Search results
Results from the WOW.Com Content Network
In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively: [2]
In enzymology, a homocysteine S-methyltransferase (EC 2.1.1.10) is an enzyme that catalyzes the chemical reaction. S-methylmethionine + L-homocysteine 2 L-methionine. Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine.
Pages for logged out editors learn more. Contributions; Talk; Betaine-homocysteine methyltransferase
Sarcosine/dimethylglycine N-methyltransferase (EC 2.1.1.157, ApDMT, sarcosine-dimethylglycine methyltransferase, SDMT, sarcosine dimethylglycine N-methyltransferase, S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:sarcosine(or N,N-dimethylglycine) N-methyltransferase (N,N-dimethylglycine(or betaine)-forming).
Levomefolic acid (INN, also known as L-5-MTHF, L-methylfolate and L-5-methyltetrahydrofolate and (6S)-5-methyltetrahydrofolate, and (6S)-5-MTHF) is the primary biologically active form of folate used at the cellular level for DNA reproduction, the cysteine cycle and the regulation of homocysteine.
Cocamidopropyl betaine is an example of a betaine. A betaine (/ ˈ b iː t ə. iː n, b ɪ ˈ t eɪ-,-ɪ n /) in chemistry is any neutral chemical compound with a positively charged cationic functional group that bears no hydrogen atom, such as a quaternary ammonium or phosphonium cation (generally: onium ions), and with a negatively charged functional group, such as a carboxylate group that ...
The enzyme from Escherichia coli consists of two alpha8-beta8 (TIM) barrels positioned face to face and thought to have evolved by gene duplication. [1] The active site lies between the tops of the two barrels, the N-terminal barrel binds 5-methyltetrahydropteroyltri-L-glutamic acid and the C-terminal barrel binds homocysteine.
The S-methyl-L-cysteine residue irreversibly inactivates the protein, allowing only one transfer for each protein. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase.