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Volumn 134, Issue 5, 2003, Pages 731-738

Interaction between Pyridoxal Kinase and Pyridoxal-5-phosphate-Dependent Enzymes

Author keywords

Alanine aminotransferase; Glutamate decarboxylase; Pyridoxal kinase; Pyridoxal 5 phosphate dependent protein; Surface plasmon resonance

Indexed keywords

ALANINE AMINOTRANSFERASE; GLUTAMATE DECARBOXYLASE; PYRIDOXAL 5 PHOSPHATE; PYRIDOXAL KINASE;

EID: 0347993776     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg201     Document Type: Article
Times cited : (22)

References (32)
  • 1
    • 0001062975 scopus 로고
    • (Machlin, L.J., ed.), Marcel Dekker, New York
    • 6 in Handbook of Vitamins (Machlin, L.J., ed.) pp. 341-392, Marcel Dekker, New York
    • (1991) 6 in Handbook of Vitamins , pp. 341-392
    • Leklem, J.E.1
  • 3
    • 0036303304 scopus 로고    scopus 로고
    • Functional attributes of the phosphate group binding cup of pyridoxal phosphate-dependent enzymes
    • Denesyuk, A.I., Denessiouk, K.A., Korpela, T., and Johnson, M.S. (2002) Functional attributes of the phosphate group binding cup of pyridoxal phosphate-dependent enzymes. J. Mol. Biol. 316, 155-172
    • (2002) J. Mol. Biol. , vol.316 , pp. 155-172
    • Denesyuk, A.I.1    Denessiouk, K.A.2    Korpela, T.3    Johnson, M.S.4
  • 4
    • 0032934972 scopus 로고    scopus 로고
    • Update on interconversions of vitamin B-6 with its coenzyme
    • McCormick, D.B. and Chen, H.J. (1999) Update on interconversions of vitamin B-6 with its coenzyme. J. Nutr. 129, 325-327
    • (1999) J. Nutr. , vol.129 , pp. 325-327
    • McCormick, D.B.1    Chen, H.J.2
  • 5
    • 0001703708 scopus 로고
    • Pyridoxal phosphokinases I. Assay, distribution, purification and properties
    • McCormick, D.B., Gregory, M.E., and Snell, E.E. (1961) Pyridoxal phosphokinases I. assay, distribution, purification and properties. J. Biol. Chem. 236, 2076-2082
    • (1961) J. Biol. Chem. , vol.236 , pp. 2076-2082
    • McCormick, D.B.1    Gregory, M.E.2    Snell, E.E.3
  • 7
    • 2242483774 scopus 로고    scopus 로고
    • Crystal structure of brain pyridoxal kinase, a novel member of the ribokinase superfamily
    • Li, M.H., Kwok, F.W., Chang, R., Lau, C.K., Zhang, J.P., Lo, S.C.L., Jiang, T.D., and Liang, C. (2002) Crystal structure of brain pyridoxal kinase, a novel member of the ribokinase superfamily. J. Biol. Chem. 277, 46385-46390
    • (2002) J. Biol. Chem. , vol.277 , pp. 46385-46390
    • Li, M.H.1    Kwok, F.W.2    Chang, R.3    Lau, C.K.4    Zhang, J.P.5    Lo, S.C.L.6    Jiang, T.D.7    Liang, C.8
  • 9
    • 0030417969 scopus 로고    scopus 로고
    • + on the catalytic activity of human erythrocyte pyridoxal kinase
    • + on the catalytic activity of human erythrocyte pyridoxal kinase. Enzyme Protein 49, 291-304
    • (1996) Enzyme Protein , vol.49 , pp. 291-304
    • Laine-Cessac, P.1    Allain, P.2
  • 10
    • 0036538611 scopus 로고    scopus 로고
    • Study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor
    • Fong, C.C., Lai, W.P., Leung, Y.C., Lo, S.C.L., Wong, M.S., and Yang, M. (2002) Study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor. Biochim. Biophys. Acta 1596, 95-107
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 95-107
    • Fong, C.C.1    Lai, W.P.2    Leung, Y.C.3    Lo, S.C.L.4    Wong, M.S.5    Yang, M.6
  • 11
    • 0344029122 scopus 로고
    • Enzymatic oxidation of pyridoxamine phosphate to pyridoxal phosphate in rabbit liver
    • Pogell, B.M. (1958) Enzymatic oxidation of pyridoxamine phosphate to pyridoxal phosphate in rabbit liver. J. Biol. Chem. 232, 761-776
    • (1958) J. Biol. Chem. , vol.232 , pp. 761-776
    • Pogell, B.M.1
  • 12
    • 85012583553 scopus 로고
    • 6
    • (Florkin, M. and Stotz, E.H., eds.), Elsevier, New York
    • 6 in Comprehensive Biochemistry (Florkin, M. and Stotz, E.H., eds.) Vol. 21, pp. 47-67, Elsevier, New York
    • (1971) Comprehensive Biochemistry , vol.21 , pp. 47-67
    • Snell, E.E.1    Haskell, B.E.2
  • 13
    • 0023761252 scopus 로고
    • Interactions of pyridoxal kinase and aspartate aminotransferase emission anisotropy and compartmentation studies
    • Kim, Y.T., Kwok, F., and Churchich, J.E. (1988) Interactions of pyridoxal kinase and aspartate aminotransferase emission anisotropy and compartmentation studies. J. Biol. Chem. 263, 13712-13717
    • (1988) J. Biol. Chem. , vol.263 , pp. 13712-13717
    • Kim, Y.T.1    Kwok, F.2    Churchich, J.E.3
  • 14
    • 0014955663 scopus 로고
    • Chemical and physical properties of Escherichia coli glutamate decarboxylase
    • Strausbauch, P.H. and Fischer, E.H. (1970) Chemical and physical properties of Escherichia coli glutamate decarboxylase. Biochemistry 9, 226-233
    • (1970) Biochemistry , vol.9 , pp. 226-233
    • Strausbauch, P.H.1    Fischer, E.H.2
  • 15
    • 0014955684 scopus 로고
    • Structure of the binding site of pyridoxal 5′-phosphate to Escherichia coli glutamate decarboxylase
    • Strausbauch, P.H. and Fischer, E.H. (1970) Structure of the binding site of pyridoxal 5′-phosphate to Escherichia coli glutamate decarboxylase. Biochemistry 9, 233-238
    • (1970) Biochemistry , vol.9 , pp. 233-238
    • Strausbauch, P.H.1    Fischer, E.H.2
  • 17
    • 0016686118 scopus 로고
    • Metabolic implications of the distribution of the alanine aminotransferase isoenzymes
    • DeRosa, G. and Swick, R.W. (1975) Metabolic implications of the distribution of the alanine aminotransferase isoenzymes. J. Biol. Chem. 250, 7961-7967
    • (1975) J. Biol. Chem. , vol.250 , pp. 7961-7967
    • DeRosa, G.1    Swick, R.W.2
  • 18
    • 0026510734 scopus 로고
    • Analysis of macromolecular interactions using immobilized ligands
    • Chaiken, I., Rose, S., and Karlsson, R. (1992) Analysis of macromolecular interactions using immobilized ligands. Analy. Biochem. 201, 197-210
    • (1992) Analy. Biochem. , vol.201 , pp. 197-210
    • Chaiken, I.1    Rose, S.2    Karlsson, R.3
  • 19
    • 0002747447 scopus 로고
    • A non-label technology for real-time biospecific interaction analysis in Techniques
    • (Villafranca, J.J. ed.), Academic Press, New York
    • Fägerstam, L. (1991) A non-label technology for real-time biospecific interaction analysis in Techniques in Protein Chemistry II (Villafranca, J.J. ed.) pp. 65-71, Academic Press, New York
    • (1991) Protein Chemistry II , pp. 65-71
    • Fägerstam, L.1
  • 20
    • 0004274707 scopus 로고    scopus 로고
    • Biacore AB, Uppsala, Sweden
    • BIAtechnology Handbook, Biacore AB, Uppsala, Sweden
    • BIAtechnology Handbook
  • 21
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Myszka, D.G. (1997) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8, 50-57
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 50-57
    • Myszka, D.G.1
  • 22
    • 0030070499 scopus 로고    scopus 로고
    • Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor. I. A computer simulation of the influence of mass transport
    • Schuck, P. (1996) Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor. I. A computer simulation of the influence of mass transport. Biophys. J. 70, 1230-1249
    • (1996) Biophys. J. , vol.70 , pp. 1230-1249
    • Schuck, P.1
  • 23
    • 0346593302 scopus 로고    scopus 로고
    • Phamacia Biosensor AB Press, Uppasla, Sweden
    • BIAcore X Instrument Handbook, Phamacia Biosensor AB Press, Uppasla, Sweden
    • BIAcore X Instrument Handbook
  • 24
    • 0032973842 scopus 로고    scopus 로고
    • Biosensor measurement of the interaction kinetics between insulin-like growth factors and their binding proteins
    • Wong, M.S., Fong, C.C., and Yang, M. (1999) Biosensor measurement of the interaction kinetics between insulin-like growth factors and their binding proteins. Biochim. Biophys. Acta 1432, 293-301
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 293-301
    • Wong, M.S.1    Fong, C.C.2    Yang, M.3
  • 25
    • 0035823108 scopus 로고    scopus 로고
    • Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor
    • Huang, M., Lai, W.P., Wong, M.S., and Yang, M. (2001) Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor. FEBS Lett. 505, 31-36
    • (2001) FEBS Lett. , vol.505 , pp. 31-36
    • Huang, M.1    Lai, W.P.2    Wong, M.S.3    Yang, M.4
  • 27
    • 0027978869 scopus 로고
    • Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors
    • Karlsson, R. (1994) Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors. Anal. Biochem. 221, 142-151
    • (1994) Anal. Biochem. , vol.221 , pp. 142-151
    • Karlsson, R.1
  • 29
    • 0016309392 scopus 로고
    • Regulation of pyridoxal 5′-phosphate metabolism in liver
    • Li, T.K., Lumeng, L., and Veitch, R.L. (1974) Regulation of pyridoxal 5′-phosphate metabolism in liver. Biochem. Biophys. Res. Commum. 61, 677-684
    • (1974) Biochem. Biophys. Res. Commum. , vol.61 , pp. 677-684
    • Li, T.K.1    Lumeng, L.2    Veitch, R.L.3
  • 30
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentrations of protein with surface plasmon resonance using radiolabeled proteins
    • Stenberg, E., Persson, B., Roos, H., and Urbaniczky, C. (1991) Quantitative determination of surface concentrations of protein with surface plasmon resonance using radiolabeled proteins. J. Coll. Interface Sci. 143, 513-526.
    • (1991) J. Coll. Interface Sci. , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 31
    • 0031863617 scopus 로고    scopus 로고
    • Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase
    • Qu, K., Martine, D.L., and Lawrence, C.E. (1998) Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase. Protein Sci. 7, 1092-1105
    • (1998) Protein Sci. , vol.7 , pp. 1092-1105
    • Qu, K.1    Martine, D.L.2    Lawrence, C.E.3
  • 32
    • 0026968975 scopus 로고
    • Evaluation of the holoenzyme content of aromatic L-amino acid decarboxylase in brain and liver tissues
    • Kawasaki, Y., Hayashi, H., Hatakeyama, K., and Kagamiyama, H. (1992) Evaluation of the holoenzyme content of aromatic L-amino acid decarboxylase in brain and liver tissues. Biochem. Biophys. Res. Commun. 186, 1242-1248
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1242-1248
    • Kawasaki, Y.1    Hayashi, H.2    Hatakeyama, K.3    Kagamiyama, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.