Type I methionine aminopeptidase from Saccharomyces cerevisiae is a potential target for antifungal drug screening

Acta Pharmacologica Sinica

Volumn 25, Issue 7, 2004, Pages 907-914

  Chen, Ling Ling ^a   Li, Jia ^a   Li, Jing Ya ^a   Luo, Qun Li ^a   Mao, Wei Feng ^a   Shen, Qiang ^a   Nan, Fa Jun ^a   Ye, Qi Zhuang ^b  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^b UNIVERSITY OF KANSAS   (United States)

Author keywords

Antifungal agent; High throughput screening; Methionine aminopeptidase

Indexed keywords

ANTIFUNGAL AGENT; METHIONYL AMINOPEPTIDASE; ORGANIC COMPOUND; PICOLINIC ACID DERIVATIVE;

ARTICLE; CHEMICAL ANALYSIS; COLORIMETRY; CONTROLLED STUDY; DRUG SCREENING; DRUG TARGETING; ESCHERICHIA COLI; FUNGAL GENE; FUNGUS GROWTH; GENE DELETION; GENE MAPPING; GROWTH INHIBITION; HIGH THROUGHPUT SCREENING; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PROTEIN EXPRESSION; PROTEIN TARGETING; SACCHAROMYCES CEREVISIAE; SCMETAP1 GENE; WILD TYPE; YEAST;

AMINOPEPTIDASES; ANTIFUNGAL AGENTS; DRUG DESIGN; DRUG EVALUATION, PRECLINICAL; ENZYME INHIBITORS; ESCHERICHIA COLI; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE;

EID: 3142710101     PISSN: 16714083     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (29)

1. Bradshaw RA, Brickey WW, Walker KW. N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families. Trends Biochem Sci 1998; 23: 263-7.
2. Lowther WT, Matthews BW. Structure and function of the methionine aminopeptidases. Biochem Biophys Acta 2000; 1477: 157-67.
3. Arfin SM, Kendall RL, Bradshaw RA. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc Natl Acad Sci USA 1995; 92: 7714-8.
4. Lowther WT, Orville AM, Madden DT, Lim S, Rich DH, Matthews BW. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry 1999; 38: 7678-88.
5. Liu S, Widom J, Kemp CW, Crews CM, Clardy J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science 1998; 282: 1324-7.
6. Tahirov TH, Oki H, Tsukihara T, Ogasahara K, Yutani K, Ogata K, et al. Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus. J Mol Biol 1998; 284: 101-24.
7. 2+ as a cofactor: a case of mistaken identity? Protein Sci 1998; 7: 2684-7.
8. D'souza VM, Holz RC. The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. Biochemistry 1999; 38: 11079-85.
9. Meng L, Ruebush S, D'souza VM, Copik AJ, Tsunasawa S, Holz RC. Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiosus. Biochemistry 2002; 41: 7199-208.
10. D'souza VM, Swierczek SI, Cosper NJ, Meng L, Ruebush S, Copik AJ, et al. Kinetic and structural characterization of manganese (II)-loaded methionyl aminopeptidases. Biochemistry 2002; 41: 13096-105.
11. Wang J, Sheppard GS, Lou P, Kawai M, Park C, Egan DA, et al. Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese. Biochemistry 2003; 42: 5035-42.
12. Li JY, Chen LL, Cui YM, Luo QL, Li J, Nan FJ, et al. Metal substitution of the methionine aminopeptidase from Escherichia coli changes specificity for substrates and inhibitors. Biochem Biophys Res Commun 2003; 307: 172-9.
13. Chang SY, McGary EC, Chang S. Methionine aminopeptidase gene of Escherichia coli is essential for cell growth. J Bacteriol 1989; 171: 4071-2.
14. Miller CG, Kukral AM, Miller JL, Movva NR. PepM is an essential gene in Salmonella typhimurium. J Bacteriol 1989; 171: 5215-7.
15. Li X, Chang YH. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc Natl Acad Sci USA 1995; 92: 12357-61.
16. Vaughan MD, Sampson PB, Honek JF. Methionine in and out of proteins: targets for drug design. Curr Med Chem 2002; 9: 385-409.
17. Sin N, Meng L, Wang MQ, Wen JJ, Bornmann WG, Crews CM. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc Natl Acad Sci USA 1997; 94: 6099-103.
18. Chen SP, Vetro JA, Chang YH. The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae. Arch Biochem Biophys 2002; 398: 87-93.
19. Dummitt B, Micka WS, Chang YH. N-terminal methionine removal and methionine metabolism in Saccharomyces cerevisiae. J Cell Biochem 2003; 89: 964-74.
20. Griffith EC, Su Z, Niwayama S, Ramsay CA, Chang YH, Liu JO. Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2. Proc Natl Acad Sci USA 1998; 95: 15183-8.
21. Keding SJ, Dales NA, Lim S, Beauliu D, Rich DH. Synthesis of (3R)-amino-(2S)-hydroxy amino acids for inhibition of methionine aminopeptidase-1. Synth Commun 1998; 28: 4463-70.
22. Luo QL, Li JY, Liu ZY, Chen LL, Shen Q, Li Y, et al. Discovery and structural modification of inhibitors of methionine aminopeptidases from Escherichia coli and Saccharomyces cerevisiae. J Med Chem 2003; 46: 2631-40.
23. Guan KL, Dixon JE. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal Biochem 1991; 192: 262-7.
24. Chang YH, Teichert U, Smith JA. Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae. J Biol Chem 1992; 267: 8007-11.
25. Klinkenberg M, Ling C, Chang YH. A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2. Arch Biochem Biophys 1997; 347: 193-200.
26. Zhou Y, Guo XC, Yi T, Yoshimoto T, Pei D. Two continuous spectrophotometric assays for methionine aminopeptidase. Anal Biochem 2000; 280: 159-65.
27. Walker KW, Yi E, Bradshaw RA. Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay. Biotechnol Appl Biochem 1999; 29: 157-63.
28. Zhuang SF, Zhou CH, Qian J, Qian Z, Shibuya M, Ye QZ. A new model for random screening inhibitors of vascular endothelial growth factor receptor 1 kinase. Acta Pharmacol Sin 2002; 23: 117-23.
29. Marino JP Jr, Thompson SK, Veber DF, inventors; Compounds and methods [P]. WO 0124796. 2001 Apr 12.