Homocistein S-metiltransferaza
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
| Homocistein S-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.10 | ||||||||
| CAS broj | 9012-40-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- 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 uredi
- ↑ Balish, E. and 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. and Yphantis, D.A. (1959). „Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases”. Biochim. Biophys. Acta 36: 241-244. PMID 14445542.
- ↑ Mudd, S.H. and 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 uredi
- 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.