The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway

Biochemistry

Volumn 46, Issue 24, 2007, Pages 7205-7214

  Christianson, Carl V ^a   Montavon, Timothy J ^a   Van Lanen, Steven G ^b   Shen, Ben ^b   Bruner, Steven D ^a  

^a BOSTON COLLEGE   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOMUTASE; CHEMICAL TRANSFORMATION; COFACTOR; LYASE;

AMINO ACIDS; AMMONIA; ANTIBIOTICS; BIOSYNTHESIS; MUTAGENESIS; ONCOLOGY; STEREOSELECTIVITY;

ENZYME KINETICS;

4 METHYLIDENEIMIDAZOL 5 ONE; AMMONIA; ANTINEOPLASTIC ANTIBIOTIC; HISTIDINE AMMONIALYASE; IMIDAZOLE DERIVATIVE; LYASE; MUTASE; PROTEIN C1027; TYROSINE; TYROSINE 2,3 AMINOMUTASE; UNCLASSIFIED DRUG;

ANTIBIOTIC BIOSYNTHESIS; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; RHODOBACTER SPHAEROIDES; STEREOSPECIFICITY;

AMINO ACID SEQUENCE; AMINOGLYCOSIDES; ANTIBIOTICS, ANTINEOPLASTIC; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENEDIYNES; IMIDAZOLES; INTRAMOLECULAR TRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOMYCES;

RHODOBACTER SPHAEROIDES;

EID: 34250824674     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7003685     Document Type: Article

References (36)

1. Shen, B., Liu, W., and Nonaka, K. (2003) Enediyne natural products: biosynthesis and prospect towards engineering novel antitumor agents, Curr. Med. Chem. 10, 2317-2325.
2. Liu, W., Christenson, S. D., Standage, S., and Shen, B. (2002) Biosynthesis of the enediyne antitumor antibiotic C-1027, Science 297, 1170-1173.
3. Ahlert, J., Shepard, E., Lomovskaya, N., Zazopoulos, E., Staffa, A., Bachmann, B. O., Huang, K., Fonstein, L., Czisny, A., Whitwam, R. E., Farnet, C. M., and Thorson, J. S. (2002) The calicheamicin gene cluster and its iterative type I enediyne PKS, Science 297, 1173-1176.
4. Liu, W., Nonaka, K., Nie, L., Zhang, J., Christenson, S. D., Bae, J., Van Lanen, S. G., Zazopoulos, E., Farnet, C. M., Yang, C. F., and Shen, B. (2005) The neocarzinostatin biosynthetic gene cluster from Streptomyces carzinostaticus ATCC 15944 involving two iterative type I polyketide synthases, Chem. Biol. 12, 293-302.
5. Liu, W., Ahlert, J., Gao, Q., Wendt-Pienkowski, E., Shen, B., and Thorson, J. S. (2003) Rapid PCR amplification of minimal enediyne polyketide synthase cassettes leads to a predictive familial classification model, Proc. Natl. Acad. Sci U.S.A. 100, 11959-11963.
6. Okuno, Y., Iwashita, T., and Sugiura, Y. (2000) Structural basis for reaction mechanism and drug delivery system of chromoprotein antitumor antibiotic C-1027, J. Am. Chem. Soc. 122, 6848-6854.
7. Christenson, S. D., Liu, W., Toney, M. D., and Shen, B. (2003) A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis, J. Am. Chem. Soc. 125, 6062-6063.
8. Christenson, S. D., Wu, W., Spies, M. A., Shen, B., and Toney, M. D. (2003) Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis, Biochemistry 42, 12708-12718.
9. Wetmore, S. D., Smith, D. M., and Radom, L. (2001) Enzyme catalysis of 1,2-amino shifts: the cooperative action of B6, B12, and aminomutases, J. Am. Chem. Soc. 123, 8678-8689.
10. Lepore, B. W., Ruzicka, F. J., Frey, P. A., and Ringe, D. (2005) The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale, Proc. Natl. Acad. Sci. U.S.A. 102, 13819-13824.
11. Berkovitch, F., Behshad, E., Tang, K. H., Enns, E. A., Frey, P. A., and Drennan, C. L. (2004) A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase, Proc. Natl. Acad. Sci. U.S.A. 101, 15870-15875.
12. Lelais, G., and Seebach, D. (2004) β-amino acids-syntheses, occurrence in natural products, and components of β-peptides, Biopolymers 76, 206-243.
13. Cheng, R. P., Gellman, S. H., and DeGrado, W. F. (2001) β-Peptides: from structure to function, Chem. Rev. 101, 3219-3232.
14. Walker, K. D., Klettke, K., Akiyama, T., and Croteau, R. (2004) Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in Taxol biosynthesis, J. Biol. Chem. 279, 53947-53954.
15. Jin, M., Fischbach, M. A., and Clardy, J. (2006) A biosynthetic gene cluster for the acetyl-CoA carboxylase inhibitor andrimid, J. Am. Chem. Soc. 128, 10660-10661.
16. Retey, J. (2003) Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group, Biochim. Biophys. Acta 1647, 179-184.
17. Barondeau, D. P., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2005) Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry, Biochemistry 44, 1960-1970.
18. Winkel-Shirley, B. (2001) Flavonoid biosynthesis. A colorful model for genetics, biochemistry, cell biology, and biotechnology, Plant Physiol. 126, 485-493.
19. + and revision of the structure of its adduct with imidazolylpropionate, Eur. J. Biochem. 192, 669-676.
20. Schwede, T. F., Retey, J., and Schulz, G. E. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile, Biochemistry 38, 5355-5361.
21. Ritter, H., and Schulz, G. E. (2004) Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase, Plant Cell 16, 3426-3436.
22. Calabrese, J. C., Jordan, D. B., Boodhoo, A., Sariaslani, S., and Vannelli, T. (2004) Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis, Biochemistry 43, 11403-11416.
23. Louie, G. V., Bowman, M. E., Moffitt, M. C., Baiga, T. J., Moore, B. S., and Noel, J. P. (2006) Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases, Chem. Biol. 13, 1327-1338.
24. Poppe, L., and Retey, J. (2005) Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine, Angew. Chem., Int. Ed. 44, 3668-3688.
25. Hermes, J. D., Weiss, P. M., and Cleland, W. W. (1985) Use of nitrogen-15 and deuterium isotope effects to determine the chemical mechanism of phenylalanine ammonia-lyase, Biochemistry 24, 2959-2967.
26. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode, in Methods in Enzymology: Macromolecular Crystallography, part A (Carter, C. W., Jr., and Sweet, R. M., Eds.) pp 307-326, Academic Press, New York.
27. COLLABORATIVE COMPUTATIONAL PROJECT, N. (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
28. Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
29. Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics, Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 2126-2132.
30. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr., Sect. D: Biol. Crystallogr. 54, 905-921.
31. Baedeker, M., and Schulz, G. E. (2002) Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism, Eur. J. Biochem. 269, 1790-1797.
32. Baedeker, M., and Schulz, G. E. (2002) Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase, Structure 10, 61-67.
33. Wang, L., Gamez, A., Sarkissian, C. N., Straub, M., Patch, M. G., Han, G. W., Striepeke, S., Fitzpatrick, P., Scriver, C. R., and Stevens, R. C. (2005) Structure-based chemical modification strategy for enzyme replacement treatment of phenylketonuria, Mol. Genet. Metab. 86, 134-140.
34. Pilbak, S., Tomin, A., Retey, J., and Poppe, L. (2006) The essential tyrosine-containing loop conformation and the role of the C-terminal multi-helix region in eukaryotic phenylalanine ammonia-lyases, FEBS J. 273, 1004-1019.
35. Appert, C., Zon, J., and Amrhein, N. (2003) Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan2-phosphonic acid and other phenylalanine analogues, Phytochemistry 62, 415-422.
36. Watts, K. T., Mijts, B. N., Lee, P. C., Manning, A. J., and Schmidt-Dannert, C. (2006) Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family, Chem. Biol. 13, 1317-1326.