Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme

Biochemistry

Volumn 48, Issue 14, 2009, Pages 3138-3145

  Mera, Paola E ^a   Maurice, Martin St ^a,b   Rayment, Ivan ^a   Escalante Semerena, Jorge C ^a,c  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b Marquette University   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CRYSTAL STRUCTURE; EFFICIENCY; ENZYME ACTIVITY; HYDROPHOBICITY;

5 ,6-DIMETHYLBENZIMIDAZOLE; CATALYTIC EFFICIENCIES; COORDINATION BONDS; HIGH RESOLUTION CRYSTAL STRUCTURE; HYDROPHOBIC RESIDUES; LACTOBACILLUS REUTERI; ORDERS OF MAGNITUDE; WILD-TYPE PROTEINS;

COBALT COMPOUNDS;

ADENOSINE TRIPHOSPHATE; CBL PROTEIN; COBALAMIN DERIVATIVE; COBALT; CORRINOID; CORRINOID ADENOSYLTRANSFERASE; CYANOCOBALAMIN; ENZYME; HISTIDINE; MUTANT PROTEIN; PHENYLALANINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; BIOSYNTHESIS; CATALYSIS; CHEMICAL BOND; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; HUMAN; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; KINETICS; LACTOBACILLUS REUTERI; PRIORITY JOURNAL; PROTEIN INTERACTION; RESIDUE ANALYSIS; SUBSTITUTION REACTION; WILD TYPE;

LACTOBACILLUS REUTERI;

EID: 65249146045     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9000134     Document Type: Article

References (41)

1. 12-dependent rearrangements. Science 227, 869-875.
2. Banerjee, R., and Chowdhury, S. (1999) Methylmalonyl-CoA mutase. In Chemistry and Biochemistry of B12 (Banerjee, R, Ed.) pp 707-729, John Wiley & Sons, Inc., New York.
3. Buckel, W., Bröker, G., Bothe, H., and Pierik, A. (1999) Glutamate mutase and 2-Methylglutarate mutase. In Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 757-782, John Wiley & Sons, Inc., New York.
4. Bandarian, V., and Reed, G. H. (1999) Ethanolamine ammonia-lyase. In Chemistry ad Biochemistry of B12 (Banerjee, R., Ed.) pp 811-833, John Wiley & Sons, Inc., New York.
5. Toraya, T. (1999) Diol dehydratase and glycerol dehydratase. In Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 783-809, John Wiley & Sons, Inc., New York.
6. Fontecave, M. (1998) Ribonucleotide reductases and radical reactions. Cell. Mol. Life Sci. 54, 684-695.
7. Fontecave, M., and Mulliez, E. (1999) Ribonucleotide Reductases. In Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 731 -756, John Wiley & Sons, Inc., New York.
8. Wohlfarth, G., and Diekert, G. (1999) Reductive dehalogenases. In Chemistry and Biochemistry of B12 (Banerjee, R., Ed.) pp 871 -893, John Wiley & Sons, Inc., New York.
9. Gartner, P., Ecker, A., Fischer, R., Linder, D., Fuchs, G., and Thauer, R. K. (1993) Purification and properties of N5-methyltet-rahydromethanopterin: coenzyme M methyltransferase from Metha-nobacterium thermoautotrophicum. Eur. J. Biochem. 213, 537-545.
10. Taylor, R. T., and Weissbach, H. (1973) N5-Methylenetetrahy-drofolate- homocysteine methyltransferases. In The Enzymes (Boyer, P. D., Ed.) pp 121 - 165, Academic Press, Inc., New York.
11. van der Meijden, P., Brommelstroet, B. W. t., Poiroit, C. M., van der Drift, C., and Vogels, G. D. (1984) Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri. J. Bacteriol. 160, 629-635.
12. Mancia, F., Keep, N. H., Nakagawa, A., Leadlay, P. F., Mc-Sweeney, S., Rasmussen, B., Bosecke, P., Diat, O., and Evans, P. R. (1996) How coenzyme B12 radicals are generated: The crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution. Structure 4, 339-350.
13. 12-binding domains of methionine synthase. Science 266, 1669-1674.
14. Fonseca, M. V., and Escalante-Semerena, J. C. (2000) Reduction of cob(III)alamin to cob(II)alamin in Salmonella enterica Serovar Typhimurium LT2. J. Bacteriol. 182, 4304-4309.
15. + oxidoreductase and flavodoxin: Key components of electron transfer in Escherichia coli. Eur. J. Biochem. 257, 577-585.
16. 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.
17. 2+cobalamin species upon binding to the human ATP: cobalamin adenosyltransferase. J. Am. Chem. Soc. 127, 7660-7661.
18. Stich, T. A., Buan, N. R., Escalante-Semerena, J. C., and Brunold, T. C. (2005) Spectroscopic and computational studies of the ATP: Corrinoid adenosyltransferase (CobA) from Salmonella enterica: Insights into the mechanism of adenosylcobalamin biosynthesis. J. Am. Chem. Soc. 127, 8710-8719.
19. Park, K., Mera, P. E., Escalante-Semerena, J. C., and Brunold, T. C. (2008) Kinetic and spectroscopic studies of the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri: Substrate specificity and insights into the mechanism of Co(II)corrinoid reduction. Biochemistry 47, 9007-9015.
20. Yamanishi, M., Labunska, T., and Banerjee, R. (2005) Mirror "base-off conformation of coenzyme B12 in human adenosyltransferase and its downstream target, methylmalonyl-CoA mutase. J. Am. Chem. Soc. 127, 526-527.
21. St Maurice, M., Mera, P., Park, K., Brunold, T. C., Escalante-Semerena, J. C., and Rayment, I. (2008) Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate. Biochemistry 47, 5755-5766.
22. Rocco, C. J., Dennison, K. L., Klenchin, V. A., Rayment, I., and Escalante-Semerena, J. C. (2008) Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli. Plasmid 59, 231-237.
23. St Maurice, M., Mera, P. E., Taranto, M. P., Sesma, F., Escalante-Semerena, J. C., and Rayment, I. (2007) Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri. J. Biol. Chem. 282, 2596-2605.
24. Blommel, P. G., and Fox, B. G. (2007) A combined approach to improving large-scale production of tobacco etch virus protease. Protein Expression Purif. 55, 53-68.
25. Hall, D. A., Jordan-Starck, T. C., Loo, R. O., Ludwig, M. L., and Matthews, R. G. (2000) Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry 39, 10711-10719.
26. Fonseca, M. V., and Escalante-Semerena, J. C. (2001) An in vitro reducing system for the enzymic conversion of cobalamin to adenosylcobalamin. J. Biol. Chem. 276, 32101-32108.
27. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
28. Vagin, A., and Teplyakov, A. (1997) J. Appl. Crystallogr. 30, 1022-1025.
29. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the Maximum-Likelihood Method. Acta Crystallogr. D53, 240-255.
30. Emsley, P., and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr. D60, 2126-2132.
31. Escalante-Semerena, J. C., Suh, S. J., and Roth, J. R. (1990) cobA function is required for both de novo cobalamin biosynthesis and assimilation of exogenous corrinoids in Salmonella typhimurium. J. Bacteriol. 172, 273-280.
32. Suh, S., and Escalante-Semerena, J. C. (1995) Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium. J. Bacteriol. 177, 921-925.
33. Berkowitz, D., Hushon, J. M., Whitfield, H. J., Jr., Roth, J., and Ames, B. N. (1968) Procedure for identifying nonsense mutations. J. Bacteriol. 96, 215-220.
34. Schubert, H. L., and Hill, C. P. (2006) Structure of ATP-bound human ATP:cobalamin adenosyltransferase. Biochemistry 45, 15188-15196.
35. Fan, C., and Bobik, T. A. (2008) Functional characterization and mutation analysis of human ATP:Cob(I)alamin adenosyltransferase. Biochemistry 47, 2806-2813.
36. Marsh, E. N., and Holloway, D. E. (1992) Cloning and sequencing of glutamate mutase component S from Clostridium tetanomor-phum. Homologies with other cobalamin-dependent enzymes. FEBS Lett. 310, 167-170.
37. Reitzer, R., Gruber, K., Jogl, G., Wagner, U. G., Bothe, H., Buckel, W., and Kratky, C. (1999) Glutamate mutase from Clostridium cochlearium: The structure of a coenzyme B12-dependent enzyme provides new mechanistic insights. Struct. Folding Des. 7, 891- 902.
38. Cook, F. C., and Cleland, W. W. (2007) Enzyme Kinetics and Mechanism, Taylor & Francis Group, LLC., New York.
39. Liu, D., Williamson, D. A., Kennedy, M. L., Williams, T. D., Morton, M. M., and Benson, D. R. (1999) Aromatic side chain-porphyrin interactions in designed hemoproteins. J. Am. Chem. Soc. 121, 11798-11812.
40. 12. Nat. Chem. Biol. 4, 194-196.
41. Lerner-Ellis, J. P., Gradinger, A. B., Watkins, D., Tirone, J. C., Villeneuve, A., Dobson, C. M., Montpetit, A., Lepage, P., Gravel, R. A., and Rosenblatt, D. S. (2006) Mutation and biochemical analysis of patients belonging to the cblB complementation class of vitamin B12-dependent methylmalonic aciduria. Mol. Genet. Metab. 87, 219-225.