Nutrition Guide

In enzymology, a homocysteine S-methyltransferase (EC 2.1.1.10) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + L-homocysteine S-adenosyl-L-homocysteine + L-methionine Thus, the two substrates of this enzyme are S-adenosyl methionine and L-homocysteine, whereas its two products are S-adenosylhomocysteine and L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S-methyltransferase. Other names in common use include S-adenosylmethionine homocysteine transmethylase, S-methylmethionine homocysteine transmethylase, adenosylmethionine transmethylase, methylmethionine:homocysteine methyltransferase, adenosylmethionine:homocysteine methyltransferase, homocysteine methylase, homocysteine methyltransferase, homocysteine transmethylase, L-homocysteine S-methyltransferase, S-adenosyl-L-methionine:L-homocysteine methyltransferase, S-adenosylmethionine-homocysteine transmethylase, and S-adenosylmethionine:homocysteine methyltransferase. This enzyme participates in

In enzymology, a thetin-homocysteine S-methyltransferase (EC 2.1.1.3) is an enzyme that catalyzes the chemical reaction dimethylsulfonioacetate + L-homocysteine S-methylthioglycolate + L-methionine Thus, the two substrates of this enzyme are dimethylsulfonioacetic acid and L-homocysteine, whereas its two products are S-methylthioglycolic acid and L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is dimethylsulfonioacetic acid:L-homocysteine S-methyltransferase. Other names in common use include dimethylthetin-homocysteine methyltransferase, and thetin-homocysteine methylpherase.

In enzymology, a betaine-homocysteine S-methyltransferase (EC 2.1.1.5) is an enzyme that catalyzes the chemical reaction trimethylammonioacetate + L-homocysteine dimethylglycine + L-methionine Thus, the two substrates of this enzyme are trimethylammonioacetate and L-homocysteine, whereas its two products are dimethylglycine and L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is trimethylammonioacetate:L-homocysteine S-methyltransferase. Other names in common use include betaine-homocysteine methyltransferase, and betaine-homocysteine transmethylase. This enzyme participates in the metabolism of glycine, serine, threonine and also methionine.

In enzymology, a 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) is an enzyme that catalyzes the chemical reaction 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine tetrahydropteroyltri-L-glutamate + L-methionine Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamatic acid and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamatic acid and L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase. Other names in common use include tetrahydropteroyltriglutamate methyltransferase, homocysteine methylase, methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase, methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase, cobalamin-independent methionine synthase, methionine synthase (cobalamin-independent), and MetE. This enzyme participates in methionine metabolism. It has 2 cofactors: orthophosphate, and zinc.

S-Adenosyl-L-homocysteine is an amino acid derivative used in several metabolic pathways in the organism Escherichia coli. It is an intermediate in the synthesis of cysteine. S-(5'-deoxy-5'-adenosyl)-l-homocysteine is a compound formed by the demethylation of S-adenosyl-L-methionine (SAM).

In enzymology, a S-ribosylhomocysteine lyase (EC 4.4.1.21) is an enzyme that catalyzes the chemical reaction S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione Hence, this enzyme has one substrate, S-(5-deoxy-D-ribos-5-yl)-L-homocysteine, and two products, L-homocysteine and (4S)-4,5-dihydroxypentan-2,3-dione. This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S-(5-deoxy-D-ribos-5-yl)-L-homocysteine L-homocysteine-lyase [(4S)-4,5-dihydroxypentan-2,3-dione-forming]. Other names in common use include S-ribosylhomocysteinase, and LuxS. This enzyme participates in methionine metabolism.

In enzymology, a homocysteine desulfhydrase (EC 4.4.1.2) is an enzyme that catalyzes the chemical reaction L-homocysteine + H2O hydrogen sulfide + NH3 + 2-oxobutanoate Thus, the two substrates of this enzyme are L-homocysteine and H2O, whereas its 3 products are hydrogen sulfide, NH3, and 2-oxobutanoate. This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-homocysteine hydrogen-sulfide-lyase (deaminating 2-oxobutanoate-forming). Other names in common use include homocysteine desulfurase, L-homocysteine hydrogen-sulfide-lyase, and (deaminating). This enzyme participates in nitrogen metabolism and sulfur metabolism. It employs one cofactor, pyridoxal phosphate.

In enzymology, a S-adenosylhomocysteine deaminase (EC 3.5.4.28) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-homocysteine + H2O S-inosyl-L-homocysteine + NH3 Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-inosyl-L-homocysteine and NH3. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called adenosylhomocysteine deaminase.

5-methyltetrahydrofolate-homocysteine methyltransferase, also known as MTR, is a human gene.[1] MTR encodes the enzyme 5-methyltetrahydrofolate-homocysteine methyltransferase. This enzyme, also known as cobalamin-dependent methionine synthase, catalyzes the final step in methionine biosynthesis. Mutations in MTR have been identified as the underlying cause of methylcobalamin deficiency complementation group G.[1] 5-Methyltetrahydrofolate-homocysteine methyltransferase or (MTR) is an enzyme responsible for the production of methionine from homocysteine. MTR forms part of the S-adenosyl methionine cycle and is also called methionine synthase.[2]

As a consequence of the biochemical reactions in which homocysteine is involved, deficiencies of the vitamins folic acid (B9), pyridoxine (B6), or B12 (cyanocobalamin) can lead to high homocysteine levels.[2] Supplementation with pyridoxine, folic acid, B12 or trimethylglycine (betaine) reduces the concentration of homocysteine in the bloodstream.[3] [4] Increased levels of homocysteine are linked to high concentrations of endothelial asymmetric dimethylarginine. Recent research suggests that intense, long duration exercise raises plasma homocysteine levels, perhaps by increasing the load on methionine metabolism.[5] Elevations of homocysteine also occur in the rare hereditary disease homocystinuria and in the methylene-tetrahydrofolate-reductase polymorphism genetic traits. The latter

In enzymology, an adenosylhomocysteine nucleosidase (EC 3.2.2.9) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-homocysteine + H2O S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-(5-deoxy-D-ribos-5-yl)-L-homocysteine and adenine. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is S-adenosyl-L-homocysteine homocysteinylribohydrolase. Other names in common use include S-adenosylhomocysteine hydrolase (ambiguous), S-adenosylhomocysteine nucleosidase, 5'-methyladenosine nucleosidase, S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase, and AdoHcy/MTA nucleosidase. This enzyme participates in methionine metabolism.

Although mammals cannot synthesize methionine, they can still utilize it in a variety of biochemical pathways: Methionine is converted to S-adenosylmethionine (SAM) by (1) methionine adenosyltransferase. SAM serves as a methyl-donor in many (2) methyltransferase reactions and is converted to S-adenosylhomocysteine (SAH). (3) adenosylhomocysteinase converts SAH to homocysteine. There are two fates of homocysteine: Methionine can be regenerated from homocysteine via (4) methionine synthase. It can also be remethylated using glycine betaine (NNN-trimethyl glycine) to methionine via the enzyme Betaine-homocysteine methyltransferase (E.C.2.1.1.5, BHMT). BHMT makes up to 1.5% of all the soluble protein of the liver, and recent evidence suggests that it may

In enzymology, a cystathionine beta-lyase (EC 4.4.1.8) is an enzyme that catalyzes the chemical reaction L-cystathionine + H2O L-homocysteine + NH3 + pyruvate Thus, the two substrates of this enzyme are L-cystathionine and H2O, whereas its 3 products are L-homocysteine, NH3, and pyruvate. This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming). Other names in common use include beta-cystathionase, cystine lyase, cystathionine L-homocysteine-lyase (deaminating), and L-cystathionine L-homocysteine-lyase (deaminating). This enzyme participates in 5 metabolic pathways: methionine metabolism, cysteine metabolism, selenoamino acid metabolism, nitrogen metabolism, and

The "extra" (relative to cysteine) one carbon methylene group allows this molecule to form a five-membered ring, homocysteine thiolactone. The facility of this reaction precludes the formation of stable peptide bonds. In other words, a protein containing homocysteine would tend to cleave itself. The 4 carbon homocysteine is (only) made from the 5 carbon methionine, an essential amino acid, in a multi step reaction via S-adenosyl methionine. Homocysteine can be recycled back into methionine or it can be permanently converted to cysteine via the transsulfuration pathway. Homocysteine is not obtained from the diet; it is a normal temporary and chemically reactive

Elevated levels of homocysteine have been linked to increased fractures in elderly persons. Elevated levels may be due to renal or liver disease, deficiency of folic acid, vitamin B6 or vitamin B12. The high level of homocysteine will auto-oxidize and react with reactive oxygen intermediates and damage endothelial cells and has a higher risk to form a thrombus. [12][13] Homocysteine does not affect bone density. Instead, it appears that homocysteine affects collagen by interfering with the cross-linking between the collagen fibers and the tissues they reinforce. While the HOPE-2 trial [6] showed a reduction in stroke incidence, in those with

Leave a Reply

Name (required)

Mail (will not be published) (required)

Website