Glutamate decarboxylase like 1 (GADL1)

Glutamate decarboxylase like 1 (GADL1) is a **PLP-dependent enzyme** primarily responsible for the decarboxylation of **aspartate to β-alanine** and **cysteine sulfinic acid to hypotaurine**; these reactions support the endogenous synthesis of peptides like carnosine and compounds such as taurine, which play key neuroprotective and antioxidant roles[1][3][5][7]. Structurally related to CSAD (cysteine sulfinic acid decarboxylase) and GAD (glutamate decarboxylase), GADL1 does not actually process glutamate as a substrate and is not involved in GABA synthesis[6][7]. GADL1 is expressed notably in skeletal muscle, kidney, and brain regions such as the olfactory bulb, with tissue-specific roles confirmed in murine knockout models[4][5][6]. Functionally, GADL1 influences cellular migration and morphology in some contexts[2]. Variants in the GADL1 gene are associated with blood carnosine levels, implicating GADL1 more broadly in *beta-alanine* and *carnosine* peptide metabolism in mammals[5]. No approved drugs directly target GADL1, and while it has been explored as a novel metabolic and neuroprotective target, therapeutic development is in early stages.

Other names

Acidic amino acid decarboxylase GADL1ADCCSADCHuADCHuCSADCaspartate 1-decarboxylasecysteine sulfinic acid decarboxylaseglutamate decarboxylase-like protein 1

Not fully established for therapeutic drugs, but enzyme inhibitors of GADL1's ADC activity have been described in biochemical screening[6] Lithium may suppress cell migration via signaling that overlaps with GADL1 function[2]