The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase

Cell

Volumn 93, Issue 1, 1998, Pages 103-109

  Zheng, Wenjin ^a   Johnston, Stephen Albert ^a   Joshua Tor, Leemor ^b  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b Watson School of Biological Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; BLEOMYCIN; BLEOMYCIN HYDROLASE; CARBOXYPEPTIDASE; CYSTEINE PROTEINASE; LIGASE; PROTEINASE; UNCLASSIFIED DRUG;

BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; DRUG BINDING; DRUG INACTIVATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 0032478519     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81150-2     Document Type: Article

References (32)

1. Adachi, H., Tsujimoto, M., Fukasawa, M., Sato, Y., Arai, H., Inoue, K., and Nishimura, T. (1997). cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity. Eur. J. Biochem. 245, 283-288.
2. Akiyama, S., Ikezaki, K., Kuramochi, H., Takahashi, K., and Kuwano, M. (1981). Bleomycin-resistant cells contain increased bleomycin-hydrolase activities. Biochem. Biophys. Res. Commun. 101, 55-60.
3. Bacon, D.J., and Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219.
4. Brömme, D., Rossi, A.B., Smeekens, S.P., Anderson, D.C., and Payan, D.G. (1996). Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization. Biochemistry 35, 6706-14.
5. Brünger, A.T. (1988). Crystallographic refinement by simulated annealing: application to a 2.8 Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203, 803.
6. Chapot, C.M., Nardi, M., Chopin, M.C., Chopin, A., and Gripon, J.C. (1993). Cloning and sequencing of pepC, a cysteine aminopeptidase gene from Lactococcus lactis subsp. cremoris AM2. Appl. Environ. Microbiol. 59, 330-333.
7. Chen, P., and Hochstrasser, M. (1996). Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86, 961-972.
8. Enenkel, C., and Wolf, D.H. (1993). BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase. J. Biol. Chem. 268, 7036-7043.
9. Ferrando, A.A., Velasco, G., Campo, E., and López-Otín, C. (1996). Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance. Cancer Res. 56, 1746-1750.
10. Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
11. Joshua-Tor, L., Xu, H.E., Johnston, S.A., and Rees, D.C. (1995). Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6. Science 269, 945-950.
12. Kambouris, N.G., Burke, D.J., and Creutz, C.E. (1992). Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J. Biol. Chem. 267, 21570-21576.
13. Klein, J.R., Schick, J., Henrich, B., and Plapp, R. (1997). Lactobacillus delbrueckii subsp. lactis DSM7290 pepG gene encodes a novel cysteine aminopeptidase. Microbiology 143, 527-537.
14. Kraulis, P.J. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946.
15. Larsen, C.N., and Finley, D. (1997). Protein translocation channels in the proteasome and other proteases. Cell, 91, 431-434.
16. Laskowski, R.A., MacArthur, R.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283.
17. Lazo, J., and Chabner, B.A. (1996). In Cancer Chemotherapy and Biotherapy: Principles and Practice, 2nd edition, B.A. Chabner and D. Longo, eds. (Philadelphia: Lippincott-Raven Publishers).
18. Lazo, J.S., and Humphreys, C.J. (1983). Lack of metabolism as the biochemical basis of bleomycin-induced pulmonary toxicity. Proc. Natl. Acad. Sci. USA 80, 3064-3068.
19. Löwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., and Huber, R. (1995). Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268, 533-539.
20. Lupas, A., Flanagan, J.M., Tamura, T., and Baumeister, W. (1997). Self-compartmentalizing proteases. TIBS 22, 399-404.
21. Magdolen, U., Muller, G., Magdolen, V., and Bandlow, W. (1993). A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases. Biochim. Biophys. Acta 1171, 299-303.
22. Mata, L., Erra-Pujada, M., Gripon, J., and Mistou, M. (1997). Experimental evidence for the essential role of the C-terminal residue in the strict aminopeptidase activity of the thiol aminopeptidase PepC, a bacterial bleomycin hydrolase. Biochem. J. 328, 343-347.
23. Merritt, E.A., and Murphy, M.E.P. (1994). Raster3D version 2.0: a program for photorealistic molecular graphics. Acta Cryst., D50, 869.
24. Otwinsowski, Z. (1993). In Data Collection and Processing, L. Sawyer, N. Isaacs, and S. Burley, eds. (Warrington, UK: Science and Engineering Research Council).
25. Schechter, I., and Berger, A. (1968). On the size of the active site in protease. 3. mapping the active site of papain; specific peptide inhibitors of papain. Biochem. Biophys. Res. Commun. 32, 888-902.
26. Schroder, E., Phillips, C., Garman, E., Harlos, K., and Crawford, C. (1993). X-ray crystallographic structure of a papain-leupeptin complex. FEBS Lett. 315, 38-42.
27. Seemuller, E., Lupas, A., and Baumeister, W. (1996). Autocatalytic processing of the 20S proteasome. Nature 382, 468-471.
28. Takeda, A., Masuda, Y., Yamamoto, T., Hirabayashi, T., Nakamura, Y., and Nakaya, K. (1996). Cloning and analysis of cDNA encoding rat bleomycin hydrolase, a DNA-binding cysteine protease. J. Biochem. (Tokyo) 120, 353-359.
29. Tong, L., Wengler, G., and Rossmann, M. (1993). Refined structure of Sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures. J. Mol. Biol. 230, 228-247.
30. Xu, H.E., and Johnston, S.A. (1994). Yeast bleomycin hydrolase is a DNA-binding cysteine protease: identification, purification, biochemical characterization. J. Biol. Chem. 269, 21177-21183.
31. Zheng, W., and Johnston, S. (1997). The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification. Mol. Cell. Biol., in press.
32. Zheng, W., Xu, H., Eric, and Johnston, S.A. (1997). The cysteine-protease bleomycin hydrolase is a new component of the galactose regulon in yeast, J. Biol. Chem. 272, 30350-30355.