Gene

Spectroscopy

Quantum mechanics

Catalysis

Acceptor

Photochemistry

Methylene

Methanol dehydrogenase

Nuclear magnetic resonance spectroscopy

Biochemistry

Stereospecificity

16S ribosomal RNA

Stereochemistry

Medicinal chemistry

Physics

Organic chemistry

Methylobacterium

Dehydrogenation

Enzyme

Dehydrogenase

Condensed matter physics

Chemistry

FEBS Letters

MtdA catalyzes the dehydrogenation of N 5 , N 10 ‐methylenetetrahydromethanopterin (methylene‐H 4 MPT) with NADP + as electron acceptor. In the reaction two prochiral centers are involved, C14a of methylene‐H 4 MPT and C4 of NADP + , between which a hydride is transferred. The two diastereotopic protons at C14a of methylene‐H 4 MPT and at C4 of NADPH can be seen separately in 1 H‐NMR spectra. This fact was used to determine the stereospecificity of the enzyme. With (14a R )‐[14a‐ 2 H 1 ]‐[14a‐ 13 C]methylene‐H 4 MPT as the substrate, it was found that the pro‐R hydrogen of methylene‐H 4 MPT is transferred by MtdA into the pro‐R position of NADPH.

<i>Re</i>‐face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from <i>Methylobacterium extorquens</i> AM1 as determined by NMR spectroscopy

Re‐face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy