Article
Biochemistry, Vol. 49, No. 26, 2010 5599
14. Yamamoto, T., Sudo, K., and Fujita, T. (1994) Significant inhibition
of endothelial-cell growth in tumor vasculature by an angiogenesis
inhibitor, TNP-470 (AGM-1470). Anticancer Res. 14, 1–3.
15. Abe, J., Zhou, W., Takuwa, N., Taguchi, J., Kurokawa, K., Kumada,
M., and Takuwa, Y. (1994) A fumagillin derivative angiogenesis
inhibitor, AGM-1470, inhibits activation of cyclin-dependent kinases
and phosphorylation of retinoblastoma gene-product but not protein
tyrosyl phosphorylation or protooncogene expression in vascular
endothelial-cells. Cancer Res. 54, 3407–3412.
16. Kendall, R. L., and Bradshaw, R. A. (1992) Isolation and character-
ization of the methionine aminopeptidase from porcine liver respon-
sible for the cotranslational processing of proteins. J. Biol. Chem. 267,
20667–20673.
17. Ben-Bassat, A., Bauer, K., Chang, S. Y., Myambo, K., Boosman, A.,
and Chang, S. (1987) Processing of the initiation methionine from
proteins: Properties of the Escherichia coli methionine aminopepti-
dase and its gene structure. J. Bacteriol. 169, 751–757.
18. Hirel, P.-H., Schmitter, J.-M., Dessen, P., Fayat, G., and Blanquet, S.
(1989) Extent of N-terminal methionine excision from Escherichia coli
proteins is governed by the side-chain length of the penultimate amino
acid. Proc. Natl. Acad. Sci. U.S.A. 86, 8247–8251.
29. Wang, J. Y., Sheppard, G. S., Lou, P. P., Kawai, M., Park, C., Egan,
D. A., Schneider, A., Bouska, J., Lesniewski, R., and Henkin, J.
(2003) Physiologically relevant metal cofactor for methionine amino-
peptidase-2 is manganese. Biochemistry 42, 5035–5042.
30. Hu, X., Addlagatta, A., Lu, J., Matthews, B. W., and Liu, J. O. (2006)
Elucidation of the function of type 1 human methionine aminopepti-
dase during cell cycle progression. Proc. Natl. Acad. Sci. U.S.A. 103,
18148–18153.
31. Li, J.-Y., Chen, L.-L., Cui, Y.-M., Luo, Q.-L., Gu, M., Nan, F.-J., and
Ye, Q.-Z. (2004) Characterization of full length and truncated type I
human methionine aminopeptidases expressed from Escherichia coli.
Biochemistry 43, 7892–7898.
32. Chhabra, S. R., Parekh, H., Khan, A. N., Bycroft, B. W., and Kellam,
B. (2001) A Dde-based carboxy linker for solid-phase synthesis.
Tetrahedron Lett. 42, 2189–2192.
33. Lam, K. S., Salmon, S. E., Hersh, E. M., Hruby, V. J., Kazmierski,
W. M., and Knapp, R. J. (1991) A new type of synthetic peptide
library for identifying ligand-binding activity. Nature 354, 82–84.
34. Furka, A., Sebestyen, F., Asgedom, M., and Dibo, G. (1991) General
method for rapid synthesis of multicomponent peptide mixtures.
Int. J. Pept. Protein Res. 37, 487–493.
19. Flinta, C., Persson, B., Jornvall, H., and von Heijne, G. (1986)
Sequence determinants of cytosolic N-terminal protein processing.
Eur. J. Biochem. 154, 193–196.
35. Kaiser, R., and Metzka, L. (1999) Enhancement of cyanogen bromide
cleavage yields for methionyl-serine and methionyl-threonine peptide
bonds. Anal. Biochem. 266, 1–8.
20. Boissel, J.-P., Kasper, T. J., Shah, S. C., Malone, J. I., and Bunn, H. F.
(1985) Amino-terminal processing of proteins: Hemoglobin south
Florida, a variant with retention of initiator methionine and N-R-
acetylation. Proc. Natl. Acad. Sci. U.S.A. 82, 8448–8452.
21. Chang, Y.-H., Teicher, U., and Smith, J. A. (1990) Purification and
characterization of a methionine aminopeptidase from Saccharo-
myces cerevisiae. J. Biol. Chem. 265, 19892–19897.
22. Tsunasawa, S., Stewart, J. W., and Sherman, F. (1985) Amino-
terminal processing of mutant forms of yeast iso-1-cytochrome-c:
The specificities of methionine aminopeptidase and acetyltransferase.
J. Biol. Chem. 260, 5382–5391.
23. Walker, K. W., and Bradshaw, R. A. (1999) Yeast methionine
aminopeptidase I: Alteration of substrate specificity by site-directed
mutagenesis. J. Biol. Chem. 274, 13403–13409.
24. Yang, G., Kirkpatrick, R. B., Ho, T., Zhang, G. F., Liang, P. H.,
Johanson, K. O., Casper, D. J., Doyle, M. L., Marino, J. P., Jr.,
Thompson, S. K., Chen, W., Tew, D. G., and Meek, T. D. (2001)
Steady-state kinetic characterization of substrates and metal-ion
specificities of the full-length and N-terminally truncated recombi-
nant human methionine aminopeptidases (type 2). Biochemistry 40,
10645–10654.
25. Frottin, F., Martinez, A., Peynot, P., Mitra, S., Holz, R. C., Giglione,
C., and Meinnel, T. (2006) The proteomics of N-terminal methionine
cleavage. Mol. Cell. Proteomics 5, 2336–2349.
26. Addlagatta, A., Hu, X., Liu, J. O., and Matthews, B. W. (2005)
Structural basis for the functional differences between type I and type
II human methionine aminopeptidases. Biochemistry 44, 14741–
14749.
27. Thakkar, A., Wavreille, A. S., and Pei, D. (2006) Traceless capping
agent for peptide sequencing by partial Edman degradation and mass
spectrometry. Anal. Chem. 78, 5935–5939.
36. Sweeney, M. C., and Pei, D. (2003) An improved method for rapid
sequencing of support-bound peptides by partial Edman degradation
and mass spectrometry. J. Comb. Chem. 5, 218–222.
37. Gevaert, K., Goethals, M., Martens, L., Van Damme, J., Staes, A.,
Thomas, G. R., and Vandekerckhove, J. (2003) Exploring proteomes
and analyzing protein processing by mass spectrometric identification
of sorted N-terminal peptides. Nat. Biotechnol. 21, 566–569.
38. Luo, Q. L., Li, J. Y., Liu, Z. Y., Chen, L. L., Li, J., Qian, Z., Shen, Q.,
Li, Y., Lushington, G. H., Ye, Q. Z., and Nan, F. J. (2003) Discovery
and structural modification of inhibitors of methionine aminopepti-
dases from Escherichia coli and Saccharomyces cerevisiae. J. Med.
Chem. 46, 2631–2640.
39. Bond, C. S., White, M. F., and Hunter, W. N. (2001) High resolution
structure of the phosphohistidine-activated form of Escherichia coli
cofactor-dependent phosphoglycerate mutase. J. Biol. Chem. 276,
3247–3253.
40. Warder, S. E., Tucker, L. A., McLoughlin, S. M., Strelitzer, T. J.,
Meuth, J. L., Zhang, Q., Sheppard, G. S., Richardson, P. L.,
Lesniewski, R., Davidsen, S. K., Bell, R. L., Rogers, J. C., and Wang, J.
(2008) Discovery, Identification, and Characterization of Candidate
Pharmacodynamic Markers of Methionine Aminopeptidase-2 Inhibi-
tion. J. Proteome Res. 7, 4807–4820.
41. Turk, B. E., Griffith, E. C., Wolf, S., Biemann, K., Chang, Y. H., and Liu,
J. O. (1999) Selective inhibition of amino terminal methionine processing
by TNP-470 and ovalicin in endothelial cells. Chem. Biol. 6, 823–833.
42. Towbin, H., Bair, K. W., DeCaprio, J. A., Eck, M. J., Kim, S., Kinder,
F. R., Morollo, A., Mueller, D. R., Schindler, P., Song, H. K., van
Oostrum, J., Versace, R. W., Voshol, H., Wood, J., Zabludoff, S., and
Phillips, P. E. (2003) Proteomics-based target identification: Benga-
mides as a new class of methionine aminopeptidase inhibitors. J. Biol.
Chem. 278, 52964–52971.
28. Hu, X., Dang, Y., Tenney, K., Crews, P., Tsai, C. W., Sixt, K. M.,
Cole, P. A., and Liu, J. O. (2007) Regulation of c-Src tyrosine kinase
activity by bengamide a through inbition of methionine aminopepti-
dases. Chem. Biol. 14, 764–774.
43. Martinetz, A., Traverso, J. A., Valot, B., Ferro, M., Espagne, C.,
Ephritikhine, G., Zivy, M., Giglione, C., and Meinnel, T. (2008)
Extent of N-terminal modifications in cytosolic proteins from
eukaryotes. Proteomics 8, 2809–2831.