Heksaprenildihidroksibenzoat metiltransferaza
| Heksaprenildihidroksibenzoat metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.114 | ||||||||
| CAS broj | 139569-31-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Heksaprenildihidroksibenzoat metiltransferaza (EC 2.1.1.114, 3,4-dihidroksi-5-heksaprenilbenzoatna metiltransferaza, dihidroksiheksaprenilbenzoatna metiltransferaza, COQ3 (gen), Coq3 O-metiltransferaza, DHHB O-metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:3,4-dihidroksi-5-sve-trans-poliprenilbenzoat 3-O-metiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- S-adenozil-L-metionin + 3,4-dihidroksi-5-sve-trans-poliprenilbenzoat S-adenozil-L-homocistein + 3-metoksi-4-hidroksi-5-sve-trans-poliprenilbenzoat
Ovaj enzim učestvuje u biosintezi ubihinona. Ubihinoni iz različitih organizama imaju različiti broj prenilnih jedinica.
Reference
- ↑ Clarke, C.F., Williams, W., Teruya, J.H. (1991). „Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene”. J. Biol. Chem. 266: 16636-16641. PMID 1885593.
- ↑ Poon, W.W., Barkovich, R.J., Hsu, A.Y., Frankel, A., Lee, P.T., Shepherd, J.N., Myles, D.C. and Clarke, C.F. (1999). „Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis”. J. Biol. Chem. 274: 21665-21672. PMID 10419476.
- ↑ Jonassen, T. and Clarke, C.F. (2000). „Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis”. J. Biol. Chem. 275: 12381-12387. PMID 10777520.
- ↑ Xing, L., Zhu, Y., Fang, P., Wang, J., Zeng, F., Li, X., Teng, M. and Li, X. (2011). „Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli”. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67: 727-729. PMID 21636923.
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 Polyprenyldihydroxybenzoate+methyltransferase
- 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
