Metionin sintaza

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Metionin sintaza
PBB Protein MTR image.jpg
Identifikatori
EC broj 2.1.1.13
CAS broj 9033-23-2
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures

Metionin sintaza (EC 2.1.1.13, 5-metiltetrahidrofolat-homocisteinska S-metiltransferaza, 5-metiltetrahidrofolat-homocisteinska transmetilaza, N-metiltetrahidrofolat:L-homocisteinska metiltransferaza, N5-metiltetrahidrofolatna metiltransferaza, N5-metiltetrahidrofolat-homocistein kobalaminska metiltransferaza, N5-metiltetrahidrofolni-homocistein vitamin B12 transmetilaza, B12 N5-metiltetrahidrofolat homocisteinska metiltransferaza, metiltetrahidrofolat-homocistein vitamin B12 metiltransferaza, tetrahidrofolatna metiltransferaza, tetrahidropteroilglutamatna metiltransferaza, tetrahidropteroilglutaminska metiltransferaza, vitamin B12 metiltransferaza, kobalamin-zavisna metioninska sintaza, metioninska sintaza (kobalamin-zavisna), METH) je enzim sa sistematskim imenom 5-metiltetrahidrofolat:L-homocistein S-metiltransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-metiltetrahidrofolat + L-homocistein \rightleftharpoons tetrahidrofolat + L-metionin

Ovaj enzim sadrži cink i kobamid.

Reference[уреди]

  1. ^ Burton, E.G. and Sakami, W. (1969). „The formation of methionine from the monoglutamate form of methyltetrahydrofolate by higher plants“. Biochem. Biophys. Res. Commun. 36: 228-234. PMID 5799642. 
  2. ^ Foster, M.A., Dilworth, M.J. and Woods, D.D. (1964). „Cobalamin and the synthesis of methionine by Escherichia coli“. Nature 201: 39-42. PMID 14085561. 
  3. ^ Guest, J.R., Friedman, S., Foster, M.A., Tejerina, G. and Woods, D.D. (1964). „Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli“. Biochem. J. 92: 497-504. PMID 5319972. 
  4. ^ Loughlin, R.E., Elford, H.L. and Buchanan, J.M. (1964). „Enzymatic synthesis of the methyl group of methionine. VII. Isolation of a cobalamin-containing transmethylase (5-methyltetrahydro-folate-homocysteine) from mammalian liver“. J. Biol. Chem. 239: 2888-2895. PMID 14216440. 
  5. ^ Taylor, R.T. (1971). „Escherichia coli B N 5 -methyltetrahydrofolate-homocysteine cobalamin methyltransferase: gel-filtration behavior of apoenzyme and holoenzymes“. Biochim. Biophys. Acta 242: 355-364. PMID 4946148. 
  6. ^ Jarrett, J.T., Huang, S. and Matthews, R.G. (1998). „Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, adenosylmethionine, and flavodoxin“. Biochemistry 37: 5372-5382. PMID 9548919. 
  7. ^ Peariso, K., Goulding, C.W., Huang, S., Matthews, R.G. and Penner-Hahn, J.E. (1998). „Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine“. J. Am. Chem. Soc. 120: 8410-8416. 
  8. ^ Hall, D.A., Jordan-Starck, T.C., Loo, R.O., Ludwig, M.L. and Matthews, R.G. (2000). „Interaction of flavodoxin with cobalamin-dependent methionine synthase“. Biochemistry 39: 10711-10719. PMID 10978155. 
  9. ^ Bandarian, V., Pattridge, K.A., Lennon, B.W., Huddler, D.P., Matthews, R.G. and Ludwig, M.L. (2002). „Domain alternation switches B12-dependent methionine synthase to the activation conformation“. Nat. Struct. Biol. 9: 53-56. PMID 11731805. 

Literatura[уреди]

Spoljašnje vezе[уреди]