ASS1
ASS1 (argininosuccinate synthase 1, also known as CTLN1 or ASS) is a cytosolic ligase of the urea cycle. It catalyses the formation of argininosuccinate from aspartate, citrulline and ATP, and contributes to arginine biosynthesis in most body tissues. Browse Assay Genie's current range of ASS1 research reagents below, or read on for the biology behind the target.
ASS1 is one of the enzymes of the urea cycle, the metabolic pathway that converts neurotoxic ammonia produced by protein catabolism into innocuous urea in the liver of ureotelic animals. The enzyme catalyses the formation of argininosuccinate from aspartate, citrulline and ATP. Together with ASL, it is responsible for the biosynthesis of arginine in most body tissues, and it catalyses the penultimate step of the arginine biosynthetic pathway.
ASS1 is a member of the ligase gene group and belongs to the argininosuccinate synthase family, Type 1 subfamily. The protein localises to the cytosol. The ASS1 gene on chromosome 9 appears to be the only functional gene for argininosuccinate synthetase in the human genome. Roughly 10 to 14 copies of the sequence, including pseudogenes, are scattered across the genome. Two transcript variants have been described, and both encode the same protein. Mouse and rat each carry an Ass1 ortholog, which allows the enzyme to be studied in common rodent models.
The enzyme was formerly named argininosuccinate synthetase, and the gene has also been listed under the symbols ASS and CTLN1. The CTLN1 alias reflects the disease link: mutations in the chromosome 9 copy of the gene cause citrullinemia. Researchers working on the ASS1 gene or ASS1 protein therefore tend to focus on urea cycle function, arginine supply and the biochemical basis of this disorder.
ASS1 is a core urea cycle enzyme that helps convert neurotoxic ammonia from protein catabolism into urea in the liver.
With ASL, ASS1 is responsible for arginine biosynthesis in most body tissues, making it central to studies of arginine supply.
Mutations in the chromosome 9 copy of the ASS1 gene cause citrullinemia, so the enzyme is a focus for studying this disorder.
ASS1 is an ATP-dependent ligase of the argininosuccinate synthase family, useful for studying aspartate and citrulline condensation.
ASS1 is a urea cycle enzyme that catalyses the formation of argininosuccinate from aspartate, citrulline and ATP. Together with ASL, it drives arginine biosynthesis in most body tissues. In the liver, the urea cycle converts neurotoxic ammonia from protein catabolism into urea.
ASS1 stands for argininosuccinate synthase 1. The enzyme was previously called argininosuccinate synthetase, and the gene has also appeared as ASS and CTLN1. The UniProt entry is named argininosuccinate synthase. NCBI reports two transcript variants that encode the same protein.
Mouse and rat both have an Ass1 ortholog. In humans, the functional gene is on chromosome 9, and mutations in it cause citrullinemia. Other copies scattered across the genome are pseudogenes. Check the datasheet of any product for its validated reactivity.
Other urea cycle enzymes, arginine metabolism targets and related metabolic enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P00966; product specifications from Assay Genie datasheets.