Protein geranilgeraniltransferaza tip II
(Preusmjereno sa stranice Rab geranylgeranyltransferase)
Protein geranilgeraniltransferaza tip II (EC 2.5.1.60, GGTaseII, Rab geranilgeraniltransferaza, RabGGTaze, geranilgeranil-difosfat,geranilgeranil-difosfat:protein-cistein geraniltransferaza) je enzim sa sistematskim imenom geranilgeranil-difosfat:protein-cistein geraniltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Protein geranilgeraniltransferaza tip II | |||||||||
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Identifikatori | |||||||||
EC broj | 2.5.1.60 | ||||||||
CAS broj | 135371-29-8 | ||||||||
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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- geranilgeranil difosfat + protein-cistein S-geranilgeranil-protein + difosfat
Ovaj enzim zajedno sa proteinskom farneziltransferazom (EC 2.5.1.58) i proteinskom geranilgeraniltransferazom tip I (EC 2.5.1.59) sačinjava proteinsku preniltransferaznu familiju enzima.
Reference
uredi- ↑ Casey, P.J. and Seabra, M.C. (1996). „Protein prenyltransferases”. J. Biol. Chem. 271: 5289-5292. PMID 8621375.
- ↑ Wilson, A.L., Erdman, R.A., Castellano, F. and Maltese, W.A. (1998). „Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases”. Biochem. J. 333: 497-504. PMID 9677305.
- ↑ Zhang, H., Seabra, M.C. and Deisenhofer, J. (2000). „Crystal structure of Rab geranylgeranyltransferase at 2.0 Å resolution”. Structure 8: 241-251. PMID 10745007.
- ↑ Thomä, N.H., Niculae, A., Goody, R.S. and Alexandrov, K. (2001). „Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate”. J. Biol. Chem. 276: 48631-48636. PMID 11591706.
- ↑ Rak, A., Niculae, A., Kalinin, A., Thomä, N.H., Sidorovitch, V., Goody, R.S. and Alexandrov, K. (2002). „In vitro assembly, purification, and crystallization of the Rab geranylgeranyl transferase:substrate complex”. Protein Expr. Purif. 25: 23-30. PMID 12071695.
- ↑ Gibbs, R.A. (1998). „Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis”. u: Sinnott, M.. Comprehensive Biological Catalysis. A Mechanistic Reference. 1. San Diego, CA: Academic Press. str. 31-118.
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.
- Gibbs, R.A. (1998). „Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis”. u: Sinnott, M.. Comprehensive Biological Catalysis. A Mechanistic Reference. 1. San Diego, CA: Academic Press. str. 31-118.