The mechanism of 7,8-diaminopelargonate synthase; the role of S-adenosylmethionine as the amino donor

Organic and Biomolecular Chemistry

Volumn 1, Issue 20, 2003, Pages 3498-3499

  Breen, Rachel S ^a   Campopiano, Dominic J ^a   Webster, Scott ^a   Brunton, Mhairi ^a   Watt, Rory ^a   Baxter, Robert L ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CARBOXYLATION; CATALYSIS; CRYSTAL STRUCTURE; ENZYME KINETICS; SYNTHESIS (CHEMICAL);

AMINO DONORS;

AMINES;

EID: 0142258247     PISSN: 14770520     EISSN: None     Source Type: Journal    
DOI: 10.1039/b310443p     Document Type: Article

References (18)

1. M. A. Eisenberg, Adv. Enzymol., 1973, 38, 317; M. A. Eisenberg, Biosynthesis of Biotin and Lipoic Acid, vol. 1, American Society for Microbiology, Washington DC, 1987.
2. M. A. Eisenberg, Adv. Enzymol., 1973, 38, 317; M. A. Eisenberg, Biosynthesis of Biotin and Lipoic Acid, vol. 1, American Society for Microbiology, Washington DC, 1987.
3. A. R. Rendina, W. S. Taylor, K. Gibson, G. Lorimer, D. Raynor, B. Locket, K. Kranis, B. Wexler, D. Marcovici-Mizrahi, A. Nudelman, A. Nudelman, E. Marsilii, C. Hongji, Z. Wawrzak, J. Calabrese, W. Huang, J. Jia, G. Schneider, Y. Linquist and G. Yang, J. Pestic. Sci., 1999, 55, 236; O. Ploux, O. Breyne, S. Carillon and A. Marquet, Eur. J. Biochem., 1999, 259, 63.
4. A. R. Rendina, W. S. Taylor, K. Gibson, G. Lorimer, D. Raynor, B. Locket, K. Kranis, B. Wexler, D. Marcovici-Mizrahi, A. Nudelman, A. Nudelman, E. Marsilii, C. Hongji, Z. Wawrzak, J. Calabrese, W. Huang, J. Jia, G. Schneider, Y. Linquist and G. Yang, J. Pestic. Sci., 1999, 55, 236; O. Ploux, O. Breyne, S. Carillon and A. Marquet, Eur. J. Biochem., 1999, 259, 63.
5. G. L. Stoner and M. A. Eisenberg, J. Biol. Chem., 1975, 259, 4029; G. L. Stoner and M. A. Eisenberg, J. Biol. Chem., 1975, 259, 4037.
6. G. L. Stoner and M. A. Eisenberg, J. Biol. Chem., 1975, 259, 4029; G. L. Stoner and M. A. Eisenberg, J. Biol. Chem., 1975, 259, 4037.
7. J. L. Martin and F. M. McMillan, Curr. Opin. Struct. Biol., 2002, 12, 783.
8. P. A. Frey and O. T. Magnusson, Chem. Rev., 2003, 103, 2129.
9. H. Kack, J. Sandmark, K. Gibson, G. Schneider and Y. Linqvist, J. Mol. Biol., 1999, 291, 857.
10. A. C. Elliot, J. Sandmark, G. Schneider and J. F. Kirsch, Biochemistry, 2002, 41, 12582.
11. J. Sandmark, S. Mann, A. Marquet and G. Schneider, J. Biol. Chem., 2002, 277, 43352.
12. S. Kuramitsu, K. Hiromi, H. Hayashi, Y. Morino and H. Kagamiyama, Biochemistry, 1990, 29, 5469.
13. C. M. Leir, J. Org. Chem., 1972, 37, 887.
14. Commercially available SAM is a ∼3: 2 mixture of the S and R forms and can contain up to 10% 5′ -methylthioadenosine. SAM used in these experiments was purified by HPLC and contained less than 1% 5′ -methylthioadenosine. The unnatural R isomer is not a substrate (see ref. 7).
15. Steady state incubations were typically carried out at 37 °C in 20 mM potassium phosphate buffer (pH 7.5) containing 20 μM DAPA synthase (equilibrated with 100 μM PLP), 1 mM SAM and 6 μM (±)-1.
16. -1 the retention times of SAM, 3, 4 and 5′ thioadenosine were 3.9, 4.0, 4.9 and 21.4 min respectively.
17. V. Zappia, C. R. Zydek-Cwick and F. Schlenk, J. Biol. Chem., 1969, 244, 4499.
18. 2 signal (at 51.6 ppm in the spectrum of SAM). Fully concordant MS, NMR and UV data were obtained for the product. The stereochemistry of the 2-hydroxyl group was not determined.