threonine racemase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-threonine = D-threonine. [EC:5.1.1.6, RHEA:13913]

Threonine racemase activity is a crucial enzyme involved in the interconversion of L-threonine and D-threonine. This process occurs via an amino-acid racemization reaction, where the stereochemistry around the alpha-carbon of threonine is inverted. L-threonine is the naturally occurring enantiomer utilized in protein biosynthesis, while D-threonine is considered a non-canonical amino acid. The enzymatic activity of threonine racemase is catalyzed by a pyridoxal phosphate (PLP)-dependent mechanism. The active site of the enzyme binds to L-threonine, facilitating the removal of a proton from the alpha-carbon, leading to the formation of a carbanion intermediate. This intermediate is then protonated on the opposite side of the molecule, resulting in the formation of D-threonine. The conversion of L-threonine to D-threonine serves a variety of biological roles. In bacteria, D-threonine is utilized in the biosynthesis of peptidoglycans, a major component of bacterial cell walls. In mammals, D-threonine has been linked to the regulation of immune function and neuronal signaling. Furthermore, threonine racemase activity has been implicated in various diseases, including cancer and neurodegenerative disorders. The dysregulation of threonine racemase activity has been associated with cellular proliferation, survival, and inflammation, highlighting its potential as a therapeutic target.'
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Proteins (1)

Compounds (9)