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Volumn 43, Issue 46, 2004, Pages 14594-14601

Molecular functions of conserved aspects of the GHMP kinase family

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CARBOHYDRATES; CATALYSIS; MOLECULAR BIOLOGY; ORGANIC SOLVENTS;

EID: 8844260402     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048963o     Document Type: Article
Times cited : (53)

References (34)
  • 1
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, A. (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins, Proc. Natl. Acad. Sci. U.S.A. 89, 7290-7294.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 2
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork, P., Sander, C., and Valencia, A. (1993) Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases, Protein Sci. 2, 31-40.
    • (1993) Protein Sci. , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 3
    • 0345373988 scopus 로고    scopus 로고
    • XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators
    • Luz, J. G., Hassig, C. A., Pickle, C., Godzik, A., Meyer, B. J., and Wilson, I. A. (2003) XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators, Genes Dev. 17, 977-990.
    • (2003) Genes Dev. , vol.17 , pp. 977-990
    • Luz, J.G.1    Hassig, C.A.2    Pickle, C.3    Godzik, A.4    Meyer, B.J.5    Wilson, I.A.6
  • 4
    • 0034917990 scopus 로고    scopus 로고
    • Mevalonate kinase deficiency in a child with periodic fever and without hyperimmunoglobulinaemia D
    • Di Rocco, M., Caruso, U., Waterham, H. R., Picco, P., Loy, A., and Wanders, R. J. (2001) Mevalonate kinase deficiency in a child with periodic fever and without hyperimmunoglobulinaemia D, J. Inherited Metab. Dis. 24, 411-412.
    • (2001) J. Inherited Metab. Dis. , vol.24 , pp. 411-412
    • Di Rocco, M.1    Caruso, U.2    Waterham, H.R.3    Picco, P.4    Loy, A.5    Wanders, R.J.6
  • 5
    • 0032727538 scopus 로고    scopus 로고
    • Molecular characterization of galactokinase deficiency in Japanese patients
    • Asada, M., Okano, Y., Imamura, T., Suyama, I., Hase, Y., and Isshiki, G. (1999) Molecular characterization of galactokinase deficiency in Japanese patients, J. Hum. Genet. 44, 377-382.
    • (1999) J. Hum. Genet. , vol.44 , pp. 377-382
    • Asada, M.1    Okano, Y.2    Imamura, T.3    Suyama, I.4    Hase, Y.5    Isshiki, G.6
  • 6
    • 0034476899 scopus 로고    scopus 로고
    • Structure and mechanism of homoserine kinase: Prototype for the GHMP kinase superfamily
    • Zhou, T., Daugherty, M., Grishin, N. V., Osterman, A. L., and Zhang, H. (2000) Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily, Struct. Fold. Des. 8, 1247-1257.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 1247-1257
    • Zhou, T.1    Daugherty, M.2    Grishin, N.V.3    Osterman, A.L.4    Zhang, H.5
  • 7
    • 0035180870 scopus 로고    scopus 로고
    • Archaeal shikimate kinase, a new member of the GHMP-kinase family
    • Daugherty, M., Vonstein, V., Overbeek, R., and Osterman, A. (2001) Archaeal shikimate kinase, a new member of the GHMP-kinase family, J. Bacteriol. 183, 292-300.
    • (2001) J. Bacteriol. , vol.183 , pp. 292-300
    • Daugherty, M.1    Vonstein, V.2    Overbeek, R.3    Osterman, A.4
  • 8
    • 0042858220 scopus 로고    scopus 로고
    • Molecular structure of galactokinase
    • Thoden, J. B., and Holden, H. M. (2003) Molecular structure of galactokinase, J. Biol. Chem. 278, 33305-33311.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33305-33311
    • Thoden, J.B.1    Holden, H.M.2
  • 10
    • 0035845650 scopus 로고    scopus 로고
    • Structural basis for the catalysis and substrate specificity of homoserine kinase
    • Krishna, S. S., Zhou, T., Daugherty, M., Osterman, A., and Zhang, H. (2001) Structural basis for the catalysis and substrate specificity of homoserine kinase, Biochemistry 40, 10810-10818.
    • (2001) Biochemistry , vol.40 , pp. 10810-10818
    • Krishna, S.S.1    Zhou, T.2    Daugherty, M.3    Osterman, A.4    Zhang, H.5
  • 11
    • 0036606171 scopus 로고    scopus 로고
    • Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily
    • Romanowski, M. J., Bonanno, J. B., and Burley, S. K. (2002) Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily, Proteins 47, 568-571.
    • (2002) Proteins , vol.47 , pp. 568-571
    • Romanowski, M.J.1    Bonanno, J.B.2    Burley, S.K.3
  • 12
    • 0042030862 scopus 로고    scopus 로고
    • Crystal structure of 4-(cytidine 5′-diphospho)-2-C-methyl-D- erythritol kinase, an enzyme in the nonmevalonate pathway of isoprenoid synthesis
    • Wada, T., Kuzuyama, T., Satoh, S., Kuramitsu, S., Yokoyama, S., Unzai, S., Tame, J. R., and Park, S. Y. (2003) Crystal structure of 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the nonmevalonate pathway of isoprenoid synthesis, J. Biol. Chem. 278, 30022-30027.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30022-30027
    • Wada, T.1    Kuzuyama, T.2    Satoh, S.3    Kuramitsu, S.4    Yokoyama, S.5    Unzai, S.6    Tame, J.R.7    Park, S.Y.8
  • 13
    • 0037088680 scopus 로고    scopus 로고
    • Structure of the Methanococcus jannaschii mevalonate kinase, a member of the GHMP kinase superfamily
    • Yang, D., Shipman, L. W., Roessner, C. A., Scott, A. I., and Sacchettini, J. C. (2002) Structure of the Methanococcus jannaschii mevalonate kinase, a member of the GHMP kinase superfamily, J. Biol. Chem. 277, 9462-9467.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9462-9467
    • Yang, D.1    Shipman, L.W.2    Roessner, C.A.3    Scott, A.I.4    Sacchettini, J.C.5
  • 14
    • 0032170425 scopus 로고    scopus 로고
    • The deoxyxylulose phosphate pathway of terpenoid biosynthesis in plants and microorganisms
    • Eisenreich, W., Schwarz, M., Cartayrade, A., Arigoni, D., Zenk, M. H., and Bacher, A. (1998) The deoxyxylulose phosphate pathway of terpenoid biosynthesis in plants and microorganisms, Chem. Biol. 5, R221-R233.
    • (1998) Chem. Biol. , vol.5
    • Eisenreich, W.1    Schwarz, M.2    Cartayrade, A.3    Arigoni, D.4    Zenk, M.H.5    Bacher, A.6
  • 15
    • 0022341287 scopus 로고
    • The interaction of phosphorothioate analogues of ATP with phosphomevalonate kinase. Kinetic and 31P NMR studies
    • Lee, C., and O'Sullivan, W. (1985) The interaction of phosphorothioate analogues of ATP with phosphomevalonate kinase. Kinetic and 31P NMR studies, J. Biol. Chem. 260, 13909-13915.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13909-13915
    • Lee, C.1    O'Sullivan, W.2
  • 16
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products
    • Cleland, W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products, Biochim. Biophys. Acta 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 17
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • Oberg, K. A., Ruysschaert, J. M., and Goormaghtigh, E. (2004) The optimization of protein secondary structure determination with infrared and circular dichroism spectra, Eur. J. Biochem. 271, 2937-2948.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2937-2948
    • Oberg, K.A.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 19
    • 0014546530 scopus 로고
    • A kinetic analysis of coupled enzyme assays
    • McClure, W. R. (1969) A kinetic analysis of coupled enzyme assays, Biochemistry 8, 2782-2786.
    • (1969) Biochemistry , vol.8 , pp. 2782-2786
    • McClure, W.R.1
  • 20
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data, Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 21
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. (1953) The determination of enzyme inhibitor constants, Biochem. J. 55, 170-171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 22
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej, T., Gibrat, J. F., and Bryant, S. H. (1995) Threading a database of protein cores, Proteins 23, 356-369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.F.2    Bryant, S.H.3
  • 25
    • 0037124052 scopus 로고    scopus 로고
    • The structure of a binary complex between a mammalian mevalonate kinase and ATP: Insights into the reaction mechanism and human inherited disease
    • Fu, Z., Wang, M., Potter, D., Miziorko, H. M., and Kim, J. J. (2002) The structure of a binary complex between a mammalian mevalonate kinase and ATP: insights into the reaction mechanism and human inherited disease, J. Biol. Chem. 277, 18134-18142.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18134-18142
    • Fu, Z.1    Wang, M.2    Potter, D.3    Miziorko, H.M.4    Kim, J.J.5
  • 26
    • 0029410712 scopus 로고
    • Mapping the transition state for ATP hydrolysis: Implications for enzymatic catalysis
    • Admiraal, S. J., and Herschlag, D. (1995) Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis, Chem. Biol. 2, 729-739.
    • (1995) Chem. Biol. , vol.2 , pp. 729-739
    • Admiraal, S.J.1    Herschlag, D.2
  • 27
    • 0031052035 scopus 로고    scopus 로고
    • Identification and functional characterization of an active-site lysine in mevalonate kinase
    • Potter, D., Wojnar, J. M., Narasimhan, C., and Miziorko, H. M. (1997) Identification and functional characterization of an active-site lysine in mevalonate kinase, J. Biol. Chem. 272, 5741-5746.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5741-5746
    • Potter, D.1    Wojnar, J.M.2    Narasimhan, C.3    Miziorko, H.M.4
  • 28
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz, G. E. (1992) Binding of nucleotides by proteins, Curr. Opin. Struct. Biol. 2, 61-67.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 29
    • 0035918177 scopus 로고    scopus 로고
    • Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate binding motif and a site implicated in human inherited disease
    • Cho, Y. K., Rios, S. E., Kim, J. J., and Miziorko, H. M. (2001) Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate binding motif and a site implicated in human inherited disease, J. Biol. Chem. 276, 12573-12578.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12573-12578
    • Cho, Y.K.1    Rios, S.E.2    Kim, J.J.3    Miziorko, H.M.4
  • 30
    • 0022634509 scopus 로고
    • Mevalonic aciduria - An inborn error of cholesterol and nonsterol isoprene biosynthesis
    • Hoffmann, G., Gibson, K. M., Brandt, I. K., Bader, P. I., Wappner, R. S., and Sweetman, L. (1986) Mevalonic aciduria - an inborn error of cholesterol and nonsterol isoprene biosynthesis, N. Engl. J. Med. 314, 1610-1614.
    • (1986) N. Engl. J. Med. , vol.314 , pp. 1610-1614
    • Hoffmann, G.1    Gibson, K.M.2    Brandt, I.K.3    Bader, P.I.4    Wappner, R.S.5    Sweetman, L.6
  • 32
    • 0030671277 scopus 로고    scopus 로고
    • Identification of an active site alanine in mevalonate kinase through characterization of a novel mutation in mevalonate kinase deficiency
    • Hinson, D. D., Chambliss, K. L., Hoffmann, G. F., Krisans, S., Keller, R. K., and Gibson, K. M. (1997) Identification of an active site alanine in mevalonate kinase through characterization of a novel mutation in mevalonate kinase deficiency, J. Biol. Chem. 272, 26756-26760.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26756-26760
    • Hinson, D.D.1    Chambliss, K.L.2    Hoffmann, G.F.3    Krisans, S.4    Keller, R.K.5    Gibson, K.M.6
  • 33
    • 0035969875 scopus 로고    scopus 로고
    • The role of aldose reductase in sugar cataract formation: Aldose reductase plays a key role in lens epithelial cell death (apoptosis)
    • Murata, M., Ohta, N., Sakurai, S., Alam, S., Tsai, J., Kador, P. F., and Sato, S. (2001) The role of aldose reductase in sugar cataract formation: aldose reductase plays a key role in lens epithelial cell death (apoptosis), Chem.-Biol. Interact. 130-132, 617-625.
    • (2001) Chem.-Biol. Interact. , vol.130-132 , pp. 617-625
    • Murata, M.1    Ohta, N.2    Sakurai, S.3    Alam, S.4    Tsai, J.5    Kador, P.F.6    Sato, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.