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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.
Reference ranges (reference intervals) for blood tests are sets of values used by a health professional to interpret a set of medical test results from blood samples. Reference ranges for blood tests are studied within the field of clinical chemistry (also known as "clinical biochemistry", "chemical pathology" or "pure blood chemistry"), the ...
Pages for logged out editors learn more. Contributions; Talk; Betaine-homocysteine methyltransferase
In enzymology, a thetin-homocysteine S-methyltransferase (EC 2.1.1.3) is an enzyme that catalyzes the chemical reaction dimethylsulfonioacetate + L-homocysteine ⇌ {\displaystyle \rightleftharpoons } S-methylthioglycolate + L-methionine
In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). [ 5 ] [ 6 ] Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, [ 7 ] and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle.
Blood pressure is one of the vital signs—together with respiratory rate, heart rate, oxygen saturation, and body temperature—that healthcare professionals use in evaluating a patient's health. Normal resting blood pressure in an adult is approximately 120 millimetres of mercury (16 kPa) systolic over 80 millimetres of mercury (11 kPa ...
S-adenosyl-L-methionine + DNA adenine S-adenosyl-L-homocysteine + DNA 6-methylaminopurine m6A was primarily found in prokaryotes until 2015 when it was also identified in some eukaryotes. m6A methyltransferases methylate the amino group in DNA at C-6 position specifically to prevent the host system to digest own genome through restriction enzymes.
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