A2LD1 Human

The A2LD1 gene is located on chromosome 13q32.3 and spans approximately 2.2 kb. It contains two exons, with only the second exon being protein-coding . The protein itself is composed of 153 amino acids and has a calculated molecular mass of 17.3 kDa .

A2LD1 is involved in the breakdown of the isodipeptide L-gamma-glutamyl-L-epsilon-lysine, a product of fibrin degradation. This process is catalyzed by the enzyme gamma-glutamylamine cyclotransferase, which cyclizes the gamma-glutamyl moiety to produce 5-oxo-L-proline and free alkylamine . The enzyme is inactive against L-gamma-glutamyl-alpha amino acids .

The crystal structure of recombinant human GGACT reveals a 5-stranded beta barrel decorated with helices and connecting loops, including characteristic crossover strands . This structure is similar to that of GGCT, despite the two proteins sharing less than 10% amino acid identity, indicating convergent evolution in their catalytic mechanisms .

Recombinant human A2LD1 protein is typically expressed in Escherichia coli and purified using conventional chromatography techniques . The recombinant protein is often tagged with a His tag at the N-terminus to facilitate purification . It is used in various applications, including SDS-PAGE and mass spectrometry (MS), and is available with a purity of over 95% .

The recombinant A2LD1 protein is valuable in research focused on understanding the biochemical pathways involved in protein degradation and the role of crosslinked fibrin in blood clotting. It is also used in high-throughput screening assays and other experimental setups to study its enzymatic activity and structural properties .