Homocistein S-metiltransferaza
| Homocistein S-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.10 | ||||||||
| CAS broj | 9012-40-2 | ||||||||
| 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 | ||||||||
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Homocistein S-metiltransferaza (EC 2.1.1.10, S-adenozilmetionin homocistein transmetilaza, S-metilmetionin homocistein transmetilaza, adenozilmetionin transmetilaza, metilmetionin:homocistein metiltransferaza, adenozilmetionin:homocistein metiltransferaza, homocisteinska metilaza, homocisteinska metiltransferaza, homocisteinska transmetilaza, L-homocisteinska S-metiltransferaza, S-adenozil-L-metionin:L-homocisteinska metiltransferaza, S-adenozilmetionin-homocisteinska transmetilaza, S-adenozilmetionin:homocistein metiltransferaza) je enzim sa sistematskim imenom S-metil-L-metionin:L-homocistein S-metiltransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- S-metil-L-metionin + L-homocistein 2 L-metionin
Enzim koristi S-adenozil-L-metionin kao metilni donor, mada on pruža umanjenu aktivnost u odnosu na S-metil-L-metionin.
Reference
[уреди | уреди извор]- ^ Balish, E. & Shapiro, S.K. (1967). „Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine (or adenosylmethionine):homocysteine methyltransferase”. Arch. Biochem. Biophys. 119: 62—68. PMID 4861151.
- ^ Shapiro, S.K. (1958). „Adenosylmethionine-homocysteine transmethylase”. Biochim. Biophys. Acta. 29: 405—409. PMID 13572358.
- ^ Shapiro, S.K. & Yphantis, D.A. (1959). „Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases”. Biochim. Biophys. Acta. 36: 241—244. PMID 14445542.
- ^ Mudd, S.H. & Datko, A.H. (1990). „The S-Methylmethionine Cycle in Lemna paucicostata”. Plant Physiol. 93: 623—630. PMID 16667513.
- ^ Ranocha, P., McNeil, S.D., Ziemak, M.J., Li, C., Tarczynski, M.C. and Hanson, A.D. (2001). „The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and activity”. Plant J. 25: 575—584. PMID 11309147.
- ^ Ranocha, P., Bourgis, F., Ziemak, M.J., Rhodes, D., Gage, D.A. and Hanson, A.D. (2000). „Characterization and functional expression of cDNAs encoding methionine-sensitive and -insensitive homocysteine S-methyltransferases from Arabidopsis”. J. Biol. Chem. 275: 15962—15968. PMID 10747987.
- ^ Grue-Sørensen, G., Kelstrup, E., Kjær, A. and Madsen, J.Ø. (1984). „Diastereospecific, enzymically catalysed transmethylation from S-methyl-L-methionine to L-homocysteine, a naturally occurring process”. J. Chem. Soc. Perkin Trans. 1: 1091—1097.
Literatura
[уреди | уреди извор]- 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.
Spoljašnje veze
[уреди | уреди извор]- Homocysteine+S-methyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)
