Metionin sintaza

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Metionin sintaza
Metionin sintaza
Identifikatori
EC broj	2.1.1.13
CAS broj	9033-23-2
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

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. & 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 изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

Methionine+synthase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Burton, E.G. & 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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