Alanine dehydrogenase (ALD)

Alanine dehydrogenase (ALD) is an enzyme that catalyzes the reversible oxidative deamination of L-alanine to pyruvate, with concurrent reduction of NAD+ to NADH. It is a homo-hexameric enzyme, widely found in bacteria, and plays a critical role in microbial carbon and nitrogen metabolism by enabling the interconversion of alanine and pyruvate for energy generation and biosynthetic reactions[1][2][4][6]. It participates in key metabolic pathways—including the tricarboxylic acid (TCA) cycle, taurine and hypotaurine metabolism, and CO2 fixation[2][3][4]. In some pathogenic bacteria, alanine dehydrogenase serves as a secreted antigen and virulence factor during infection[5]. In general, it is not a major therapeutic target in current clinical drug discovery, but its role as a microbial antigen may have diagnostic applications[5]. The enzyme is not known to interact with specific approved drugs.

Other names

L-alanine dehydrogenaseAlaDHNAD+-linked alanine dehydrogenasealpha-alanine dehydrogenaseNAD+-dependent alanine dehydrogenasealanine oxidoreductaseNADH-dependent alanine dehydrogenase

Catalysis of NAD+-dependent reversible conversion of L-alanine and pyruvate via hydride transfer and deamination (targeted as an antigen/virulence factor in some bacterial pathogens)