Metionin sintaza
| Metionin sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Metionin sintaza homodimer, Human | |||||||||
| 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 | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
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 Neuspjeh pri parsiranju (SVG (MathML se može omogućiti putem plugina u pregledniku): Neispravan odgovor ("Math extension cannot connect to Restbase.") sa servera "http://localhost:6011/sh.wikipedia.org/v1/":): {\displaystyle \rightleftharpoons} tetrahidrofolat + L-metionin
Ovaj enzim sadrži cink i kobamid.
Reference
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Methionine+synthase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
