dc.relation.reference | Agbo-Kpati, P., C. Frossard, et al. (1999). "[Isolated and persistent elevation and of transaminases (aspartate aminotransferase) using a macroenzyme]." Arch Pediatr 6(5): 590-1.
Arnone, M. I., L. Birolo, et al. (1992). "Expression of a hyperthermophilic aspartate aminotransferase in Escherichia coli." Biochim Biophys Acta 1160(2): 206-12.
Arnone, M. I., L. Birolo, et al. (1997). "Stability of aspartate aminotransferase from Sulfolobus solfataricus." Protein Eng 10(3): 237-48.
Arrio-Dupont, M., I. Cournil, et al. (1970). "L-aspartate aminotransferase: Protection against the formation of multiple forms." FEBS Lett 11(2): 144-146.
Artigues, A., D. L. Crawford, et al. (1998). "Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase. Implications for their segregation to different cellular compartments." J Biol Chem 273(50): 33130-4.
Birchmeier, W. and P. Christen (1971). "Chemical evidence for syncatalytic conformational changes in aspartate aminotransferase." FEBS Lett 18(2): 209-213.
Birolo, L., M. I. Arnone, et al. (1991). "The active site of Sulfolobus solfataricus aspartate aminotransferase." Biochim Biophys Acta 1080(3): 198-204.
Birolo, L., V. N. Malashkevich, et al. (1999). "Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase." Biochemistry 38(3): 905-13.
Bradbury, M. W. and P. D. Berk (2000). "Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA." Biochem J 345 Pt 3: 423-7.
Chow, M. A., K. E. McElroy, et al. (2004). "Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase." Biochemistry 43(40): 12780-7.
Christen, P., R. Jaussi, et al. (1990). "Evolutionary and biosynthetic aspects of aspartate aminotransferase isoenzymes and other aminotransferases." Ann N Y Acad Sci 585: 331-8.
Chothia, C. and A. M. Lesk (1986). "The relation between the divergence of sequence and structure in proteins." Embo J 5(4): 823-6.
Cubellis, M. V., M. I. Arnone, et al. (1993). "Comparative studies on thermophilicity and thermostability of aspartate aminotransferases." Biotechnol Appl Biochem 18 (Pt 3): 417-25.
Daly, M. J. and K. W. Minton (1997). "Recombination between a resident plasmid and the chromosome following irradiation of the radioresistant bacterium Deinococcus radiodurans." Gene 187(2): 225-9.
Deu, E., K. A. Koch, et al. (2002). "The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants." Protein Sci 11(5): 1062-73.
Friedecky, B., J. Kratochvila, et al. (1996). "Influence of the presence or absence of pyridoxal-5'-phosphate in control sera on the interlaboratory comparability in measuring aspartate aminotransferase catalytic concentration." Eur J Clin Chem Clin Biochem 34(12): 981-2.
Goto, M., R. Omi, et al. (2004). "Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition." J Biol Chem 279(16): 16518-25.
Hayashi, H. and H. Kagamiyama (1997). "Transient-state kinetics of the reaction of aspartate aminotransferase with aspartate at low pH reveals dual routes in the enzyme-substrate association process." Biochemistry 36(44): 13558-69.
Hayashi, H., H. Mizuguchi, et al. (1998). "The imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis." Biochemistry 37(43): 15076-85.
Hayashi, H., H. Mizuguchi, et al. (1999). "The imine-pyridine torsion of the pyridoxal 5'-phosphate schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis." Biochemistry 38(2): 854.
Hayashi, H., H. Mizuguchi, et al. (2003). "Strain and catalysis in aspartate aminotransferase." Biochim Biophys Acta 1647(1-2): 103-9.
Hayashi, H., H. Mizuguchi, et al. (2003). "Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis." J Biol Chem 278(11): 9481-8.
Iriarte, A., H. A. Farach, Jr., et al. (1984). "Coenzyme active site occupancy as an indicator of independence of the subunits of mitochondrial aspartate aminotransferase." J Biol Chem 259(11): 7003-10.
Jeffery, C. J., T. Barry, et al. (1998). "Crystallization and preliminary X-ray diffraction analysis of aspartate aminotransferase from Saccharomyces cerevisiae." Acta Crystallogr D Biol Crystallogr 54 (Pt 4): 659-61.
Jeffery, C. J., L. M. Gloss, et al. (2000). "The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase." Protein Eng 13(2): 105-12.
Jensen, R. A. and W. Gu (1996). "Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases." J Bacteriol 178(8): 2161-71.
Katsura, Y., M. Shirouzu, et al. (2004). "Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV." Proteins 55(3): 487-92.
Kim, H., K. Ikegami, et al. (2003). "Characterization of aspartate aminotransferase from the cyanobacterium Phormidium lapideum." Biosci Biotechnol Biochem 67(3): 490-8.
Kochkina, V. M. (1998). "[Enzymatic activity of aspartate aminotransferase crystals]." Mol Biol (Mosk) 32(3): 460-2.
Mahon, M. M., R. Graber, et al. (1999). "The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction." Biochim Biophys Acta 1434(1): 191-201.
Marino, G., G. Nitti, et al. (1988). "Purification and characterization of aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus." J Biol Chem 263(25): 12305-9.
Martins, L. L., M. P. Mourato, et al. (2001). "Effects of substrate structural analogues on the enzymatic activities of aspartate aminotransferase isoenzymes." J Enzyme Inhib 16(3): 251-7.
Matharu, A., H. Hayashi, et al. (2001). "Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase." Eur J Biochem 268(6): 1640-5.
Mehta, P. K., T. I. Hale, et al. (1993). "Aminotransferases: demonstration of homology and division into evolutionary subgroups." Eur J Biochem 214(2): 549-61.
Mehta, P. K. and P. Christen (2000). "The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes." Adv Enzymol Relat Areas Mol Biol 74: 129-84.
Minton, K. W. (1994). "DNA repair in the extremely radioresistant bacterium Deinococcus radiodurans." Mol Microbiol 13(1): 9-15.
Minton, K. W. (1996). "Repair of ionizing-radiation damage in the radiation resistant bacterium Deinococcus radiodurans." Mutat Res 363(1): 1-7.Mahon, M. M., R. Graber, et al. (1999). "The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction." Biochim Biophys Acta 1434(1): 191-201.
Mizuguchi, H., H. Hayashi, et al. (2001). "Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase." Biochemistry 40(2): 353-60.
Mollova, E. T., D. E. Metzler, et al. (1997). "Use of 1H-15N heteronuclear multiple-quantum coherence NMR spectroscopy to study the active site of aspartate aminotransferase." Biochemistry 36(3): 615-25.
Nakai, T., K. Okada, et al. (1998). "Crystallization and preliminary X-ray characterization of aspartate aminotransferase from an extreme thermophile, Thermus thermophilus HB8." Acta Crystallogr D Biol Crystallogr 54 (Pt 5): 1032-4.
Nobe, Y., S. Kawaguchi, et al. (1998). "The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8." J Biol Chem 273(45): 29554-64.
O'Farrell, P. A., G. Sannia, et al. (1997). "Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1." Biochem Biophys Res Commun 239(3): 810-5.
Okamoto, A., R. Kato, et al. (1996). "An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8." J Biochem (Tokyo) 119(1): 135-44.
Ovchinnikov, Y. A., C. A. Egorov, et al. (1973). "The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart." FEBS Lett 29(1): 31-34.
Plee-Gautier, E., M. Aggerbeck, et al. (1998). "Identification of an adipocyte-specific negative glucose response region in the cytosolic aspartate aminotransferase gene." Endocrinology 139(12): 4936-44.
Plee-Gautier, E., H. Grimal, et al. (1998). "Cytosolic aspartate aminotransferase gene is a member of the glucose-regulated protein gene family in adipocytes." Biochem J 329 (Pt 1): 37-40.
Rhee, S., M. M. Silva, et al. (1997). "Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate." J Biol Chem 272(28): 17293-302.
Sung, M. H., K. Tanizawa, et al. (1991). "Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization." J Biol Chem 266(4): 2567-72.
Sung, M. H., K. Tanizawa, et al. (1990). "Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species." J Bacteriol 172(3): 1345-51.
Tanaka, T., S. Yamamoto, et al. (1994). "Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family." J Biochem (Tokyo) 115(2): 309-17.
Tanaka, T., S. Yamamoto, et al. (1992). "Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures." J Biochem (Tokyo) 112(6): 811-5.
Thompson, B. G. and R. G. Murray (1981). "Isolation and characterization of the plasma membrane and the outer membrane of Deinococcus radiodurans strain Sark." Can J Microbiol 27(7): 729-34.
Ura, H., K. Harata, et al. (2001). "Temperature dependence of the enzyme-substrate recognition mechanism." J Biochem (Tokyo) 129(1): 173-8.
Ura, H., T. Nakai, et al. (2001). "Substrate recognition mechanism of thermophilic dual-substrate enzyme." J Biochem (Tokyo) 130(1): 89-98.
Venkateswaran, A., S. C. McFarlan, et al. (2000). "Physiologic determinants of radiation resistance in Deinococcus radiodurans." Appl Environ Microbiol 66(6): 2620-6.
Vacca, R. A., S. Giannattasio, et al. (1997). "Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase." J Biol Chem 272(35): 21932-7.
Von Stosch, A. G. (1996). "Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate." Biochemistry 35(48): 15260-8.
Watson, R. J. and V. K. Rastogi (1993). "Cloning and nucleotide sequencing of Rhizobium meliloti aminotransferase genes: an aspartate aminotransferase required for symbiotic nitrogen fixation is atypical." J Bacteriol 175(7): 1919-28.
White, O., J. A. Eisen, et al. (1999). "Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." Science 286(5444): 1571-7.
Yano, T., S. Oue, et al. (1998). "Directed evolution of an aspartate aminotransferase with new substrate specificities." Proc Natl Acad Sci U S A 95(10): 5511-5.
Zufarova, et al. (1972). "Identification of the functionally important cysteinyl residue in pig heart aspartate aminotransferase." FEBS Lett 28(3): 302-304. | en |