TAILIEUCHUNG - Báo cáo khoa học: Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase–methionine synthase reductase complex

Human methionine synthase reductase (MSR), a diflavin enzyme, restores the activity of human methionine synthase through reductive methylation of methionine synthase (MS)-bound cob(II)alamin. Recently, it was also reported that MSR enhances uptake of cobalamin by apo-MS, a role asso-ciated with the MSR-catalysed reduction of exogenous aquacob(III)alamin to cob(II)alamin [Yamada K, Gravel RA, TorayaT & Matthews RG (2006) Proc Natl Acad Sci USA103, 9476–9481]. Here, we report the expression and purification of human methionine synthase from Pichia pastoris. . | ễFEBS Journal Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex Kirsten R. Wolthers and Nigel S. Scrutton Manchester Interdisciplinary Biocentre and Faculty of Life Sciences University of Manchester UK Keywords chaperone cobalamin diflavin reductase methionine synthase methionine synthase reductase Correspondence N. S. Scrutton Manchester Interdisciplinary Biocentre and Faculty of Life Sciences University of Manchester 131 Princess Street Manchester M1 7DN UK Fax 44 161 306 8918 Tel 44 161 306 5153 E-mail Received 30 November 2008 revised 8 January 2009 accepted 21 January 2009 doi Human methionine synthase reductase MSR a diflavin enzyme restores the activity of human methionine synthase through reductive methylation of methionine synthase MS -bound cob II alamin. Recently it was also reported that MSR enhances uptake of cobalamin by apo-MS a role associated with the MSR-catalysed reduction of exogenous aquacob III alamin to cob II alamin Yamada K Gravel RA TorayaT Matthews RG 2006 Proc Natl Acad Sci USA 103 9476-9481 . Here we report the expression and purification of human methionine synthase from Pichia pastoris. This has enabled us to assess the ability of human MSR and two other structurally related diflavin reductase enzymes cytochrome P450 reductase and the reductase domain of neuronal nitric oxide synthase to a stimulate formation of holo-MS from aquacob III alamin and the apo-form of MS and b reactivate the inert cob II alamin form of MS that accumulates during enzyme catalysis. Of the three diflavin reductases studied cytochrome P450 reductase had the highest turnover rate s-1 for aquacob III alamin reduction and the reductase domain of neuronal nitric oxide synthase elicited the highest specificity kcat Km of X 105 M-1-s-1 and MSR had the lowest Km pM for the cofactor. Despite the .

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