Re-face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase fromMethylobacterium extorquensAM1 as determined by NMR spectroscopy
- 4 April 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 494 (1) , 95-98
- https://doi.org/10.1016/s0014-5793(01)02306-7
Abstract
MtdA catalyzes the dehydrogenation of N(5),N(10)-methylenetetrahydromethanopterin (methylene-H4MPT) with NADP(+) as electron acceptor. In the reaction two prochiral centers are involved, C14a of methylene-H4MPT and C4 of NADP(+), between which a hydride is transferred. The two diastereotopic protons at C14a of methylene-H4MPT and at C4 of NADPH can be seen separately in 1H-NMR spectra. This fact was used to determine the stereospecificity of the enzyme. With (14aR)-[14a-2H(1)]-[14a-13C]methylene-H4MPT as the substrate, it was found that the pro-R hydrogen of methylene-H4MPT is transferred by MtdA into the pro-R position of NADPH.Keywords
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