메뉴 건너뛰기




Volumn 49, Issue 24, 2010, Pages 5048-5056

Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION EDGES; ACTIVE SITE; AMINO ACID SEQUENCE; BIOLOGICAL FUNCTIONS; COFACTORS; DIFFERENCE-FOURIER MAP; HISTONE DEACETYLASES; HYDROXAMATE; IN-VIVO; LIVING CELL; METAL BINDING SITES; METAL CONCENTRATIONS; METAL CONTENT; METAL COORDINATION; METAL SPECIFICITY; METAL SUBSTITUTION; MICHAELIS COMPLEX; PROTEIN FOLDS; PROTEIN SAMPLES; RAT LIVERS; SOLUTION STUDY; X RAY CRYSTAL STRUCTURES; X-RAY DIFFRACTION DATA;

EID: 77953664293     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1005046     Document Type: Article
Times cited : (70)

References (78)
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function Cell 128, 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches
    • Seo, J. and Lee, K. J. (2004) Post-translational modifications and their biological functions: proteomic analysis and systematic approaches J. Biochem. Mol. Biol. 37, 35-44
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 35-44
    • Seo, J.1    Lee, K.J.2
  • 4
    • 27544505676 scopus 로고    scopus 로고
    • Chromatin modifier enzymes, the histone code and cancer
    • Santos-Rosa, H. and Caldas, C. (2005) Chromatin modifier enzymes, the histone code and cancer Eur. J. Cancer 41, 2381-2402
    • (2005) Eur. J. Cancer , vol.41 , pp. 2381-2402
    • Santos-Rosa, H.1    Caldas, C.2
  • 5
    • 68349135058 scopus 로고    scopus 로고
    • Histone modification patterns and epigenetic codes
    • Lennartsson, A. and Ekwall, K. (2009) Histone modification patterns and epigenetic codes Biochim. Biophys. Acta 1790, 863-868
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 863-868
    • Lennartsson, A.1    Ekwall, K.2
  • 6
    • 65249123485 scopus 로고    scopus 로고
    • Histone acetylation: Truth of consequences?
    • Choi, J. K. and Howe, L. J. (2009) Histone acetylation: truth of consequences? Biochem. Cell Biol. 87, 139-150
    • (2009) Biochem. Cell Biol. , vol.87 , pp. 139-150
    • Choi, J.K.1    Howe, L.J.2
  • 7
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution Nature 389, 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 8
    • 34547858913 scopus 로고    scopus 로고
    • Structure and acetyl-lysine recognition of the bromodomain
    • Mujtaba, S., Zeng, L., and Zhou, M.-M. (2007) Structure and acetyl-lysine recognition of the bromodomain Oncogene 26, 5521-5527
    • (2007) Oncogene , vol.26 , pp. 5521-5527
    • Mujtaba, S.1    Zeng, L.2    Zhou, M.-M.3
  • 10
    • 70149105669 scopus 로고    scopus 로고
    • The role of human bromodomains in chromatin biology and gene transcription
    • Sanchez, R. and Zhou, M.-M. (2009) The role of human bromodomains in chromatin biology and gene transcription Curr. Opin. Drug Discovery Dev. 12, 659-665
    • (2009) Curr. Opin. Drug Discovery Dev. , vol.12 , pp. 659-665
    • Sanchez, R.1    Zhou, M.-M.2
  • 11
    • 66149185424 scopus 로고    scopus 로고
    • Unbiased proteomic screen for binding proteins to modified lysines on histone H3
    • Chan, D. W., Wang, Y., Wu, M., Wong, J., Qin, J., and Zhao, Y. (2009) Unbiased proteomic screen for binding proteins to modified lysines on histone H3 Proteomics 9, 2343-2354
    • (2009) Proteomics , vol.9 , pp. 2343-2354
    • Chan, D.W.1    Wang, Y.2    Wu, M.3    Wong, J.4    Qin, J.5    Zhao, Y.6
  • 12
    • 66149127693 scopus 로고    scopus 로고
    • The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes
    • Li, S. and Shogren-Knaak, M. A. (2008) The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes J. Biol. Chem. 284, 9411-9417
    • (2008) J. Biol. Chem. , vol.284 , pp. 9411-9417
    • Li, S.1    Shogren-Knaak, M.A.2
  • 13
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti, I. V., Lee, Y.-M., and Goodson, H. V. (2004) Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis J. Mol. Biol. 338, 17-31
    • (2004) J. Mol. Biol. , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.-M.2    Goodson, H.V.3
  • 14
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C. A., and Schreiber, S. L. (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p Science 272, 408-411
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 18
    • 3242793175 scopus 로고    scopus 로고
    • Expression of histone deacetylase 8, a class i histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues
    • Waltregny, D., de Leval, L., Glénisson, W., Ly Tran, S., North, B. J., Bellahcene, A., Weidle, U., Verdin, E., and Castronovo, V. (2004) Expression of histone deacetylase 8, a class I histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues Am. J. Pathol. 165, 553-564
    • (2004) Am. J. Pathol. , vol.165 , pp. 553-564
    • Waltregny, D.1    De Leval, L.2    Glénisson, W.3    Ly Tran, S.4    North, B.J.5    Bellahcene, A.6    Weidle, U.7    Verdin, E.8    Castronovo, V.9
  • 19
    • 34547919621 scopus 로고    scopus 로고
    • Class IIa histone deacetylases: Regulating the regulators
    • Martin, M., Kettmann, R., and Dequiedt, F. (2007) Class IIa histone deacetylases: regulating the regulators Oncogene 26, 5450-5467
    • (2007) Oncogene , vol.26 , pp. 5450-5467
    • Martin, M.1    Kettmann, R.2    Dequiedt, F.3
  • 20
    • 0029962708 scopus 로고    scopus 로고
    • Structure of a unique binuclear manganese cluster in arginase
    • Kanyo, Z. F., Scolnick, L. R., Ash, D. E., and Christianson, D. W. (1996) Structure of a unique binuclear manganese cluster in arginase Nature 383, 554-557
    • (1996) Nature , vol.383 , pp. 554-557
    • Kanyo, Z.F.1    Scolnick, L.R.2    Ash, D.E.3    Christianson, D.W.4
  • 27
    • 33646548638 scopus 로고    scopus 로고
    • Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion
    • Gantt, S. L., Gattis, S. G., and Fierke, C. A. (2006) Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion Biochemistry 45, 6170-6178
    • (2006) Biochemistry , vol.45 , pp. 6170-6178
    • Gantt, S.L.1    Gattis, S.G.2    Fierke, C.A.3
  • 30
    • 0037472109 scopus 로고    scopus 로고
    • S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein
    • Zhu, J., Dizin, E., Hu, X., Wavreille, A.-S., Park, J., and Pei, D. (2003) S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein Biochemistry 42, 4717-4726
    • (2003) Biochemistry , vol.42 , pp. 4717-4726
    • Zhu, J.1    Dizin, E.2    Hu, X.3    Wavreille, A.-S.4    Park, J.5    Pei, D.6
  • 31
    • 0033600583 scopus 로고    scopus 로고
    • The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme
    • D'souza, V. M. and Holz, R. C. (1999) The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme Biochemistry 38, 11079-11085
    • (1999) Biochemistry , vol.38 , pp. 11079-11085
    • D'souza, V.M.1    Holz, R.C.2
  • 32
    • 0001267065 scopus 로고    scopus 로고
    • Characterization of cobalt(II)-substituted peptide deformylase: Function of the metal ion and the catalytic residue glu-133
    • Rajagopalan, P. T. R., Grimme, S., and Pei, D. (2000) Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue glu-133 Biochemistry 39, 779-790
    • (2000) Biochemistry , vol.39 , pp. 779-790
    • Rajagopalan, P.T.R.1    Grimme, S.2    Pei, D.3
  • 33
    • 14744298615 scopus 로고    scopus 로고
    • Both nucleophile and substrate bind to the catalytic Fe(II)-center in the type-II methionyl aminopeptidase from Pyrococcus furiousus
    • Copik, A. J., Waterson, S., Swierczek, S. I., Bennett, B., and Holz, R. C. (2005) Both nucleophile and substrate bind to the catalytic Fe(II)-center in the type-II methionyl aminopeptidase from Pyrococcus furiousus Inorg. Chem. 44, 1160-1162
    • (2005) Inorg. Chem. , vol.44 , pp. 1160-1162
    • Copik, A.J.1    Waterson, S.2    Swierczek, S.I.3    Bennett, B.4    Holz, R.C.5
  • 34
    • 0027488896 scopus 로고
    • Cytosine deaminase. The roles of divalent metal ions in catalysis
    • Porter, D. J. T. and Austin, E. A. (1993) Cytosine deaminase. The roles of divalent metal ions in catalysis J. Biol. Chem. 268, 24005-24011
    • (1993) J. Biol. Chem. , vol.268 , pp. 24005-24011
    • Porter, D.J.T.1    Austin, E.A.2
  • 36
    • 58149144730 scopus 로고    scopus 로고
    • Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors
    • Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., and Christianson, D. W. (2008) Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors Biochemistry 47, 13554-13563
    • (2008) Biochemistry , vol.47 , pp. 13554-13563
    • Dowling, D.P.1    Gantt, S.L.2    Gattis, S.G.3    Fierke, C.A.4    Christianson, D.W.5
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • Jung, M., Brosch, G., Kolle, D., Scherf, H., Gerhauser, C., and Loidl, P. (1999) Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation J. Med. Chem. 42, 4669-4679
    • (1999) J. Med. Chem. , vol.42 , pp. 4669-4679
    • Jung, M.1    Brosch, G.2    Kolle, D.3    Scherf, H.4    Gerhauser, C.5    Loidl, P.6
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 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. D 53, 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 44
    • 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 60, 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 45
    • 1842591322 scopus 로고    scopus 로고
    • Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis
    • McCall, K. A. and Fierke, C. A. (2004) Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis Biochemistry 43, 3979-3986
    • (2004) Biochemistry , vol.43 , pp. 3979-3986
    • McCall, K.A.1    Fierke, C.A.2
  • 46
    • 0034633293 scopus 로고    scopus 로고
    • Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals
    • McCall, K. A. and Fierke, C. A. (2000) Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals Anal. Biochem. 284, 307-315
    • (2000) Anal. Biochem. , vol.284 , pp. 307-315
    • McCall, K.A.1    Fierke, C.A.2
  • 48
    • 0036570964 scopus 로고    scopus 로고
    • A review of fluorescence methods for assessing labile iron in cells and biological fluids
    • Esposito, B. P., Epsztejn, S., Breuer, W., and Cabantchik, Z. I. (2002) A review of fluorescence methods for assessing labile iron in cells and biological fluids Anal. Biochem. 304, 1-18
    • (2002) Anal. Biochem. , vol.304 , pp. 1-18
    • Esposito, B.P.1    Epsztejn, S.2    Breuer, W.3    Cabantchik, Z.I.4
  • 49
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C. E. and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis Science 292, 2488-2492
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'halloran, T.V.2
  • 50
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L. and Falchuk, K. H. (1993) The biochemical basis of zinc physiology Physiol. Rev. 73, 79-118
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 52
    • 21544440823 scopus 로고
    • Order of stability of metal complexes
    • Irving, J. T. and Williams, J. P. (1948) Order of stability of metal complexes Nature 162, 746-747
    • (1948) Nature , vol.162 , pp. 746-747
    • Irving, J.T.1    Williams, J.P.2
  • 53
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym, R. A., Thompson, R. B., Stoddard, A. K., and Fierke, C. A. (2006) Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor ACS Chem. Biol. 1, 103-111
    • (2006) ACS Chem. Biol. , vol.1 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 56
    • 41349120026 scopus 로고    scopus 로고
    • Intracellular iron transport and storage: From molecular mechanisms to health implications
    • MacKenzie, E. L., Iwasaki, K., and Tsuji, Y. (2008) Intracellular iron transport and storage: from molecular mechanisms to health implications Antioxid. Redox Signaling 10, 997-1030
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 997-1030
    • MacKenzie, E.L.1    Iwasaki, K.2    Tsuji, Y.3
  • 57
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cells
    • Petrat, F., de Groot, H., and Rauen, U. (2001) Subcellular distribution of chelatable iron: a laser scanning microscopic study in isolated hepatocytes and liver endothelial cells Biochem. J. 356, 61-69
    • (2001) Biochem. J. , vol.356 , pp. 61-69
    • Petrat, F.1    De Groot, H.2    Rauen, U.3
  • 58
    • 0029121270 scopus 로고
    • Interaction of arginase with metal ions: Studies of the enzyme from human liver and comparison with other arginases
    • Carvajal, N., Torres, C., Uribe, E., and Salas, M. (1995) Interaction of arginase with metal ions: studies of the enzyme from human liver and comparison with other arginases Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 112, 153-159
    • (1995) Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. , vol.112 , pp. 153-159
    • Carvajal, N.1    Torres, C.2    Uribe, E.3    Salas, M.4
  • 60
    • 0029822783 scopus 로고    scopus 로고
    • Acetylpolyamine amidohydrolase from Mycoplana ramosa: Gene cloning and characterization of the metal-substituted enzyme
    • Sakurada, K., Ohta, T., Fujishiro, K., Hasegawa, M., and Aisaka, K. (1996) Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme J. Bacteriol. 178, 5781-5786
    • (1996) J. Bacteriol. , vol.178 , pp. 5781-5786
    • Sakurada, K.1    Ohta, T.2    Fujishiro, K.3    Hasegawa, M.4    Aisaka, K.5
  • 61
    • 5444254467 scopus 로고    scopus 로고
    • Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates
    • Riester, D., Wegener, D., Hildmann, C., and Schwienhorst, A. (2004) Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates Biochem. Biophys. Res. Commun. 324, 1116-1123
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1116-1123
    • Riester, D.1    Wegener, D.2    Hildmann, C.3    Schwienhorst, A.4
  • 62
    • 37549067781 scopus 로고    scopus 로고
    • Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases
    • Smith, B. C. and Denu, J. M. (2007) Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases J. Biol. Chem. 282, 37256-37265
    • (2007) J. Biol. Chem. , vol.282 , pp. 37256-37265
    • Smith, B.C.1    Denu, J.M.2
  • 64
    • 4644221775 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Toward an understanding of cellular machinery and molecular mechanism
    • Mansy, S. S. and Cowan, J. A. (2004) Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism Acc. Chem. Res. 37, 719-725
    • (2004) Acc. Chem. Res. , vol.37 , pp. 719-725
    • Mansy, S.S.1    Cowan, J.A.2
  • 65
    • 27644580799 scopus 로고    scopus 로고
    • Understanding how cells allocate metals using metal sensors and metallochaperones
    • Tottey, S., Harvie, D. R., and Robinson, N. J. (2005) Understanding how cells allocate metals using metal sensors and metallochaperones Acc. Chem. Res. 38, 775-783
    • (2005) Acc. Chem. Res. , vol.38 , pp. 775-783
    • Tottey, S.1    Harvie, D.R.2    Robinson, N.J.3
  • 66
    • 33646155960 scopus 로고    scopus 로고
    • The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2
    • Yang, M., Cobine, P. A., Molik, S., Naranuntarat, A., Lill, R., Winge, D. R., and Culotta, V. C. (2006) The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2 EMBO J. 25, 1775-1783
    • (2006) EMBO J. , vol.25 , pp. 1775-1783
    • Yang, M.1    Cobine, P.A.2    Molik, S.3    Naranuntarat, A.4    Lill, R.5    Winge, D.R.6    Culotta, V.C.7
  • 67
    • 15244353301 scopus 로고    scopus 로고
    • Arginase: Structure, mechanism, and physiological role in male and female sexual arousal
    • Christianson, D. W. (2005) Arginase: structure, mechanism, and physiological role in male and female sexual arousal Acc. Chem. Res. 38, 191-201
    • (2005) Acc. Chem. Res. , vol.38 , pp. 191-201
    • Christianson, D.W.1
  • 69
    • 77949908961 scopus 로고    scopus 로고
    • Activation and inhibition of histone deacetylase 8 by monovalent cations
    • Gantt, S. L., Joseph, C. G., and Fierke, C. A. (2009) Activation and inhibition of histone deacetylase 8 by monovalent cations J. Biol. Chem. 285, 6036-6043
    • (2009) J. Biol. Chem. , vol.285 , pp. 6036-6043
    • Gantt, S.L.1    Joseph, C.G.2    Fierke, C.A.3
  • 70
    • 77953677834 scopus 로고    scopus 로고
    • Ph.D. Dissertation, University of Michigan, Ann Arbor
    • Gantt, S. L. (2006) Ph.D. Dissertation, University of Michigan, Ann Arbor.
    • (2006)
    • Gantt, S.L.1
  • 71
    • 39549112496 scopus 로고    scopus 로고
    • Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor
    • Mochalkin, I., Knafels, J. D., and Lightle, S. (2008) Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor Protein Sci. 17, 450-457
    • (2008) Protein Sci. , vol.17 , pp. 450-457
    • Mochalkin, I.1    Knafels, J.D.2    Lightle, S.3
  • 73
    • 0027988841 scopus 로고
    • Subcellular localization, metal ion requirement and kinetic properties of arginase from the gill tissue of the bivalve Semele solida
    • Carvajal, N., Uribe, E., and Torres, C. (1994) Subcellular localization, metal ion requirement and kinetic properties of arginase from the gill tissue of the bivalve Semele solida Comp. Biochem. Physiol 109B, 683-689
    • (1994) Comp. Biochem. Physiol , vol.109 , pp. 683-689
    • Carvajal, N.1    Uribe, E.2    Torres, C.3
  • 74
    • 0038339405 scopus 로고    scopus 로고
    • Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase i
    • Cama, E., Emig, F. A., Ash, D. E., and Christianson, D. W. (2003) Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase I Biochemistry 42, 7748-7758
    • (2003) Biochemistry , vol.42 , pp. 7748-7758
    • Cama, E.1    Emig, F.A.2    Ash, D.E.3    Christianson, D.W.4
  • 76
    • 0032971984 scopus 로고    scopus 로고
    • UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme
    • Jackman, J. E., Raetz, C. R. H., and Fierke, C. A. (1999) UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme Biochemistry 38, 1902-1911
    • (1999) Biochemistry , vol.38 , pp. 1902-1911
    • Jackman, J.E.1    Raetz, C.R.H.2    Fierke, C.A.3
  • 77
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb, W. N. and Strater, N. (1996) Recent advances in zinc enzymology Chem. Rev. 96, 2375-2434
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2434
    • Lipscomb, W.N.1    Strater, N.2
  • 78
    • 9744244982 scopus 로고    scopus 로고
    • Zinc hydrolases: The mechanisms of zinc-dependent deacetylases
    • Hernick, M. and Fierke, C. A. (2005) Zinc hydrolases: the mechanisms of zinc-dependent deacetylases Arch. Biochem. Biophys. 433, 71-84
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 71-84
    • Hernick, M.1    Fierke, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.