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
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

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

↑ 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.

Vanjske veze

MeSH Methionine+synthase

[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.

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