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Volumn 11, Issue 4, 1997, Pages 217-226

Chemical arrows for enzymatic targets

Author keywords

adenylosuccinate synthetase; affinity cleavage; enzyme; glutamate dehydrogenase; isocitrate dehydrogenase

Indexed keywords

ADENYLOSUCCINATE LYASE; ADENYLOSUCCINATE SYNTHASE; ENZYME; GLUTAMATE DEHYDROGENASE; GLUTATHIONE TRANSFERASE; ISOCITRATE DEHYDROGENASE; NUCLEOTIDE DERIVATIVE;

EID: 0030932349     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.4.9068610     Document Type: Review
Times cited : (18)

References (27)
  • 1
    • 0020696906 scopus 로고
    • Affinity labeling of purine nucleotide sites in proteins
    • Colman, R. F. (1983) Affinity labeling of purine nucleotide sites in proteins. Annu. Rev. Biochem. 52, 67-91
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 67-91
    • Colman, R.F.1
  • 2
    • 77956937268 scopus 로고
    • Site-specific modification of enzyme sites
    • Colman, R. F. (1990) Site-specific modification of enzyme sites. Enzymes 19, 283-321
    • (1990) Enzymes , vol.19 , pp. 283-321
    • Colman, R.F.1
  • 3
    • 0022428168 scopus 로고
    • 2-[(4-Bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate, a new nucleotide analogue that acts as an affinity label of pyruvate kinase
    • Kapetanovic, E., Bailey, J. M., and Colman, R. F. (1985) 2-[(4-Bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate, a new nucleotide analogue that acts as an affinity label of pyruvate kinase. Biochemistry 24, 7586-7593
    • (1985) Biochemistry , vol.24 , pp. 7586-7593
    • Kapetanovic, E.1    Bailey, J.M.2    Colman, R.F.3
  • 5
    • 0027240254 scopus 로고
    • Expression, purification and kinetic characterization of recombinant human adenylosuccinate lyase
    • Stone, R. L., Zalkin, H., and Dixon, J. K. (1993) Expression, purification and kinetic characterization of recombinant human adenylosuccinate lyase. J. Biol. Chem. 268, 19710-19716
    • (1993) J. Biol. Chem. , vol.268 , pp. 19710-19716
    • Stone, R.L.1    Zalkin, H.2    Dixon, J.K.3
  • 6
    • 0029874233 scopus 로고    scopus 로고
    • Affinity labeling of the active site of rabbit muscle adenylosuccinate lyase by 2-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate
    • Gite, S. U., and Colman, R. F. (1996) Affinity labeling of the active site of rabbit muscle adenylosuccinate lyase by 2-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate. Biochemistry 35, 2658-2667
    • (1996) Biochemistry , vol.35 , pp. 2658-2667
    • Gite, S.U.1    Colman, R.F.2
  • 7
    • 0016651874 scopus 로고
    • Reversible modification of arginine residues
    • Patthy, L., and Smith, K. L. (1975) Reversible modification of arginine residues. J. Biol. Chem. 250, 557-564
    • (1975) J. Biol. Chem. , vol.250 , pp. 557-564
    • Patthy, L.1    Smith, K.L.2
  • 9
    • 4344566056 scopus 로고    scopus 로고
    • Identification of His-141 in the active of B. subtilis adenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutylthio)adenosine 5′-monophosphate
    • abstr.
    • Lee, T. L., Dixon, J. E., and Colman, R. F. (1996) Identification of His-141 in the active of B. subtilis adenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutylthio)adenosine 5′-monophosphate. FASEB J. 10, A1101 (abstr.)
    • (1996) FASEB J. , vol.10
    • Lee, T.L.1    Dixon, J.E.2    Colman, R.F.3
  • 10
    • 0020668139 scopus 로고
    • Regulation, genetics and properties of adenylosuccinate synthetase: A review
    • Stayton, M. M., Rudolph, F. G., and Fromm, H. J. (1983) Regulation, genetics and properties of adenylosuccinate synthetase: A review. Curr. Top. Cell. Regul. 32, 103-141
    • (1983) Curr. Top. Cell. Regul. , vol.32 , pp. 103-141
    • Stayton, M.M.1    Rudolph, F.G.2    Fromm, H.J.3
  • 11
    • 0027444661 scopus 로고
    • Crystal structure of adenylosuccinate synthetase from E. coli. Evidence for convergent evolution of GTP-binding domains
    • Poland, B. W., Silva, M. M., Serra, M. M., Cho, Y., Kim, K. H., Harris, E. M. S., and Honzatko, R. B. (1993) Crystal structure of adenylosuccinate synthetase from E. coli. Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 268, 25334-25342
    • (1993) J. Biol. Chem. , vol.268 , pp. 25334-25342
    • Poland, B.W.1    Silva, M.M.2    Serra, M.M.3    Cho, Y.4    Kim, K.H.5    Harris, E.M.S.6    Honzatko, R.B.7
  • 12
    • 0029953044 scopus 로고    scopus 로고
    • Involvement of Arg-143 in nucleotide substrate binding at the active site of adenylosuccinate synthetase from E. coli
    • Moe, O. A., Baker-Malcolm, J. F., Wang, W., Kang, C., Fromm, H. J., and Colman, R. F. (1996) Involvement of Arg-143 in nucleotide substrate binding at the active site of adenylosuccinate synthetase from E. coli. Biochemistry 35, 9024-9033
    • (1996) Biochemistry , vol.35 , pp. 9024-9033
    • Moe, O.A.1    Baker-Malcolm, J.F.2    Wang, W.3    Kang, C.4    Fromm, H.J.5    Colman, R.F.6
  • 13
    • 0028240325 scopus 로고
    • Guanosine 5′-O-[S-(4-bromo-2,3-dioxobutyl)]thiophosphate and adenosine 5′-O-[S-(4-bromo-2,3-dioxobutyl)]thiophosphate: New nucleotide affinity labels which react with rabbit muscle pyruvate kinase
    • Vollmer, S. H., Walner, M. B., Tarbell, K. V., and Colman, R. F. (1994) Guanosine 5′-O-[S-(4-bromo-2,3-dioxobutyl)]thiophosphate and adenosine 5′-O-[S-(4-bromo-2,3-dioxobutyl)]thiophosphate: New nucleotide affinity labels which react with rabbit muscle pyruvate kinase. J. Biol. Chem. 269, 8082-8090.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8082-8090
    • Vollmer, S.H.1    Walner, M.B.2    Tarbell, K.V.3    Colman, R.F.4
  • 14
    • 0028007435 scopus 로고
    • Activation of bovine liver glutamate dehydrogenase by covalent reaction of adenosine 5′-O-[S-4-bromo-2,3-dioxobutylthiophosphale] with arginine-459 at an ADP regulatory site
    • Wrzeszczynski, K. O., and Colman, R. F. (1994) Activation of bovine liver glutamate dehydrogenase by covalent reaction of adenosine 5′-O-[S-4-bromo-2,3-dioxobutyl)thiophosphale] with arginine-459 at an ADP regulatory site. Biochemistry 33, 11544-11553
    • (1994) Biochemistry , vol.33 , pp. 11544-11553
    • Wrzeszczynski, K.O.1    Colman, R.F.2
  • 15
    • 0024434696 scopus 로고
    • 5′-p-Fluorosulfonylbenzoyl-8-azidoadenosine: A new bifunctional affinity label for nucleotide binding sites in proteins
    • Dombrowski, K. E., and Colman, R. F. (1989) 5′-p-Fluorosulfonylbenzoyl-8-azidoadenosine: A new bifunctional affinity label for nucleotide binding sites in proteins. Arch. Biochem. Biophys. 275, 302-308
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 302-308
    • Dombrowski, K.E.1    Colman, R.F.2
  • 16
    • 0026652145 scopus 로고
    • Identification of amino acids modified by the bifunctional affinity label 5′-p-(fluorosulfonylbenzoyl)-8-azidoadenosine in the reduced coenzyme site of bovine liver glutamate dehydrogenase
    • Dombrowski, K. E., Huang, Y.-C., and Colman, R. F. (1992) Identification of amino acids modified by the bifunctional affinity label 5′-p-(fluorosulfonylbenzoyl)-8-azidoadenosine in the reduced coenzyme site of bovine liver glutamate dehydrogenase. Biochemistry 31, 3785-3793
    • (1992) Biochemistry , vol.31 , pp. 3785-3793
    • Dombrowski, K.E.1    Huang, Y.-C.2    Colman, R.F.3
  • 17
    • 0026652838 scopus 로고
    • Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase
    • Haselbeck, R. J., Colman, R. F., and McAlister-Henn, L. (1992) Isolation and sequence of a cDNA encoding porcine mitochondrial NADP-specific isocitrate dehydrogenase. Biochemistry 31, 6219-6223
    • (1992) Biochemistry , vol.31 , pp. 6219-6223
    • Haselbeck, R.J.1    Colman, R.F.2    McAlister-Henn, L.3
  • 20
    • 0024269217 scopus 로고
    • Glutathione transferases -structure and catalytic activity
    • Mannervik, B., and Danielson, U. H. (1988) Glutathione transferases -structure and catalytic activity. CRC Crit. Rev. Biochem. 23, 283-337
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 22
    • 0026460365 scopus 로고
    • The three-dimensional structure of a glutalhione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution
    • Ji, X., Zhang, P., Armstrong, R. N., and Gilliland, G. L. (1992) The three-dimensional structure of a glutalhione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution. Biochemistry 31, 10169-10184
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 23
    • 0026722795 scopus 로고
    • Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution
    • Reinemer, P., Dirr, H. W., Ladenstein, R., Huber, R., LoBello, M., Federici, G., and Parker, M. W. (1992) Three-dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227, 214-226.
    • (1992) J. Mol. Biol. , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    LoBello, M.5    Federici, G.6    Parker, M.W.7
  • 24
    • 0026320285 scopus 로고
    • S-(4-Bromo-2,3-dioxobutyl)glutathione: A new affinity label for the 4-4 isoenzyme of rat liver glutathione S-transferase
    • Katusz, R. M., and Colman, R. F. (1991) S-(4-Bromo-2,3-dioxobutyl)glutathione: A new affinity label for the 4-4 isoenzyme of rat liver glutathione S-transferase. Biochemistry 30, 11230-11238
    • (1991) Biochemistry , vol.30 , pp. 11230-11238
    • Katusz, R.M.1    Colman, R.F.2
  • 25
    • 0026613704 scopus 로고
    • Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3
    • Katusz, R. M., Bono, B., and Colman, R. F. (1992) Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3. Arch. Biochem. Biophys. 298, 667-677
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 667-677
    • Katusz, R.M.1    Bono, B.2    Colman, R.F.3
  • 26
    • 0027769771 scopus 로고
    • 115 to be an important determinant of xenobiotic substrate specificity
    • 115 to be an important determinant of xenobiotic substrate specificity. Biochemistry 32, 13002-13011
    • (1993) Biochemistry , vol.32 , pp. 13002-13011
    • Barycki, J.J.1    Colman, R.F.2
  • 27
    • 0029127173 scopus 로고
    • Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase. 3-3
    • Hu, L., and Colman, R. F. (1995) Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase. 3-3. J. Biol. Chem. 270, 21875-21883
    • (1995) J. Biol. Chem. , vol.270 , pp. 21875-21883
    • Hu, L.1    Colman, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.