Navigating the B12 road: Assimilation, delivery, and disorders of cobalamin

Journal of Biological Chemistry

Volumn 288, Issue 19, 2013, Pages 13186-13193

  Gherasim, Carmen ^a   Lofgren, Michael ^a   Banerjee, Ruma ^a  

^a UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT-CARBON BOND; COFACTORS; EFFICIENT SYSTEMS; HIGH REACTIVITY; ISOMERIZATION REACTION; METHYL TRANSFERS; VITAMIN B-12;

ISOMERIZATION;

PROTEINS;

COBALAMIN; COBAMAMIDE; CYANOCOBALAMIN; MECOBALAMIN; METHIONINE SYNTHASE; METHYLMALONYL COENZYME A MUTASE;

ABSORPTION; BIOCHEMISTRY; CATALYSIS; CHEMICAL STRUCTURE; COBALAMIN DEFICIENCY; CONFORMATION; CYTOSOL; HUMAN; LYSOSOME MEMBRANE; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; REVIEW; TRANSPORT AT THE CELLULAR LEVEL; VITAMIN DEFICIENCY; VITAMIN METABOLISM;

ADENOSYLCOBALAMIN; COFACTORS; METABOLIC DISEASES; METAL HOMEOSTASIS; TRAFFICKING; VITAMINS;

5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE S-METHYLTRANSFERASE; ANIMALS; BIOLOGICAL TRANSPORT; COBALT; COENZYMES; GTP-BINDING PROTEINS; HUMANS; INTESTINAL ABSORPTION; LYSOSOMES; METHYLMALONYL-COA MUTASE; MITOCHONDRIA; MOLECULAR CONFORMATION; VITAMIN B 12;

EID: 84877708745     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R113.458810     Document Type: Review

References (79)

1. Waldron, K. J., Rutherford, J. C., Ford, D., and Robinson, N. J. (2009) Metalloproteins and metal sensing. Nature 460, 823-830
2. Boal, A. K., and Rosenzweig, A. C. (2009) Structural biology of copper trafficking. Chem. Rev. 109, 4760-4779
3. Hu, Y., and Ribbe, M. W. (2012) Nitrogenase assembly. Biochim. Biophys. Acta, DOI 10.1016/j.bbabio.2012.12.001
4. Reddi, A. R., Jensen, L. T., and Culotta, V. C. (2009) Manganese homeostasis in Saccharomyces cerevisiae. Chem. Rev. 109, 4722-4732
5. Lutsenko, S. (2010) Human copper homeostasis: a network of interconnected pathways. Curr. Opin. Chem. Biol. 14, 211-217
6. Fukada, T., Yamasaki, S., Nishida, K., Murakami, M., and Hirano, T. (2011) Zinc homeostasis and signaling in health and diseases: zinc signaling. J. Biol. Inorg. Chem. 16, 1123-1134
7. Lill, R. (2009) Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838
8. 12 trafficking. Curr. Opin. Chem. Biol. 13, 484-491
9. 12 trafficking in mammals: A for coenzyme escort service. ACS Chem. Biol. 1, 149-159
10. Shevell, M. I., and Rosenblatt, D. S. (1992) The neurology of cobalamin. Can. J. Neurol. Sci. 19, 472-486
11. 12. Nature 178, 64-66
12. 12: catalysis by cobalamin-dependent enzymes. Annu. Rev. Biochem. 72, 209-247
13. 12 by a trafficking chaperone. Proc. Natl. Acad. Sci. U.S.A. 105, 14551-14554
14. 12-binding domains of methionine synthase. Science 266, 1669-1674
15. 12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution. Structure 4, 339-350
16. Brown, K. L., and Hakimi, J. M. (1984) Heteronuclear NMR studies of cobalamins. 3. Phosphorus-31 NMR of aquocobalamin and various organocobalamins. J. Am. Chem. Soc. 106, 7894-7899
17. 12 at physiological temperatures: activation parameters for cobalt-carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactobacillus leichmannii. J. Inorg. Biochem. 77, 185-195
18. Waddington, M. D., and Finke, R. G. (1993) Neopentylcobalamin (neopentyl-B12) cobalt-carbon bond thermolysis products, kinetics, activation parameters, and bond dissociation energy: a chemical model exhibiting 106 of the 1012 enzymic activation of coenzyme B12's cobalt-carbon bond. J. Am. Chem. Soc. 115, 4629-4640
19. 12-binding proteins intrinsic factor, transcobalamin and haptocorrin. FEBS J. 199, 299-303
20. Fedosov, S. N., Berglund, L., Fedosova, N. U., Nexø, E., and Petersen, T. E. (2002) Comparative analysis of cobalamin binding kinetics and ligand protection for intrinsic factor, transcobalamin, and haptocorrin. J. Biol. Chem. 277, 9989-9996
21. 12 receptor, cubilin, cause hereditary megaloblastic anaemia 1. Nat. Genet. 21, 309-313
22. Quadros, E. V. (2010) Advances in the understanding of cobalamin assimilation and metabolism. Br. J. Haematol. 148, 195-204
23. Beedholm-Ebsen, R., van de Wetering, K., Hardlei, T., Nexø, E., Borst, P., and Moestrup, S. K. (2010) Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin. Blood 115, 1632-1639
24. 12 in normal human serum. Clin. Sci. Mol. Med. 53, 453-457
25. Seetharam, B., and Yammani, R. R. (2003) Cobalamin transport proteins and their cell-surface receptors. Expert Rev. Mol. Med. 5, 1-18
26. 12 transport by transcobalamin. Proc. Natl. Acad. Sci. U.S.A. 103, 4386-4391
27. Quadros, E. V., Nakayama, Y., and Sequeira, J. M. (2009) The protein and the gene encoding the receptor for the cellular uptake of transcobalaminbound cobalamin. Blood 113, 186-192
28. Li, N., Seetharam, S., and Seetharam, B. (1995) Genomic structure of human transcobalamin II: comparison to human intrinsic factor and transcobalamin I. Biochem. Biophys. Res. Commun. 208, 756-764
29. Kolhouse, J. F., Kondo, H., Allen, N. C., Podell, E., and Allen, R. H. (1978) Cobalamin analogues are present in human plasma and can mask cobalamin deficiency because current radioisotope dilution assays are not specific for true cobalamin. N. Engl. J. Med. 299, 785-792
30. 12 metabolism. Nat. Genet. 41, 234-239
31. 12 metabolism. Nat. Genet. 44, 1152-1155
32. Rosenblatt, D. S., Hosack, A., Matiaszuk, N. V., Cooper, B. A., and Laframboise, R. (1985) Defect in vitamin B12 release from lysosomes: newly described inborn error of vitamin B12 metabolism. Science 228, 1319-1321
33. 12 uptake. Biochemistry 44, 16301-16309
34. Lerner-Ellis, J. P., Tirone, J. C., Pawelek, P. D., Doré, C., Atkinson, J. L., Watkins, D., Morel, C. F., Fujiwara, T. M., Moras, E., Hosack, A. R., Dunbar, G. V., Antonicka, H., Forgetta, V., Dobson, C. M., Leclerc, D., Gravel, R. A., Shoubridge, E. A., Coulton, J. W., Lepage, P., Rommens, J. M., Morgan, K., and Rosenblatt, D. S. (2006) Identification of the gene responsible for methylmalonic aciduria and homocystinuria, cblC type. Nat. Genet. 38, 93-100
35. 12-processing enzyme. J. Biol. Chem. 286, 29780-29787
36. 12 metabolism. Mol. Genet. Metab. 107, 352-362
37. 12 processing function. Biochemistry 51, 5083-5090
38. 12 trafficking protein uses glutathione transferase activity for processing alkylcobalamins. J. Biol. Chem. 284, 33418-33424
39. Hannibal, L., Kim, J., Brasch, N. E., Wang, S., Rosenblatt, D. S., Banerjee, R., and Jacobsen, D. W. (2009) Processing of alkylcobalamins in mammalian cells: a role for the MMACHC(cblC) gene product. Mol. Genet. Metab. 97, 260-266
40. 12 metabolism. N. Engl. J. Med. 358, 1454-1464
41. Suormala, T., Baumgartner, M. R., Coelho, D., Zavadakova, P., Kozich, V., Koch, H. G., Berghaüser, M., Wraith, J. E., Burlina, A., Sewell, A., Herwig, J., and Fowler, B. (2004) The cblD defect causes either isolated or combined deficiency of methylcobalamin and adenosylcobalamin synthesis. J. Biol. Chem. 279, 42742-42749
42. Stucki, M., Coelho, D., Suormala, T., Burda, P., Fowler, B., and Baumgartner, M. R. (2012) Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism. Hum. Mol. Genet. 21, 1410-1418
43. Gherasim, C., Hannibal, L., Rajagopalan, D., Jacobsen, D. W., and Banerjee, R. (2013) The C-terminal domain of CblD interacts with CblC and influences intracellular cobalamin partitioning. Biochemie, 95, 1023-1032
44. Gulati, S., Baker, P., Li, Y. N., Fowler, B., Kruger, W., Brody, L. C., and Banerjee, R. (1996) Mutations in human methionine synthase in cblG patients. Hum. Mol. Genet. 5, 1859-1865
45. Leclerc, D., Campeau, E., Goyette, P., Adjalla, C. E., Christensen, B., Ross, M., Eydoux, P., Rosenblatt, D. S., Rozen, R., and Gravel, R. A. (1996) Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum. Mol. Genet. 5, 1867-1874
46. Chen, L. H., Liu, M.-L., Hwang, H.-Y., Chen, L.-S., Korenberg, J., and Shane, B. (1997) Human methionine synthase. cDNA cloning, gene localization, and expression. J. Biol. Chem. 272, 3628-3634
47. Matthews, R. G., Koutmos, M., and Datta, S. (2008) Cobalamin-dependent and cobamide-dependent methyltransferases. Curr. Opin. Struct. Biol. 18, 658-666
48. Watkins, D., and Rosenblatt, D. S. (1989) Functional methionine synthase deficiency (cblE and cblG): clinical and biochemical heterogeneity. Am. J. Med. Genet. 34, 427-434
49. 12-dependent enzymes. Annu. Rev. Biochem. 66, 269-313
50. Olteanu, H., and Banerjee, R. (2001) Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation. J. Biol. Chem. 276, 35558-35563
51. Olteanu, H., Munson, T., and Banerjee, R. (2002) Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase. Biochemistry 41, 13378-13385
52. Olteanu, H., Wolthers, K. R., Munro, A. W., Scrutton, N. S., and Banerjee, R. (2004) Kinetic and thermodynamic characterization of the common polymorphic variants of human methionine synthase reductase. Biochemistry 43, 1988-1997
53. Wolthers, K. R., Basran, J., Munro, A. W., and Scrutton, N. S. (2003) Molecular dissection of human methionine synthase reductase: determination of the flavin redox potentials in full-length enzyme and isolated flavin-binding domains. Biochemistry 42, 3911-3920
54. Banerjee, R. V., Harder, S. R., Ragsdale, S. W., and Matthews, R. G. (1990) Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study. Biochemistry 29, 1129-1135
55. Yamada, K., Gravel, R. A., Toraya, T., and Matthews, R. G. (2006) Human methionine synthase reductase is a molecular chaperone for human methionine synthase. Proc. Natl. Acad. Sci. U.S.A. 103, 9476-9481
56. Gulati, S., Chen, Z., Brody, L. C., Rosenblatt, D. S., and Banerjee, R. (1997) Defects in auxiliary redox proteins lead to functional methionine synthase deficiency. J. Biol. Chem. 272, 19171-19175
57. 12-dependent methylmalonic aciduria. Hum. Mol. Genet. 11, 3361-3369
58. Leal, N. A., Park, S. D., Kima, P. E., and Bobik, T. A. (2003) Identification of the human and bovine ATP:cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant. J. Biol. Chem. 278, 9227-9234
59. 12. Nat. Chem. Biol. 4, 194-196
60. 2+ cobalamin species upon binding to the human ATP:cobalamin adenosyltransferase. J. Am. Chem. Soc. 127, 7660-7661
61. 12 in human adenosyltransferase and its downstream target, methylmalonyl-CoA mutase. J. Am. Chem. Soc. 127, 526-527
62. 12? Trends Biochem. Sci. 30, 304-308
63. 12. Acc. Chem. Res. 16, 235-243
64. Mera, P. E., and Escalante-Semerena, J. C. (2010) Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins? J. Biol. Chem. 285, 2911-2917
65. Leal, N. A., Olteanu, H., Banerjee, R., and Bobik, T. A. (2004) Human ATP:cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase. J. Biol. Chem. 279, 47536-47542
66. 12. Appl. Microbiol. Biotechnol. 88, 41-48
67. 12 synthesis by adenosyltransferase. Biochemistry 48, 5350-5357
68. 12 delivery by a pathogenic mutation in adenosyltransferase. Biochemistry 50, 5790-5798
69. 12 loading and is corrupted in methylmalonic aciduria. Proc. Natl. Acad. Sci. U.S.A. 106, 21567-21572
70. Takahashi-Íñiguez, T., García-Arellano, H., Trujillo-Roldán, M. A., and Flores, M. E. (2011) Protection and reactivation of human methylmalonyl-CoA mutase by MMAA protein. Biochem. Biophys. Res. Commun. 404, 443-447
71. 12 metabolism. Hum. Mutat. 24, 509-516
72. 12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements. Proc. Natl. Acad. Sci. U.S.A. 99, 15554-15559
73. Korotkova, N., and Lidstrom, M. E. (2004) MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation. J. Biol. Chem. 279, 13652-13658
74. Padovani, D., and Banerjee, R. (2006) Assembly and protection of the radical enzyme, methylmalonyl-CoA mutase, by its chaperone. Biochemistry 45, 9300-9306
75. 12-dependent methylmalonyl-CoA mutase. J. Biol. Chem. 281, 17838-17844
76. Hubbard, P. A., Padovani, D., Labunska, T., Mahlstedt, S. A., Banerjee, R., and Drennan, C. L. (2007) Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduria. J. Biol. Chem. 282, 31308-31316
77. 12-dependent methylmalonyl-CoA mutase and insight into their complex formation. J. Biol. Chem. 285, 38204-38213
78. Pérez, B., Angaroni, C., Sánchez-Alcudia, R., Merinero, B., Pérez-Cerdá, C., Specola, N., Rodríguez-Pombo, P., Wajner, M., de Kremer, R. D., Cornejo, V., Desviat, L. R., and Ugarte, M. (2010) The molecular landscape of propionic acidemia and methylmalonic aciduria in Latin America. J. Inherit. Metab. Dis. 33, S307-S314
79. Dempsey-Nunez, L., Illson, M. L., Kent, J., Huang, Q., Brebner, A., Watkins, D., Gilfix, B. M., Wittwer, C. T., and Rosenblatt, D. S. (2012) High resolution melting analysis of the MMAA gene in patients with cblA and in those with undiagnosed methylmalonic aciduria. Mol. Genet. Metab. 107, 363-367