , pp. 551-554
    • Natesh, R.1    Schwager, S.L.2    Sturrock, E.D.3    Acharya, K.R.4
  • 25
    • 0017578611 scopus 로고
    • Design of specific inhibitors of angiotensin-converting enzyme: New class of orally active antihypertensive agents
    • 10.1126/science.191908
    • MA Ondetti B Rubin DW Cushman 1977 Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents Science 196 441 444 10.1126/science.191908
    • (1977) Science , vol.196 , pp. 441-444
    • Ondetti, M.A.1    Rubin, B.2    Cushman, D.W.3
  • 26
    • 34748870747 scopus 로고    scopus 로고
    • Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures
    • K Patel A Kumar S Durani 2007 Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures Biochim Biophys Acta 1774 1247 1253
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1247-1253
    • Patel, K.1    Kumar, A.2    Durani, S.3
  • 27
    • 0004936640 scopus 로고
    • Zinc and iron deficiencies in male subjects with dwarfism and hypogonadism but without ancylostomiasis, schistosomiasis or severe anemia
    • AS Prasad AR Schulert A Miale Jr Z Farid HH Sandstead 1963 Zinc and iron deficiencies in male subjects with dwarfism and hypogonadism but without ancylostomiasis, schistosomiasis or severe anemia Am J Clin Nutr 12 437 444
    • (1963) Am J Clin Nutr , vol.12 , pp. 437-444
    • Prasad, A.S.1    Schulert, A.R.2    Miale Jr, A.3    Farid, Z.4    Sandstead, H.H.5
  • 28
    • 0002826692 scopus 로고
    • Etudes cliniques sur la vegetation
    • J Raulin 1869 Etudes cliniques sur la vegetation Ann Sci Bot Biol Veg 11 93
    • (1869) Ann Sci Bot Biol Veg , vol.11 , pp. 93
    • Raulin, J.1
  • 29
    • 59449093873 scopus 로고
    • The Chemical Society London
    • Sillen LG, Martell AE (1971) Stability constants of metal-ion complexes. The Chemical Society, London, pp 250-281
    • (1971) , pp. 250-281
    • Sillen, L.G.1    Martell, A.E.2
  • 30
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent human fibroblast collagenase: Evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation
    • 10.1073/pnas.87.1.364
    • EB Springman EL Angleton H Birkedal-Hansen HE Van Wart 1990 Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation Proc Natl Acad Sci USA 87 364 368 10.1073/pnas.87.1.364
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 364-368
    • Springman, E.B.1    Angleton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 33
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • 10.1021/bi00476a001
    • BL Vallee DS Auld 1990 Zinc coordination, function, and structure of zinc enzymes and other proteins Biochemistry 29 5647 5659 10.1021/bi00476a001
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 34
    • 0027303379 scopus 로고
    • New perspective on zinc biochemistry: Cocatalytic sites in multi-zinc enzymes
    • 10.1021/bi00077a001
    • BL Vallee DS Auld 1993 New perspective on zinc biochemistry: cocatalytic sites in multi-zinc enzymes Biochemistry 32 6493 6500 10.1021/bi00077a001
    • (1993) Biochemistry , vol.32 , pp. 6493-6500
    • Vallee, B.L.1    Auld, D.S.2
  • 35
    • 85163993912 scopus 로고
    • Spectroscopic properties of metallothionein
    • M Vasak JHR Kagi 1983 Spectroscopic properties of metallothionein Metal Ions Biol Syst 16 213 273
    • (1983) Metal Ions Biol Syst , vol.16 , pp. 213-273
    • Vasak, M.1    Kagi, J.H.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.