메뉴 건너뛰기




Volumn 8, Issue 11, 1999, Pages 2406-2417

Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: Substrate specificity is influenced by cofactor binding mode

Author keywords

Chagas' disease; Pyridoxal 5' phosphate; Trypanosoma cruzi; Tyrosine aminotransferase; X ray crystallography

Indexed keywords

TYROSINE AMINOTRANSFERASE;

EID: 0032696346     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.11.2406     Document Type: Article
Times cited : (51)

References (83)
  • 1
    • 0028044574 scopus 로고
    • Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes
    • Alexander FM, Sandmeier E, Mehta PK, Christen, P. 1994. Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Eur J Biochem 219:953-960.
    • (1994) Eur J Biochem , vol.219 , pp. 953-960
    • Alexander, F.M.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4
  • 2
    • 0019898613 scopus 로고
    • Purification and properties of human liver tyrosine aminotransferase
    • Andersson SM, Pispa JP. 1982. Purification and properties of human liver tyrosine aminotransferase. Clin Chim Acta 125:117-123.
    • (1982) Clin Chim Acta , vol.125 , pp. 117-123
    • Andersson, S.M.1    Pispa, J.P.2
  • 3
    • 0002000553 scopus 로고
    • Ground state of sigma-bonded molecules. IV. M.I.N.D.O. method and its applications to hydrocarbons
    • Baird NC, Dewar MJS. 1969. Ground state of sigma-bonded molecules. IV. M.I.N.D.O. method and its applications to hydrocarbons. J Chem Phys 50:1262-1274.
    • (1969) J Chem Phys , vol.50 , pp. 1262-1274
    • Baird, N.C.1    Dewar, M.J.S.2
  • 4
    • 9244221583 scopus 로고    scopus 로고
    • Aromatic amino acid transamination and methionine recycling in trypanosomatids
    • Berger BJ, Dai WW, Wang H, Stark RE Cerami A. 1996. Aromatic amino acid transamination and methionine recycling in trypanosomatids. Proc Natl Acad Sci USA 93:4126-4130.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4126-4130
    • Berger, B.J.1    Dai, W.W.2    Wang, H.3    Stark, R.E.4    Cerami, A.5
  • 5
    • 0032468851 scopus 로고    scopus 로고
    • Methionine formation from α-ketomethiobutyrate in the trypanosomatid crithidia fasciculata
    • Berger BJ, Dai WW, Wilson J. 1998. Methionine formation from α-ketomethiobutyrate in the trypanosomatid Crithidia fasciculata. FEMS Microbiol Lett 165:305-312.
    • (1998) FEMS Microbiol Lett , vol.165 , pp. 305-312
    • Berger, B.J.1    Dai, W.W.2    Wilson, J.3
  • 7
    • 0027166777 scopus 로고
    • Isolation and characterization of a gene from Trypanosoma cruzi encoding a 46-kilodalton protein with homology to human and rat tyrosine aminotransferase
    • Bontempi EJ, Bua J, Aslund L, Porcel B, Segura EL, Henriksson J, Orn A, Pettersson U, Ruiz AM. 1993. Isolation and characterization of a gene from Trypanosoma cruzi encoding a 46-kilodalton protein with homology to human and rat tyrosine aminotransferase. Mol Biochem Parasitol 59:253-262.
    • (1993) Mol Biochem Parasitol , vol.59 , pp. 253-262
    • Bontempi, E.J.1    Bua, J.2    Aslund, L.3    Porcel, B.4    Segura, E.L.5    Henriksson, J.6    Orn, A.7    Pettersson, U.8    Ruiz, A.M.9
  • 9
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger AT, Krukowski A, Erickson J. 1990. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A46:585-593.
    • (1990) Acta Cryst. , vol.A46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.3
  • 10
    • 0027033271 scopus 로고
    • Energy metabolism in Trypanosoma cruzi
    • Cazzulo JJ. 1992. Energy metabolism in Trypanosoma cruzi. Subcell Biochem 18:235-57.
    • (1992) Subcell Biochem , vol.18 , pp. 235-257
    • Cazzulo, J.J.1
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computational Project No. 4). 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 13
    • 0010325305 scopus 로고
    • Transaminases of Leishmania donovani, the causative agent of Kala azar
    • Chatterjee AN, Ghosh JJ. 1957. Transaminases of Leishmania donovani, the causative agent of Kala azar. Nature 180:1425.
    • (1957) Nature , vol.180 , pp. 1425
    • Chatterjee, A.N.1    Ghosh, J.J.2
  • 14
    • 0015240657 scopus 로고
    • Crithidia fasciculata tyrosine aminotransferase
    • Constansas NS, Levis GM, Vakirtzi-Lemonias CS. 1971. Crithidia fasciculata tyrosine aminotransferase. Characterization and differentiation from alanine aminotransferase. Biochim Biophys Acta 230:137-145.
    • (1971) Biochim Biophys Acta , vol.230 , pp. 137-145
    • Constansas, N.S.1    Levis, G.M.2    Vakirtzi-Lemonias, C.S.3
  • 16
    • 0033106268 scopus 로고    scopus 로고
    • Remarks about protein structure precision
    • Cruickshank DWJ. 1999. Remarks about protein structure precision. Acta Crystallogr D55:583-601.
    • (1999) Acta Crystallogr , vol.D55 , pp. 583-601
    • Cruickshank, D.W.J.1
  • 17
    • 0026004665 scopus 로고
    • Expression of mammalian tyrosine aminotransferase in Saccharomyces cerevisiae and Escherichia coli. Purification to homogeneity and characterization of the enzyme overproduced in the bacteria
    • Dietrich JB, Lorber B, Kern D. 1991. Expression of mammalian tyrosine aminotransferase in Saccharomyces cerevisiae and Escherichia coli. Purification to homogeneity and characterization of the enzyme overproduced in the bacteria. Eur J Biochem 201:399-407.
    • (1991) Eur J Biochem , vol.201 , pp. 399-407
    • Dietrich, J.B.1    Lorber, B.2    Kern, D.3
  • 18
    • 0031302438 scopus 로고    scopus 로고
    • Diagnosis of chronic camel trypanosomosis by detection of the antibody of trypanosome tyrosine aminotransferase
    • El Sawalhy A, El-Sherbini S. 1997. Diagnosis of chronic camel trypanosomosis by detection of the antibody of trypanosome tyrosine aminotransferase. Dtsch tierärztl Wschr 104:531-533.
    • (1997) Dtsch Tierärztl Wschr , vol.104 , pp. 531-533
    • El Sawalhy, A.1    El-Sherbini, S.2
  • 19
    • 0031812502 scopus 로고    scopus 로고
    • Increased excretion of aromatic amino acids catabolites in mammals infected with Trypanosoma brucei evansi
    • El Sawalhy A, Seed JR, Hall JE, El Attar H. 1998. Increased excretion of aromatic amino acids catabolites in mammals infected with Trypanosoma brucei evansi. J Parasitol 84:469-473.
    • (1998) J Parasitol , vol.84 , pp. 469-473
    • El Sawalhy, A.1    Seed, J.R.2    Hall, J.E.3    El Attar, H.4
  • 20
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of molscript that includes greatly enhanced coloring capabilities
    • Esnouf RM. 1997. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 15:112-113, 132-134.
    • (1997) J Mol Graph Model , vol.15 , pp. 112-113
    • Esnouf, R.M.1
  • 22
    • 0015104105 scopus 로고
    • Alanine aminotransferase and aspartate aminotransferase in Leishmania tarentolae
    • Fair DS, Krassner SM. 1971. Alanine aminotransferase and aspartate aminotransferase in Leishmania tarentolae. J Parasitol 18:441-444.
    • (1971) J Parasitol , vol.18 , pp. 441-444
    • Fair, D.S.1    Krassner, S.M.2
  • 23
    • 0014472314 scopus 로고
    • Soluble and mitochondrial forms of tyrosine aminotransferase: Relationship to human tyrosinemia
    • Fellman JH, Vanbellinghen PJ, Jones RT, Koler RD. 1969. Soluble and mitochondrial forms of tyrosine aminotransferase: Relationship to human tyrosinemia. Biochemistry 8:615-622.
    • (1969) Biochemistry , vol.8 , pp. 615-622
    • Fellman, J.H.1    Vanbellinghen, P.J.2    Jones, R.T.3    Koler, R.D.4
  • 24
    • 0031875873 scopus 로고    scopus 로고
    • The Achilles' heel of trypanosomatids: Trypanothione-mediated hydroperoxide metabolism
    • Flohé L. 1998. The Achilles' heel of trypanosomatids: Trypanothione-mediated hydroperoxide metabolism. Biofaclors 8:87-91.
    • (1998) Biofaclors , vol.8 , pp. 87-91
    • Flohé, L.1
  • 25
    • 0019014846 scopus 로고
    • Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase
    • Ford GC, Eichele G, Jansonius JN. 1980. Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase. Proc Natl Acad Sci USA 77:2559-2263.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2559-12263
    • Ford, G.C.1    Eichele, G.2    Jansonius, J.N.3
  • 26
    • 0032961270 scopus 로고    scopus 로고
    • SPript: Analysis of multiple sequence alignments in postscript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. 1999. SPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 27
    • 0022429495 scopus 로고
    • Complete complementary DNA of rat tyrosine aminotransferase messenger RNA. Deduction of the primary structure of the enzyme
    • Grange T, Pictet R. 1985. Complete complementary DNA of rat tyrosine aminotransferase messenger RNA. Deduction of the primary structure of the enzyme. J Mol Biol 184:347-350.
    • (1985) J Mol Biol , vol.184 , pp. 347-350
    • Grange, T.1    Pictet, R.2
  • 28
    • 78651186187 scopus 로고
    • Neue sonderformen von Keratosis palmo-plantaris, u.a. eine regelmäßig-dominante mit systematisierten Lipomen, ferner 2 einfachrezessive mit Schwachsinn und z.T. mit Hornhautveränderungen des Auges (Ektodermatosyndrom)
    • Hanhart E. 1947. Neue Sonderformen von Keratosis palmo-plantaris, u.a. eine regelmäßig-dominante mit systematisierten Lipomen, ferner 2 einfachrezessive mit Schwachsinn und z.T. mit Hornhautveränderungen des Auges (Ektodermatosyndrom). Dermatologica 94:286-308.
    • (1947) Dermatologica , vol.94 , pp. 286-308
    • Hanhart, E.1
  • 29
    • 0024297286 scopus 로고
    • Persulfide generated from L-cysteine inactivates tyrosine aminotransferase. Requirement for a protein with cysteine oxidase activity and γ-cystathionase
    • Hargrove JL. 1988. Persulfide generated from L-cysteine inactivates tyrosine aminotransferase. Requirement for a protein with cysteine oxidase activity and γ-cystathionase. J Biol Chem 263:17262-17269.
    • (1988) J Biol Chem , vol.263 , pp. 17262-17269
    • Hargrove, J.L.1
  • 30
    • 0023664452 scopus 로고
    • A cystine-dependent inactivator of tyrosine aminotransferase co-purifies with gamma-cystathionase (cystine desulfurase)
    • Hargrove JL, Wichman RD. 1987. A cystine-dependent inactivator of tyrosine aminotransferase co-purifies with gamma-cystathionase (cystine desulfurase). J Biol Chem 262:7351-7357.
    • (1987) J Biol Chem , vol.262 , pp. 7351-7357
    • Hargrove, J.L.1    Wichman, R.D.2
  • 32
    • 0033605317 scopus 로고    scopus 로고
    • Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 Å resolution: Comparison of the unligated enzyme and a complex with α-methyl-L-glutamate
    • Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN. 1999. Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 Å resolution: Comparison of the unligated enzyme and a complex with α-methyl-L-glutamate. J Mol Biol 286:829-850.
    • (1999) J Mol Biol , vol.286 , pp. 829-850
    • Hester, G.1    Stark, W.2    Moser, M.3    Kallen, J.4    Markovic-Housley, Z.5    Jansonius, J.N.6
  • 33
    • 0030047142 scopus 로고    scopus 로고
    • WHAT_CHECK (verification routines from WHAT IF): Errors in protein structures
    • Hooft RWW, Vriend G, Sander C, Abola EE. 1996. WHAT_CHECK (verification routines from WHAT IF): Errors in protein structures. Nature 381:272.
    • (1996) Nature , vol.381 , pp. 272
    • Hooft, R.W.W.1    Vriend, G.2    Sander, C.3    Abola, E.E.4
  • 35
    • 0018831215 scopus 로고
    • Richner-Hanhart syndrome and tyrosinemia type II
    • Hunziker N. 1980. Richner-Hanhart syndrome and tyrosinemia type II. Dermatologica 160:180-189.
    • (1980) Dermatologica , vol.160 , pp. 180-189
    • Hunziker, N.1
  • 36
    • 0015607134 scopus 로고
    • Studies on the induction and repression of enzymes in rat liver. Characterization and metabolic regulation of multiple forms of tyrosine aminotransferase
    • Iwasaki Y, Lamar C, Danenberg K, Pilot HC. 1973. Studies on the induction and repression of enzymes in rat liver. Characterization and metabolic regulation of multiple forms of tyrosine aminotransferase. Eur J Biochem 34:347-357.
    • (1973) Eur J Biochem , vol.34 , pp. 347-357
    • Iwasaki, Y.1    Lamar, C.2    Danenberg, K.3    Pilot, H.C.4
  • 37
    • 0029919942 scopus 로고    scopus 로고
    • Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases
    • Jensen RA, Gu W. 1996. Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases. J Bacteriol 178:2161-2171.
    • (1996) J Bacteriol , vol.178 , pp. 2161-2171
    • Jensen, R.A.1    Gu, W.2
  • 38
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsion and neuraminidase crystal structures
    • Jiang JS, Brünger AT. 1994. Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsion and neuraminidase crystal structures. J Mol Biol 243:100-115.
    • (1994) J Mol Biol , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brünger, A.T.2
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1993. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1993) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 42
    • 0002700643 scopus 로고
    • Halloween . . . Masks and bones
    • Warrington, UK: SERC Daresbury Laboratory
    • Kleywegt GJ, Jones TA. 1994. Halloween . . . masks and bones. In: From first map to final model. Warrington, UK: SERC Daresbury Laboratory. pp 59-66.
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 43
    • 0026244229 scopus 로고
    • A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 1991. A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 44
    • 0025366034 scopus 로고
    • Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity
    • Kuramitsu S, Hiromi K, Hayashi H, Morino Y, Kagamiyama H. 1990. Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry 29:5469-5476.
    • (1990) Biochemistry , vol.29 , pp. 5469-5476
    • Kuramitsu, S.1    Hiromi, K.2    Hayashi, H.3    Morino, Y.4    Kagamiyama, H.5
  • 45
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin VS, Wilson KS. 1993. Automated refinement of protein models. Acta Crystallogr D49:129-147.
    • (1993) Acta Crystallogr , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 46
  • 47
    • 0021196423 scopus 로고
    • Aspartate aminotransferase in Leishmania is a broad spectrum transaminase
    • Le Blanq SM, Lanham SM. 1984. Aspartate aminotransferase in Leishmania is a broad spectrum transaminase. Trans Roy Soc Trop Med Hyg 78:373-375.
    • (1984) Trans Roy Soc Trop Med Hyg , vol.78 , pp. 373-375
    • Le Blanq, S.M.1    Lanham, S.M.2
  • 48
    • 0029124159 scopus 로고
    • Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase
    • Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN. 1995a. Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nat Struct Biol 2:548-553.
    • (1995) Nat Struct Biol , vol.2 , pp. 548-553
    • Malashkevich, V.N.1    Onuffer, J.J.2    Kirsch, J.F.3    Jansonius, J.N.4
  • 50
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 52
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary groups
    • Mehta PK, Hale TI, Christen P. 1993. Aminotransferases: Demonstration of homology and division into evolutionary groups. Eur J Biochem 214:549-561.
    • (1993) Eur J Biochem , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 53
    • 0015239516 scopus 로고
    • Purification, properties and identity of liver mitochondrial tyrosine aminotransferase
    • Miller JE, Litwack G. 1971. Purification, properties and identity of liver mitochondrial tyrosine aminotransferase. J Biol Chem 246:3234-3240.
    • (1971) J Biol Chem , vol.246 , pp. 3234-3240
    • Miller, J.E.1    Litwack, G.2
  • 54
    • 0027228096 scopus 로고
    • Purification and parial structural and kinetic characterization of tyrosine aminotransferase from epimastigotes of Trypanosoma cruzi
    • Montemartini M, Santomé JA, Cazzulo JJ, Nowicki C. 1993. Purification and parial structural and kinetic characterization of tyrosine aminotransferase from epimastigotes of Trypanosoma cruzi. Biochem J 292:901-906.
    • (1993) Biochem J , vol.292 , pp. 901-906
    • Montemartini, M.1    Santomé, J.A.2    Cazzulo, J.J.3    Nowicki, C.4
  • 55
    • 0028175771 scopus 로고
    • Production of aromatic α-hydroxy acids by epimastigotes of Trypanosoma cruzi, and its possible role in NADH re-oxidation
    • Montemartini M, Santomé JA, Cazzulo JJ, Nowicki C. 1994a. Production of aromatic α-hydroxy acids by epimastigotes of Trypanosoma cruzi, and its possible role in NADH re-oxidation. FEMS Microbiol Lett 118:89-92.
    • (1994) FEMS Microbiol Lett , vol.118 , pp. 89-92
    • Montemartini, M.1    Santomé, J.A.2    Cazzulo, J.J.3    Nowicki, C.4
  • 56
    • 0028079911 scopus 로고
    • Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi
    • Montemartini M, Santomé JA, Cazzulo JJ, Nowicki C. 1994b. Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi. Mol Biochem Parasitol 68:15-23.
    • (1994) Mol Biochem Parasitol , vol.68 , pp. 15-23
    • Montemartini, M.1    Santomé, J.A.2    Cazzulo, J.J.3    Nowicki, C.4
  • 57
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris GM, Goodsell DS, Huey R, Olson AJ. 1996. Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4. J Comput Aided Mol Des 10:293-304.
    • (1996) J Comput Aided Mol Des , vol.10 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4
  • 58
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D53:240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 59
    • 0026701404 scopus 로고
    • Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II
    • Natt E, Kida K, Odievre M, Di Rocco M, Scherer G. 1992. Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. Proc Natl Acad Sci USA 89:9297-9301.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9297-9301
    • Natt, E.1    Kida, K.2    Odievre, M.3    Di Rocco, M.4    Scherer, G.5
  • 60
    • 84920325457 scopus 로고
    • An automated package for molecular replacement
    • Navaza J. 1994. An automated package for molecular replacement. Acta Crystallogr A50:157-163.
    • (1994) Acta Crystallogr , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 61
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 62
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyzes trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke E, Gommel DU, Kieß M, Kalisz HM, Flohé L. 1997. A unique cascade of oxidoreductases catalyzes trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol Chem 378:827-836.
    • (1997) Biol Chem , vol.378 , pp. 827-836
    • Nogoceke, E.1    Gommel, D.U.2    Kieß, M.3    Kalisz, H.M.4    Flohé, L.5
  • 63
    • 0027120030 scopus 로고
    • Presence and subcellular localization of tyrosine aminotransferase and p-hydroxyphenyllactate dehydrogenase in epimastigotes of Trypanosoma cruzi
    • Nowicki C, Montemartini M, Duschak V, Santome JA, Cazzulo JJ. 1992. Presence and subcellular localization of tyrosine aminotransferase and p-hydroxyphenyllactate dehydrogenase in epimastigotes of Trypanosoma cruzi. FEMS Microbiol Lett 71:119-124.
    • (1992) FEMS Microbiol Lett , vol.71 , pp. 119-124
    • Nowicki, C.1    Montemartini, M.2    Duschak, V.3    Santome, J.A.4    Cazzulo, J.J.5
  • 64
    • 0031912734 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of tyrosine aminotransferase from Trypanosoma cruzi epimastigotes
    • Nowicki C, Montemartini M, Hunter GR, Blankenfeldt W, Kalisz HM, Hecht HJ. 1998. Crystallization and preliminary X-ray analysis of tyrosine aminotransferase from Trypanosoma cruzi epimastigotes. Acta Crystallogr D54:105-107.
    • (1998) Acta Crystallogr , vol.D54 , pp. 105-107
    • Nowicki, C.1    Montemartini, M.2    Hunter, G.R.3    Blankenfeldt, W.4    Kalisz, H.M.5    Hecht, H.J.6
  • 65
    • 0028167665 scopus 로고
    • X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form
    • Okamoto A, Higuchi T, Hirotsu K, Kuramitsu S, Kagamiyama H. 1994. X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form. J Biochem 116:95-107.
    • (1994) J Biochem , vol.116 , pp. 95-107
    • Okamoto, A.1    Higuchi, T.2    Hirotsu, K.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 66
    • 0032540849 scopus 로고    scopus 로고
    • Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: A substrate recognition site constructed by rearrangement of hydrogen bond network
    • Okamoto A, Nakai Y, Hayashi H, Hirotsu K, Kagamiyama H. 1998. Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: A substrate recognition site constructed by rearrangement of hydrogen bond network. J Mol Biol 280:443-461.
    • (1998) J Mol Biol , vol.280 , pp. 443-461
    • Okamoto, A.1    Nakai, Y.2    Hayashi, H.3    Hirotsu, K.4    Kagamiyama, H.5
  • 67
    • 0023464501 scopus 로고
    • Compartmentation of carbohydrate metabolism in trypanosomes
    • Opperdoes FR. 1987. Compartmentation of carbohydrate metabolism in trypanosomes. Annu Rev Microbiol 41:127-151.
    • (1987) Annu Rev Microbiol , vol.41 , pp. 127-151
    • Opperdoes, F.R.1
  • 68
    • 85030332879 scopus 로고
    • Data collection and processing
    • Warrington, UK: SERC Daresbury Laboratory
    • Otwinowski Z. 1993. Data collection and processing. In: CCP4 Daresbury study weekend. Warrington, UK: SERC Daresbury Laboratory.
    • (1993) CCP4 Daresbury Study Weekend
    • Otwinowski, Z.1
  • 69
    • 0023189810 scopus 로고
    • Purification and characterization of a tyrosine aminotransferase from Crithidia fasciculata
    • Rege AA. 1987. Purification and characterization of a tyrosine aminotransferase from Crithidia fasciculata. Mol Biochem Parasitol 25:1-9.
    • (1987) Mol Biochem Parasitol , vol.25 , pp. 1-9
    • Rege, A.A.1
  • 70
    • 0025302147 scopus 로고
    • Isolation and characterization of the human tyrosine aminotransferase gene
    • Rettenmeier R, Natt E, Zentgraf H, Scherer G. 1990. Isolation and characterization of the human tyrosine aminotransferase gene. Nucleic Acids Res 18:3853-3861.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3853-3861
    • Rettenmeier, R.1    Natt, E.2    Zentgraf, H.3    Scherer, G.4
  • 71
    • 0030845064 scopus 로고    scopus 로고
    • Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
    • Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A. 1997. Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate. J Biol Chem 272:17293-17302.
    • (1997) J Biol Chem , vol.272 , pp. 17293-17302
    • Rhee, S.1    Silva, M.M.2    Hyde, C.C.3    Rogers, P.H.4    Metzler, C.M.5    Metzler, D.E.6    Arnone, A.7
  • 72
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice LM, Brünger AT. 1994. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19:277-290.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 73
    • 0003364945 scopus 로고
    • Hornhautaffektion bei Keratoma palmare et plantare hereditarium
    • Richner H. 1938. Hornhautaffektion bei Keratoma palmare et plantare hereditarium. Klin Mol Augenheilk 100:580-588.
    • (1938) Klin Mol Augenheilk , vol.100 , pp. 580-588
    • Richner, H.1
  • 74
    • 0024079259 scopus 로고
    • BRAGI: A comprehensive protein modeling program system
    • Schomburg D, Reichelt J. 1988. BRAGI: A comprehensive protein modeling program system. J Mol Graphics 6:161-165.
    • (1988) J Mol Graphics , vol.6 , pp. 161-165
    • Schomburg, D.1    Reichelt, J.2
  • 75
    • 0027936280 scopus 로고
    • Correlating solvation free energies and surface tensions of hydrocarbon solutes
    • Sitkoff D, Sharp KA, Honig B. 1994. Correlating solvation free energies and surface tensions of hydrocarbon solutes. Biophys Chem 51:397-403.
    • (1994) Biophys Chem , vol.51 , pp. 397-403
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 76
    • 0001681540 scopus 로고
    • Metabolism of tyrosine and phenylalanine in Trypanosoma brucei gambiense
    • Stibbs HH, Seed JR. 1975a. Metabolism of tyrosine and phenylalanine in Trypanosoma brucei gambiense. Int J Biochem 6:197-203.
    • (1975) Int J Biochem , vol.6 , pp. 197-203
    • Stibbs, H.H.1    Seed, J.R.2
  • 77
    • 0016762113 scopus 로고
    • Short-term metabolism of 14C tryptophan in rats infected with Trypanosoma brucei gambiense
    • Stibbs HH, Seed JR. 1975b. Short-term metabolism of 14C tryptophan in rats infected with Trypanosoma brucei gambiense. J Infect Dis 131:459-462.
    • (1975) J Infect Dis , vol.131 , pp. 459-462
    • Stibbs, H.H.1    Seed, J.R.2
  • 78
    • 0032214622 scopus 로고    scopus 로고
    • Protein Data Bank (PDB): Database of three-dimensional structural information of biological macromolecules
    • Sussman JL, Lin D, Jiang J, Manning NO, Prilusky J, Ritter O, Abola EE. 1998. Protein Data Bank (PDB): Database of three-dimensional structural information of biological macromolecules. Acta Crystallogr D54:1078-1084.
    • (1998) Acta Crystallogr , vol.D54 , pp. 1078-1084
    • Sussman, J.L.1    Lin, D.2    Jiang, J.3    Manning, N.O.4    Prilusky, J.5    Ritter, O.6    Abola, E.E.7
  • 79
    • 0000888502 scopus 로고
    • The locked rotation function
    • Tong L, Rossmann MG. 1990. The locked rotation function. Acta Crystallogr A46:783-792.
    • (1990) Acta Crystallogr , vol.A46 , pp. 783-792
    • Tong, L.1    Rossmann, M.G.2
  • 80
    • 0001408294 scopus 로고    scopus 로고
    • Computation of Bhat's OMIT maps with different coefficients
    • Vellieux FMD, Dijkstra BW. 1997. Computation of Bhat's OMIT maps with different coefficients. J Appl Crystallogr 30:396-399.
    • (1997) J Appl Crystallogr , vol.30 , pp. 396-399
    • Vellieux, F.M.D.1    Dijkstra, B.W.2
  • 81
    • 0032582840 scopus 로고    scopus 로고
    • Isolation and partial characterization of a broad specificity aminotransferase from Leishmania mexicana promastigotes
    • Vernal J, Cazzulo JJ, Nowicki C. 1998. Isolation and partial characterization of a broad specificity aminotransferase from Leishmania mexicana promastigotes. Mol Biochem Parasitol 96:83-92.
    • (1998) Mol Biochem Parasitol , vol.96 , pp. 83-92
    • Vernal, J.1    Cazzulo, J.J.2    Nowicki, C.3
  • 82
    • 0003579421 scopus 로고    scopus 로고
    • Geneva, Switzerland: World Health Organisation
    • st century: A vision for all. Geneva, Switzerland: World Health Organisation.
    • (1998) st Century: A Vision for All
  • 83
    • 0026664513 scopus 로고
    • Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate
    • Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H. 1992. Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate. Biochemistry 31:5878-5887.
    • (1992) Biochemistry , vol.31 , pp. 5878-5887
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Kagamiyama, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.