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Volumn 88, Issue 1-2, 1997, Pages 1-11

Characterization of Trypanosoma brucei pyridoxal kinase: Purification, gene isolation and expression in Escherichia coli

Author keywords

E. coli; Gene isolation; Pyridoxal kinase; T. brucei

Indexed keywords

PYRIDOXAL KINASE; PYRIDOXINE;

EID: 0030744397     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(97)00077-7     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0028138663 scopus 로고
    • American trypanosomiasis (Chagas' disease) and African trypanosomiasis (sleeping sickness)
    • Kirchhoff LV. American trypanosomiasis (Chagas' disease) and African trypanosomiasis (sleeping sickness). Curr Opin Infect Dis 1994;7:542-6.
    • (1994) Curr Opin Infect Dis , vol.7 , pp. 542-546
    • Kirchhoff, L.V.1
  • 2
    • 0028949538 scopus 로고
    • Molecular mechanisms and therapeutic approaches to the treatment of African Trypanosomiasis
    • Wang CC. Molecular mechanisms and therapeutic approaches to the treatment of African Trypanosomiasis. Annu Rev Pharmacol Toxicol 1995;35:93-127.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 93-127
    • Wang, C.C.1
  • 3
    • 0016774250 scopus 로고
    • Stable multisubstrate adducts as enzyme inhibitors: Potent inhibition of ornithine decarboxylase by N-(5′-phosphopyridoxyl)-ornithine
    • Heller JS, Canellakis ES, Bussolotti DL, Coward JK. Stable multisubstrate adducts as enzyme inhibitors: potent inhibition of ornithine decarboxylase by N-(5′-phosphopyridoxyl)-ornithine. Biochim Biophys Acta 1975;403:197-207.
    • (1975) Biochim Biophys Acta , vol.403 , pp. 197-207
    • Heller, J.S.1    Canellakis, E.S.2    Bussolotti, D.L.3    Coward, J.K.4
  • 4
    • 0001703708 scopus 로고
    • Pyridoxal phosphokinases: I. assay, distribution, purification and prpoerties
    • McCormick DB, Gregory MA, Snell EE. Pyridoxal phosphokinases: I. assay, distribution, purification and prpoerties. J Biol Chem 1961;236:2076-84.
    • (1961) J Biol Chem , vol.236 , pp. 2076-2084
    • McCormick, D.B.1    Gregory, M.A.2    Snell, E.E.3
  • 5
    • 0029015333 scopus 로고
    • Trypanosoma brucei brucei: Uptake and metabolism of pyridoxine and pyridoxal
    • Gray A. Trypanosoma brucei brucei: Uptake and metabolism of pyridoxine and pyridoxal. Exp Parasitol 1995;80:390-400.
    • (1995) Exp Parasitol , vol.80 , pp. 390-400
    • Gray, A.1
  • 6
    • 0025719391 scopus 로고
    • Uptake of N-(4′-pyridoxyl)amines and release by renal cells: A model for transporter-enhanced delivery of bioactive compounds
    • USA
    • Zhang A, McCormick DB. Uptake of N-(4′-pyridoxyl)amines and release by renal cells: a model for transporter-enhanced delivery of bioactive compounds. Proc Natl Acad Sci USA 1991;88:10407-10.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 10407-10410
    • Zhang, A.1    McCormick, D.B.2
  • 7
    • 0026639274 scopus 로고
    • Uptake and metabolism of N-(4′-pyridoxyl)amines by isolated rat liver cells
    • Zhang A, McCormick DB. Uptake and metabolism of N-(4′-pyridoxyl)amines by isolated rat liver cells. Arch Biochem Biophys 1992;294:394-7.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 394-397
    • Zhang, A.1    McCormick, D.B.2
  • 9
    • 0014940698 scopus 로고
    • Purification, properties, and a possilbe mechanism for pyridoxal kinase from bovien brain
    • Neary JT, Diven WF. Purification, properties, and a possilbe mechanism for pyridoxal kinase from bovien brain. J Biol Chem 1970;245:5585-93.
    • (1970) J Biol Chem , vol.245 , pp. 5585-5593
    • Neary, J.T.1    Diven, W.F.2
  • 10
    • 0022546623 scopus 로고
    • Brain pyridoxal kinase: Purification and characterization
    • Kerry JA, Rohde M, Kwok F. Brain pyridoxal kinase: purification and characterization. Eur J Biochem 1986;158:581-5.
    • (1986) Eur J Biochem , vol.158 , pp. 581-585
    • Kerry, J.A.1    Rohde, M.2    Kwok, F.3
  • 11
    • 0023642562 scopus 로고
    • Brain pyridoxal kinase dissociation of the dimeric structure and catalytic activity of the monomeric species
    • Kwok F, Scholz G, Churchich JE. Brain pyridoxal kinase dissociation of the dimeric structure and catalytic activity of the monomeric species. Eur J Biochem 1987;168:577-83.
    • (1987) Eur J Biochem , vol.168 , pp. 577-583
    • Kwok, F.1    Scholz, G.2    Churchich, J.E.3
  • 12
    • 0024323331 scopus 로고
    • Kinetic studies of the pyridoxal kinase from pig liver: Slow-binding inhibition by adenosine tetraphosphoyridoxal
    • Tagaya M, Yamano K, Fukui T. Kinetic studies of the pyridoxal kinase from pig liver: slow-binding inhibition by adenosine tetraphosphoyridoxal. Biochemistry 1989;28:4670-5.
    • (1989) Biochemistry , vol.28 , pp. 4670-4675
    • Tagaya, M.1    Yamano, K.2    Fukui, T.3
  • 13
    • 0020491271 scopus 로고
    • Nucleotide phosphorothioates as probes of the nucleotide binding site of brain pyridoxal kinase
    • Churchich JE, Wu C. Nucleotide phosphorothioates as probes of the nucleotide binding site of brain pyridoxal kinase. J Biol Chem 1982;257:12136-40.
    • (1982) J Biol Chem , vol.257 , pp. 12136-12140
    • Churchich, J.E.1    Wu, C.2
  • 14
    • 0023737213 scopus 로고
    • Affinity labeling of pyridoxal kinase with adenosine polyphosphopyridoxal
    • Dominici P, Scholz G, Kwok F, Churchich JE. Affinity labeling of pyridoxal kinase with adenosine polyphosphopyridoxal. J Biol Chem 1988;263:14712-6.
    • (1988) J Biol Chem , vol.263 , pp. 14712-14716
    • Dominici, P.1    Scholz, G.2    Kwok, F.3    Churchich, J.E.4
  • 15
    • 0025123494 scopus 로고
    • Binding of a photoaffinity analogue of pyridoxal to pyridoxal kinase
    • Scholz G, Kwok F, Churchich JE. Binding of a photoaffinity analogue of pyridoxal to pyridoxal kinase. Eur J Biochem 1990;193:479-84.
    • (1990) Eur J Biochem , vol.193 , pp. 479-484
    • Scholz, G.1    Kwok, F.2    Churchich, J.E.3
  • 16
    • 0025369708 scopus 로고
    • Pyridoxal kinase: Structure and function
    • Churchich JE, Kim YT. Pyridoxal kinase: structure and function. Ann NY Acad Sci 1990;585:357-67.
    • (1990) Ann NY Acad Sci , vol.585 , pp. 357-367
    • Churchich, J.E.1    Kim, Y.T.2
  • 17
    • 0030586254 scopus 로고    scopus 로고
    • Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia colt K-12
    • Yang Y, Zhao G, Winkler ME. Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia colt K-12. FEMS Microbiol Lett 1996;141:89-95.
    • (1996) FEMS Microbiol Lett , vol.141 , pp. 89-95
    • Yang, Y.1    Zhao, G.2    Winkler, M.E.3
  • 18
    • 0026161739 scopus 로고
    • The effects of the methylating agent 1,2-Bis(-methylsulfonyl)-1-methylhydrazine on morphology, DNA content and mitochondrial function of Try-panosoma brucei subspecies
    • Penketh PG, Divo AA, Shyam K, Patton CL, Sartorelli AC. The effects of the methylating agent 1,2-Bis(-methylsulfonyl)-1-methylhydrazine on morphology, DNA content and mitochondrial function of Try-panosoma brucei subspecies. J Protozool 1991;38:172-7.
    • (1991) J Protozool , vol.38 , pp. 172-177
    • Penketh, P.G.1    Divo, A.A.2    Shyam, K.3    Patton, C.L.4    Sartorelli, A.C.5
  • 19
    • 0022264053 scopus 로고
    • Cross-linking of the enzymes in the glycosomes of Trypanosoma brucei
    • Aman RA, Kenyon GL, Wang CC. Cross-linking of the enzymes in the glycosomes of Trypanosoma brucei. J Biol Chem 1985;260:6966-73.
    • (1985) J Biol Chem , vol.260 , pp. 6966-6973
    • Aman, R.A.1    Kenyon, G.L.2    Wang, C.C.3
  • 20
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphates
    • Wada H, Snell EE. The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J Biol Chem 1961;236:2089-95.
    • (1961) J Biol Chem , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 21
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of protein electroblotted onto polyvinylidene difuoride membrane
    • Matsudaira P. Sequence from picomole quantities of protein electroblotted onto polyvinylidene difuoride membrane. J Biol Chem 1987;262:10035-8.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 22
    • 0030016346 scopus 로고    scopus 로고
    • Characterization of try-panosoma brucei y-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione
    • Lueder DV, Phillips MA. Characterization of try-panosoma brucei y-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione. J Biol Chem 1996;271:17485-90.
    • (1996) J Biol Chem , vol.271 , pp. 17485-17490
    • Lueder, D.V.1    Phillips, M.A.2
  • 23
    • 0023219692 scopus 로고
    • Cloning and sequencing of the ornithine decarboxylase gene from Try panosoma brucei. implications for enzyme turnover and selective α-difluoromethylornithine inhibition
    • Phillips MA, Coffino P, Wang CC. Cloning and sequencing of the ornithine decarboxylase gene from Try panosoma brucei. implications for enzyme turnover and selective α-difluoromethylornithine inhibition. J Biol Chem 1987;262:8721-7.
    • (1987) J Biol Chem , vol.262 , pp. 8721-8727
    • Phillips, M.A.1    Coffino, P.2    Wang, C.C.3
  • 24
    • 0016800090 scopus 로고
    • A rapid method for determining sequences in dna by primed synthesis with dna polymerase
    • Sanger F, Coulson AR. A rapid method for determining sequences in dna by primed synthesis with dna polymerase. J Mol Biol 1975;94:441-8.
    • (1975) J Mol Biol , vol.94 , pp. 441-448
    • Sanger, F.1    Coulson, A.R.2
  • 25
    • 0028067923 scopus 로고
    • Formation of functional cross-species heterodimers of ornithine decarboxylase
    • Osterman A, Grishin NV, Kinch LN, Phillips MA. Formation of functional cross-species heterodimers of ornithine decarboxylase. Biochemistry 1994;33: 13662-7.
    • (1994) Biochemistry , vol.33 , pp. 13662-13667
    • Osterman, A.1    Grishin, N.V.2    Kinch, L.N.3    Phillips, M.A.4
  • 26
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • Parks PD, Leather KK, Howard ED, Johnston SA, Dougherty WG. Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal Biochem 1994;216:413-7.
    • (1994) Anal Biochem , vol.216 , pp. 413-417
    • Parks, P.D.1    Leather, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 27
    • 0029928836 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray studies of ornithine decarboxylase from Trypanosoma brucei
    • Grishin NV, Osterman AL, Goldsmith EJ, Phillips MA. Crystallization and preliminary x-ray studies of ornithine decarboxylase from Trypanosoma brucei. Proteins 1996;24:272-3.
    • (1996) Proteins , vol.24 , pp. 272-273
    • Grishin, N.V.1    Osterman, A.L.2    Goldsmith, E.J.3    Phillips, M.A.4
  • 28
    • 0024327315 scopus 로고
    • Proteolyitic cleavage of pyridoxal kinase into two structural domains
    • Dominici P, Kwok F, Churchich JE. Proteolyitic cleavage of pyridoxal kinase into two structural domains. Biochimie 1989;71:585-90.
    • (1989) Biochimie , vol.71 , pp. 585-590
    • Dominici, P.1    Kwok, F.2    Churchich, J.E.3
  • 29
    • 0029894593 scopus 로고    scopus 로고
    • Procyclic Trypanosoma brucei cell lines deficient in ornithine decarboxylase activity
    • Li F, Hua S-B, Wang CC, Gottesdiener KM. Procyclic Trypanosoma brucei cell lines deficient in ornithine decarboxylase activity. Mol Biochem Parasitol 1996;78:227-36.
    • (1996) Mol Biochem Parasitol , vol.78 , pp. 227-236
    • Li, F.1    Hua, S.-B.2    Wang, C.C.3    Gottesdiener, K.M.4
  • 30
    • 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, Valencia A. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci 1993;2:31-40.
    • (1993) Protein Sci , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 31
    • 0001607723 scopus 로고
    • Distantly related sequences in the α and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay N. Distantly related sequences in the α and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1982;1:945-51.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.4
  • 32
    • 0025048136 scopus 로고
    • The P-loop, a common motif in ATP- and GTP-binding proteins
    • Saraste M, Sibbald PR, Wittinghofer A. The P-loop, a common motif in ATP- and GTP-binding proteins. TIBS 1990;15:430-4.
    • (1990) TIBS , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 33
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin NV, Phillips MA, Goldsmith EJ. Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci 1995;4:1291-304.
    • (1995) Protein Sci , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 34
    • 0025776472 scopus 로고
    • 2+ by site-directed mutagenesis and proton, phosphorus-31, and magnesium-25 NMR
    • 2+ by site-directed mutagenesis and proton, phosphorus-31, and magnesium-25 NMR. Biochemistry 1991;30:5539-46.
    • (1991) Biochemistry , vol.30 , pp. 5539-5546
    • Yan, H.G.1    Tsai, M.D.2
  • 35
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story RM, Steitz TA. Structure of the recA protein-ADP complex. Nature 1992;355:374-6.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 36
    • 0025747939 scopus 로고
    • Arrangement of the substrates at the active site of brain pyridoxal kinase
    • Wolkers WF, Gregory JD, Churchich JE, Serpersu EH. Arrangement of the substrates at the active site of brain pyridoxal kinase. J Biol Chem 1991;266:20761-6.
    • (1991) J Biol Chem , vol.266 , pp. 20761-20766
    • Wolkers, W.F.1    Gregory, J.D.2    Churchich, J.E.3    Serpersu, E.H.4
  • 37
    • 0024601081 scopus 로고
    • Brain pyridoxal kinase: Photoaffinity labeling of the substrate-binding site
    • Scholz G, Kwok F. Brain pyridoxal kinase: photoaffinity labeling of the substrate-binding site. J Biol Chem 1989;264:4318-21.
    • (1989) J Biol Chem , vol.264 , pp. 4318-4321
    • Scholz, G.1    Kwok, F.2
  • 38
    • 0021634693 scopus 로고
    • Mechanism of action of aspartate amino-transterase proposed on the basis of its spatial structure
    • Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN. Mechanism of action of aspartate amino-transterase proposed on the basis of its spatial structure. J Mol Biol 1984;174:497-525.
    • (1984) J Mol Biol , vol.174 , pp. 497-525
    • Kirsch, J.F.1    Eichele, G.2    Ford, G.C.3    Vincent, M.G.4    Jansonius, J.N.5


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