AMT Human
Greater than 95.0% as determined by SDS-PAGE.
Description
AMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Aminomethyltransferase is a part of the glycine decarboxylase complex, which also includes three other enzymes: P-protein, T-protein, and L-protein. The primary function of AMT is to catalyze the transfer of a methylamine group from glycine to tetrahydrofolate, forming methylenetetrahydrofolate . This reaction is vital for cellular one-carbon metabolism, which is involved in the synthesis of nucleotides and amino acids.
The human recombinant form of AMT is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 398 amino acids. It has a molecular mass of approximately 43.3 kDa and is fused to a 23 amino acid His-tag at the N-terminus for purification purposes .
The AMT gene spans approximately 6 kilobases and consists of nine exons. The 5′-flanking region of the gene lacks a typical TATA box but has a single defined transcription initiation site. Additionally, the gene contains putative glucocorticoid-responsive elements and a thyroid hormone-responsive element .
The protein encoded by the AMT gene has a crystal structure resolved at 2 Angstroms, revealing a high degree of homology with its counterparts in other species, such as bovine and chicken .
Aminomethyltransferase is predominantly expressed in the liver, kidney, and pancreas, where it plays a critical role in glycine metabolism. The enzyme’s activity is essential for maintaining the balance of glycine and other amino acids in the body. Deficiencies in AMT can lead to nonketotic hyperglycinemia, a rare genetic disorder characterized by an accumulation of glycine in the body, leading to severe neurological symptoms .
Aminomethyltransferases belong to a broader family of methyltransferases that are conserved across various species, from bacteria to humans. These enzymes share conserved motifs in their amino acid sequences, which are crucial for their catalytic activity. The evolutionary conservation of these motifs highlights the fundamental role of methyltransferases in cellular metabolism .
In summary, aminomethyltransferase (human recombinant) is a vital enzyme involved in glycine metabolism, with significant implications for cellular one-carbon metabolism and overall amino acid balance. Its recombinant form, produced in Escherichia coli, provides a valuable tool for studying its structure and function in various biological processes.
