GADL1
Description
The GADL1 (glutamate decarboxylase like 1) is a protein-coding gene located on chromosome 3.
GADL1, or Glutamate decarboxylase like 1, is an enzyme that plays a crucial role in the production of beta-alanine, hypotaurine, and taurine. It achieves this by decarboxylating aspartate to beta-alanine and cysteine sulfinic acid to hypotaurine. This process involves the removal of a carboxyl group from these molecules. GADL1 requires pyridoxal 5'-phosphate (PLP) as a cofactor to function.
The production of beta-alanine by GADL1 is essential for the synthesis of carnosine, a compound known for its diverse biological functions. Carnosine, along with taurine, contributes to calcium regulation, pH buffering, metal chelation, and antioxidant activity. Beta-alanine itself also acts as a neurotransmitter or neuromodulator in the central nervous system (CNS) and olfactory bulbs.
GADL1 shares significant homology (61%) with cysteine sulfinic acid decarboxylase (CSAD), another PLP-dependent enzyme. CSAD is involved in the production of taurine by decarboxylating cysteine sulfinic acid to hypotaurine. Taurine, a highly abundant amino acid in mammals, plays various roles, including antioxidant activity, membrane stabilization, and neurotransmitter/neuromodulator function in the CNS. Notably, taurine has gained increasing attention as a biomarker for various diseases.
In terms of tissue distribution, both GADL1 and CSAD are expressed in the brain and neurons. However, only CSAD is found in the liver in humans. In mice, both enzymes are present in the brain, olfactory bulbs, and skeletal muscle, while only CSAD is found in the kidney and liver.
GADL1 is also known as ADC, CSADC, HuADC, HuCSADC.
