MTAP
MTAP (methylthioadenosine phosphorylase, also known as MSAP and c86fus) is a phosphorylase that breaks down S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis. It supports the salvage of both adenine and methionine. Browse Assay Genie's current range of MTAP research reagents below, or read on for the biology behind the target.
MTAP catalyses the phosphorolytic cleavage of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. MTA is a major by-product of polyamine biosynthesis, and MTAP is involved in its breakdown. The enzyme carries out the first step of the methionine salvage pathway once MTA has been generated from S-adenosylmethionine. It has broad substrate specificity, with 6-aminopurine nucleosides as the preferred substrates.
The MTAP protein belongs to the PNP/MTAP phosphorylase family, MTAP subfamily, and is found in the cytoplasm and the nucleus. The human MTAP gene is located at 9p21.3 and encodes a protein of 283 amino acids. Multiple alternatively spliced transcript variants have been described for the gene. The mouse ortholog is Mtap.
Through its role in polyamine metabolism and in the salvage of adenine and methionine, MTAP links nucleotide and amino acid metabolism. According to the NCBI Gene summary, the enzyme is deficient in many cancers, which makes the MTAP gene and its product a frequent subject of cancer metabolism research. Researchers studying MTAP typically examine its expression, its enzymatic activity and the consequences of its loss, using tools such as an MTAP antibody or an MTAP ELISA kit.
MTAP breaks down MTA, a major by-product of polyamine biosynthesis, so it is central to studies of polyamine turnover.
MTAP performs the first step of methionine salvage after MTA arises from S-adenosylmethionine, making it a key enzyme in this pathway.
The enzyme is deficient in many cancers, so MTAP status is a recurring focus in tumour metabolism research.
MTAP releases adenine from MTA and prefers 6-aminopurine nucleosides, placing it within adenine salvage and purine substrate studies.
MTAP catalyses the phosphorolytic cleavage of S-methyl-5'-thioadenosine into adenine and 5-methylthioribose-1-phosphate. It breaks down MTA, a by-product of polyamine biosynthesis, and performs the first step of the methionine salvage pathway after MTA is formed from S-adenosylmethionine.
MTAP is the HGNC symbol for methylthioadenosine phosphorylase. UniProt lists the protein as S-methyl-5'-thioadenosine phosphorylase, and MSAP and c86fus are recorded aliases. The enzyme carries the EC number 2.4.2.28, and multiple alternatively spliced transcript variants have been described.
The NCBI Gene summary states that the enzyme is deficient in many cancers. A mouse ortholog, Mtap, exists, so murine models can be used for study. Check the datasheet of any product for its validated reactivity.
Other polyamine metabolism enzymes, methionine salvage pathway components and cancer metabolism markers may be listed here as pages become available.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13126; product specifications from Assay Genie datasheets.