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Introduction

Structure

domains

This is the

Active Site

Function

Mechanism

The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine.

Mechanism

Hydrophobic Pocket

The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The shown in green surrounds the FAD in a way such that it exposes the that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.

Disease

Relevance

Structural highlights

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