Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase

Biochemistry

Volumn 48, Issue 34, 2009, Pages 8151-8160

  Tang, Kuo Hsiang ^b   Mansoorabadi, Steven O ^c   Reed, George H ^a   Frey, Perry A ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c The University of Texas at Austin   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; D-LYSINE; DEOXYADENOSINE; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; EPR SPECTROSCOPY; INTERCONVERSIONS; L-LYSINE; MICHAELIS COMPLEX; RADICAL BLOCK; RADICAL MECHANISM; RADICAL SPECIES; SUICIDE INACTIVATION; SUICIDE INHIBITOR; TRANSIENT RADICALS; TRANSIENT SPECIES;

ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSITIONS; ENZYMES; FREE RADICAL REACTIONS; FREE RADICALS; ISOMERIZATION; ISOMERS; PARAMAGNETIC RESONANCE; PARAMAGNETISM; QUANTUM THEORY; SPIN DYNAMICS; SUBSTRATES;

AMINO ACIDS;

5' DEOXYADENOSINE; ADENOSINE DERIVATIVE; COBALAMIN; LYSINE 5,6 AMINOMUTASE; MUTASE; THIALYSINE; UNCLASSIFIED DRUG;

AMINO ACID METABOLISM; ARTICLE; BACTERIAL METABOLISM; ELECTRON SPIN RESONANCE; ENZYME INHIBITION; NONHUMAN; PORPHYROMONAS GINGIVALIS; PRIORITY JOURNAL; REACTION ANALYSIS; STEREOCHEMISTRY;

BIOCATALYSIS; COBAMIDES; CYSTEINE; DEOXYADENOSINES; DEUTERIUM EXCHANGE MEASUREMENT; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME INHIBITORS; FREE RADICALS; INTRAMOLECULAR TRANSFERASES; MODELS, MOLECULAR; PORPHYROMONAS GINGIVALIS; PROTEIN CONFORMATION; QUANTUM THEORY; SPECTROPHOTOMETRY; STEREOISOMERISM; TIME FACTORS; TRANSCOBALAMINS;

THIA;

EID: 69249158333     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900828f     Document Type: Article

References (33)

1. Stadtman, T. C. (1973) Lysine metabolism by Clostridia. Adv. Enzymol. 28, 413-448.
2. Tang, K.-H., Chang, C. H., and Frey, P. A. (2001) Electron transfer in the substrate-dependent suicide inactivation of lysine 5,6-aminomutase. Biochemistry 40, 5190-5199.
3. Chang, C. H., and Frey, P. A. (2000) Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5,6-aminomutase from Clostridium sticklandii. J. Biol. Chem. 275, 106-114.
4. Tang, K.-H., Harms, A., and Frey, P. A. (2002) Identification of a novel pyridoxal 5′-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis. Biochemistry 41, 8767-8776.
5. Baker, J. J., van der Drift, C., and Stadtman, T. C. (1973) Purification and properties of β-lysine mutase, a pyridoxal phosphate and B12 coenzyme dependent enzyme. Biochemistry 12, 1054-1063.
6. Morley, C. D., and Stadtman, T. C. (1972) The role of pyridoxal phosphate in the B12 coenzyme-dependent D-α-lysine mutase reaction. Biochemistry 11, 600-605.
7. Retey, J., Kunz, F., Stadtman, T. C., and Arigoni, D. (1969) On the mechanism of the β-lysine-mutase reaction. Experientia 25, 801-802.
8. Tang, K. H., Casarez, A. D., Wu, W, and Frey, P. A. (2003) Kinetic and biochemical analysis of the mechanism of action of lysine 5,6-aminomutase. Arch. Biochem. Biophys. 418, 49-54.
9. Frey, P. A., and Magnusson, O. Th (2003) S-Adenosylmethionine: A wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chem. Rev. 103, 2129-2148.
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. Frey, P. A. (1990) Importance of organic radicals in enzymatic cleavage of unactivated C-H bonds. Chem. Rev. 90, 1343-1357.
13. Reed, G. H. (2004) Radical mechanisms in adenosylcobalamin-dependent enzymes. Curr. Opin. Chem. Biol. 8, 477-483.
14. Toraya, T. (2003) Radical catalysis in coenzyme B12-dependent isomerization (eliminating) reactions. Chem. Rev. 103, 2095-2127.
15. Maity, A. N., Hsieh, C.-P., Huang, M.-H., Chen, Y.-H., Tang, K.-H., Behshad, E., Frey, P. A., Ke, S.-C. (2009) Evidence for conformational movement and radical mechanism in the reaction of 4-thia-L-lysine with lysine 5,6-aminomutase. J. Phys. Chem. in press.
16. Mansoorabadi, S. O., Magnusson, O. T., Poyner, R. R., Frey, P. A., and Reed, G. H. (2006) Analysis of the cob(II)alamin-5′-deoxy-3′, 4′-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase. Biochemistry 45, 14362-14370.
17. Gerfen, G. J., Licht, S., Willems, J.-P., Hoffman, B. M., and Stubbe, J. (1996) Electron paramagnetic resonance studies of a kinetically competent intermediate in ribonucleotide reduction. J. Am. Chem. Soc. 118, 8192-8197.
18. Mansoorabadi, S. O., Padmakumar, R., Fazliddinova, N., Vlasie, M., Banerjee, R., and Reed, G. H. (2005) Characterization of a succinyl-CoA radical-cob(II)alamin spin triplet intermediate in the reaction catalyzed by adenosylcobalamin-dependent methylmalonyl-CoA mutase. Biochemistry 44, 3153-3158.
19. Bothe, H., Darley, D. J., Albracht, S. P. J., Gerfen, G. J., Golding, B. T., and Buckel, W. (1998) Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium. Biochemistry 37, 4105-4113.
20. 12-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol. Biochemistry 41, 8580-8588.
21. 15N)aminoethanesulfonic acid]. J. Labelled Compd. Radiopharm. 27, 1267-1273.
22. Cavallini, D., De Marco, C., Mondovi, B., and Azzone, G. F. (1955) A new synthetic sulfur-containing amino acid: S-Aminoethylcysteine. Experientia 11, 61-62.
23. Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
24. Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
25. Kauppinen, J. K., Moffatt, D. J., Mantsch, H. H., and Cameron, D. G. (1981) Fourier self-deconvolution: A method for resolving intrinsically overlapped bands. Appl. Spectrosc. 35, 271-276.
26. Latwesen, D. G., Poe, M., Leigh, J. S., and Reed, G. H. (1992) Electron paramagnetic resonance studies of a ras p21-MnIIGDP complex in solution. Biochemistry 31, 4946-4950.
27. Bandarian, V., and Reed, G. H. (1999) Hydrazine cation radical in the active site of ethanolamine ammonia-lyase: Mechanism-based inactivation by hydroxyethylhydrazine. Biochemistry 38, 12394-12402.
28. Miller, J., Bandarian, V., Reed, G. H., and Frey, P. A. (2001) Inhibition of lysine 2,3-aminomutase by the alternative substrate 4-thialysine and characterization of the 4-thialysyl radical intermediate. Arch. Biochem. Biophys. 387, 281-288.
29. Mansoorabadi, S. O., Reed, G. H. (2003) Effects of electron spin delocalization and non-collinearity of interaction terms in EPR triplet powder patterns, in Paramagnetic Resonance of Metallobiomolecules (Telser, J., Ed.) pp 82-96, American Chemical Society, Washington, D.C.
30. Sustman, R., and Korth, H.-G. (1990) The captodative effect. Adv. Phys. Org. Chem. 26, 131-178.
31. Sandala, G. M., Smith, D. M., and Radom, L. (2006) In search of radical intermediates in the reactions catalyzed by lysine 2,3-aminomutase and lysine 5,6-aminomutase. J. Am. Chem. Soc. 128, 16004-16005.
32. Wolthers, K. R., Rigby, S. E. J., and Scrutton, N. S. (2008) Mechanism of radical-based catalysis in the reaction catalyzed by adenosylcobalamin- dependent ornithine 4,5-aminomutase. J. Biol. Chem. 283, 34615-34625.
33. Frisch, M. J. et al. (1998) Gaussian 98, Gaussian, Inc., Pittsburgh, PA.