Abstract
Vitamin B12, in its coenzyme form, plays an essential role in mammalian metabolism where it serves as an obligatory cofactor for methylmalonyl-CoA mutase, which mediates the carbon skeleton rearrangement of methylmalonyl-CoA to succinyl-CoA1 (eq 1). The purpose of this enzymic rearrangement
is to conduct propionate, by way of methylmalonate and succinate, to the Krebs cycle and the main stream of biochemical metabolism.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References and Notes
J. Katz and I. L. Chaikoff, J. Am. Chem. Soc. 77, 2659 (1955).
M. Flavin and S. Ochoa, J. Biol. Chem., 229, 965 (1957).
E. R. Stadtman, P. Overath, H. Eggerer and F. Lynen, Biochem. Biophys. Res. Commun., 2, 1 (1960).
J. R. Stern, and D. L. Friedman, Biochem. Biophys. Res. Commun., 2, 82 (1960).
H. Eggerer, P. Overath, F. Lynen and E. R. Stadtman, Biochem. Biophys. Res. Commun., 82, 2643 (1960).
S. Gurnani, S. P. Mistry, and B. C. Johnson, Biochim. Biophys. Acta, 38, 187 (1960).
R. Stjernholm and H. G. Wood, Froc. Nat. Acad. Sci., USA, 47, 303 (1961).
For cobalt-based methylmalonate models see: (a) P. Dowd and M. Shapiro, Tetrahedron, 40, 3063 (1984)
P. Dowd and M. Shapiro, J. Am. Chem. Soc., 98, 3724 (1976).
G. Bidlingmaier, H. Flohr, U. M. Kempf, T. Krebs and J. Rétey, Angezv. Chem. Int. Ed. Engl., 15, 613 (1976).
H. Flohr, W. Pannhorst and J. Rétey, Helv. Chim. Acta., 61, 1565 (1978).
J. Rétey, in Vitamin B 12, B. Zagalak, W. Friedrich, Eds.; Walter de Gruyter, Berlin, pp 439–460 (1979).
A. I. Scott and K. Kang, J. Am. Chem. Soc., 99, 1997 (1977)
A. I. Scott, J. Kang, D. Dalton and S. K. Chung, J. Am. Chem. Soc, 100, 3603 (1978)
A. I. Scott, J. Kang, P. Dowd and B. K. Trivedi, Bioorganic Chem., 9, 426 (1980)
A. L Scott, J. B. Hansen and S. K. Chung, J. Chem. Soc, Chem. Comm., 388 (1980).
J. Halpern, Science, (Washington, D. C.) 227, 869 (1985).
S. Wollowitz and J. Halpern, J. Am. Chem. Soc, 110, 3112 (1988).
S. Wollowitz and J. Halpern, J. Am. Chem. Soc, 106, 8319 (1984).
G. Choi, S.-C. Choi, A. Galan, B. Wilk and P. Dowd, Proc Nat. Acad Sci. USA, in press.
The structure of this product was established by spectroscopic comparison with an independently synthesized authentic sample.
See: (a) A. L. J. Beckwith, Tetrahedron, 37, 3078 (1981).
A. L. J. Beckwith and C. H. Schlesser, Tetrahedron, 41, 3930 (1985).
A. L. J. Beckwith and G. Moad, J. Chem. Soc, Chem. Commun.,472 (1974).
See, for example, R. Breslow and P. L. Khanna, J. Am. Chem. Soc., 98, 1297 (1976).
A. Ghosez, T, Göbel and B, Giese, Chem. Ber., 121, 1807 (1988).
At 25 °C. the parent 5-hexenyl radical cyclizes 40 times faster than the parent 6-heptenyl radical.6b.
C. Chatgillaloglu, K. U. Ingold, and J. C Scaiano, J. Am. Chem. Soc, 103, 7739 (1981).
J. J. B. Cannata, A. Focasi, Jr., R. Mazumder, R. C. Warner, and S. Ochoa, J. Biol. Chem., 240, 3249 (1965).
W. W. Miller and J. H. Richards, J. Am. Chem. Soc., 91, 1498 (1969).
This research was generously supported by the National Institute for General Medical Sciences of the National Institutes of Health under Grant GM 19906.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Springer Science+Business Media New York
About this chapter
Cite this chapter
Dowd, P., Choi, G., Wilk, B., Choi, SC., Zhang, S., Shepherd, R.E. (1990). On the Mechanism of Action of Vitamin B12: A Non-Free Radical Model for the Methylmalonyl-CoA — Succinyl-CoA Rearrangement. In: Baldwin, T.O., Raushel, F.M., Scott, A.I. (eds) Chemical Aspects of Enzyme Biotechnology. Industry-University Cooperative Chemistry Program Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9637-7_19
Download citation
DOI: https://doi.org/10.1007/978-1-4757-9637-7_19
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-9639-1
Online ISBN: 978-1-4757-9637-7
eBook Packages: Springer Book Archive