Griffith, E.C., Su, Z., Niwayama, S., Ramsay, C.A., Chang, Y.-H. Lowther, W.T., McMillen, D.A., Orville, A.M. Griffith, E.C., Su, Z., Turk, B.E., Chen, S., Chang, Y.-H., Wu, Z., Biemann, K. By contrast, the nature of the oxygen bridging the metal ions within the metal binding site of eMetAP-1 cannot be determined based on the results here, due to the similar structural results obtained with a bridging water molecule and a bridging hydroxide ion.įolkman, J., N. Within the site of hMetAP-2 the results strongly indicate that a hydroxide ion bridges the metal ions. Another important structural issue is the identity of the bridging oxygen, which is part of either a water molecule or a hydroxide ion. colimethionine aminopeptidase type 1 (eMetAP-1). This was the case for both of the systems studied one based on the X-ray structure of the human methionine aminopeptidase type 2 (hMetAP-2) and the other based on the X-ray structure of the E. The calculations showed that the structure of the site was not influenced by the identity of the metal ions. The structure of this site with either Co 2+ions or Zn 2+ions was investigated using density functional theory. Journal of Applied Microbiology, 84, 561–566.All methionine aminopeptidases exhibit the same conserved metal binding site. Bioscience, Biotechnology, and Biochemistry, 70, 1110–1117. European Journal of Biochemistry, 258, 313–319. Papir, G., Spungin-bialik, A., Ben-Meir, D., Fudim, E., & Gilboa, R. S., Lou, P., Kawai, M., Park, C., Egan, D. Tsunasawa, S., Izu, Y., Miyagi, M., & Kato, I. Journal of Biochemistry and Molecular Biology, 35, 228–235.Ĭhang, Y. Journal of Industrial Microbiology & Biotechnology, 17, 30–35.Ĭhung, J. Journal of Applied Microbiology, 104, 380–387.īoufous, H., & Vadeboncoeur, C. M., Pandey, A., Rahulan, R., & Szakacs, G. Biochemical and Biophysical Research Communications, 332, 418–425. Applied and Environmental Microbiology, 17, 242–245.Įtienne, G., Laval, F., Villeneuve, C., Dinadayala, P., Abouwarda, A., Zerbib, D., et al. Journal of Bioscience and Bioengineering, 94, 309–314. Karadzic, I., Izrael, L., Gojgic-Cvijovic, G., & Vujcic, Z. Letters in Applied Microbiology, 41, 498–504. M., Nagy, V., Kovacs, K., Szakacs, G., & Pandey, A. Biochemical and Biophysical Research Communications, 307, 172–179. Proteins Structure Function and Bioinformatics, 66, 538–546. Molecular and Cellular Proteomics, 5, 2336–2349.Įvdokimov, A. Totowa, NJ: Humana.įrottin, F., Martinez, A., Peynot, P., Mitra, S., Holz, R. Stoker (Eds.), Methods in molecular biology, vol. Biochimica et Biophysica Acta, 1477, 157–167. Proceedings of the National Academy of Sciences of the United States of America, 84, 2718–2722.Ĭhang, S. Proceedings of the National Academy of Sciences of the United States of America, 92, 12357–12361. Current Medicinal Chemistry, 9, 385–409.įlores, Y. The enzyme activity inhibited by EDTA is restored in presence of Mg 2+ suggesting the possible role of Mg 2+ as metal cofactor of the enzyme in vitro.Īddlagatta, A., Quillin, M. The enzyme activity was enhanced by Mg 2+ and Co 2+ and was inhibited by Fe 2+ and Cu 2+. The enzyme was found to have a temperature and pH optimum of 50 ☌ and 8.5, respectively, and was found to be stable at 50 ☌ with half-life more than 8 h. The enzyme was characterized biochemically, using l-methionine p-nitroanilide as substrate. Activity staining was performed to detect the methionine aminopeptidase activity on native polyacrylamide gel. The purified enzyme exhibited a molecular weight of ≈ 37 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). MetAP from Mycobacterium smegmatis mc 2 155 was purified from the culture lysate in four sequential steps to obtain a final purification fold of 22. The methionine aminopeptidase (MetAP) catalyzes the removal of amino terminal methionine from newly synthesized polypeptide.

Metal ion bonding methionine