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Document Page 392 53. Noble MEM, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AMWH, Groendijk H, Hol WGJ. The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins: Struct Funct Genet 1991; 10:50–69. 54. Noble MEM, Witmans CJ, Verlinde CLMJ, Wierenga RK, Hol WGJ. Unpublished results. 55. Verlinde CLMJ, Witmans CJ, Pijning T, Kalk KH, Hol WGJ, Callens M, Opperdoes FR. Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphonobutanamide: binding at the active site despite an “open” flexible loop. Protein Sci 1992; 1:1578–1584. 56. Knowles JR. Enzyme catalysis: not different, just better. Nature 1991; 350:121–124. 57. Lambeir AM, Opperdoes FR, Wierenga RK. Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes. Eur J Biochem 1987; 168:69–74. 58. Verlinde CLMJ, Rudenko G, Hol WGJ. In search of new lead compounds for trypanosomiasis drug design: a protein structure-based linked-fragment approach. J Comput-Aided Drug Des 1992; 69:131–147. 59. Hannaert V, Opperdoes FR, Michels PAM. Glycosomal glyceraldehyde-3- phosphate dehydrogenase of Trypanosoma brucei and Trypanosoma cruzi: expression in Escherichia coli, purification, and characterization of the enzymes. Protein Expr Purif 1995; 6:244–250. 60. Michels PAM, Poliszczak A, Osinga KA, Misset O, Van Beeumen J, Wierenga RK, Borst P, Opperdoes FR. Two tandemly linked identical genes code for the glycosomal glyceraldehyde-phosphate dehydrogenase in Trypanosoma brucei. EMBO J 1986; 5:1049–1056. 61. Lambeir AM, Loiseau AM, Kuntz DA, Vellieux FM, Michels PAM, Opperdoes FR. The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes. Eur J Biochem 1991; 198:429–435. 62. Hannaert V, Callens M, Opperdoes FR, Michels PAM. Purification and characterization of the native and recombinant Leishmania mexicana glycosomal glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 1994; 225:143–149. 63. Desjeux P. Human leishmaniases: epidemiology and health aspects. World Health Stat Q 1992; 45:267–275. 64. Berman JD, Gallalee JV, Best JM. Sodium stibogluconate (Penstostam) inhibition of glucose catabolism via the glycolytic pathway, and fatty acid β-oxidation in Leishmania mexicana amastigotes. Biochem Pharmacol 1987; 36:197–201. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_392.html (1 of 2) [4/5/2004 5:43:36 PM]
Document 65. João HC, Williams RJP. The anatomy of a kinase and the control of phosphate transfer. Eur J Biochem 1993; 216:1–18. 66. Michels PAM, personal communication. 67. Huang IY, Welch CD, Yoshida A. Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence. J Biol Chem 1980; 255:6412–6420. 68. McCarrey JR, Thomas K. Human testis-specific PGK gene lacks introns and possesses characteristics of a processed gene. Nature 1987; 326:501–504. 69. Davies GJ, Gamblin SJ, Littlechild JA, Dauter Z, Wilson KS, Watson HC. Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 Å. Acta Cryst D 1994; 50:202–209. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_392.html (2 of 2) [4/5/2004 5:43:36 PM]
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Document D ddI, 152 tumour necrosis
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