BHMT Human

BHMT is part of the enzyme family [Pfam02574], which utilizes catalytic zinc to activate thiol or selenol substrates to thiolate or selenate anions prior to methyl transfer . The enzyme’s primary function is to maintain homocysteine levels in the body by converting it into methionine, an essential amino acid. Elevated homocysteine levels are associated with cardiovascular diseases, making BHMT a critical enzyme for cardiovascular health .

Recombinant BHMT refers to the enzyme produced through recombinant DNA technology, which allows for the production of human proteins in non-human cells. This technology is widely used in research and therapeutic applications to study the enzyme’s function and to develop treatments for diseases related to homocysteine metabolism .

BHMT and its closely related enzyme, BHMT-2, have evolved to perform specific functions in the methionine cycle. BHMT-2, although highly homologous to BHMT, cannot use betaine as a methyl donor and instead uses S-methylmethionine (SMM) for the methylation of homocysteine . This specialization highlights the evolutionary adaptation of these enzymes to different substrates and functions within the methionine cycle.

The clinical significance of BHMT lies in its role in regulating homocysteine levels. Abnormalities in BHMT function can lead to hyperhomocysteinemia, which is linked to various health issues, including cardiovascular diseases, neural tube defects, and cognitive impairments. Understanding the function and regulation of BHMT is crucial for developing therapeutic strategies to manage these conditions .

Research on recombinant BHMT has provided insights into its structure, function, and regulation. Studies have demonstrated the enzyme’s role in homocysteine metabolism and its potential as a therapeutic target. Recombinant BHMT is also used in biochemical assays to study the effects of various compounds on homocysteine levels and to develop drugs that can modulate its activity .