Dolihil-fosfat b-D-manoziltransferaza
Dolihil-fosfat b-D-manoziltransferaza (EC 2.4.1.83, GDP-Man:DolP manoziltransferaza, dolihil manozil fosfat sintaza, dolihil-fosfo-manoza sintaza, GDP-manoza:dolihil-fosfat manoziltransferaza, guanozin difosfomanoza-dolihol fosfat manoziltransferaza, dolihol fosfat manozna sintaza, dolihil fosfatna manoziltransferaza, dolihil-fosfat manozna sintaza, GDP-manoza-dolihol fosfatna manoziltransferaza, GDP-manoza-dolihilmonofosfatna manoziltransferaza, manozilfosfodoliholna sintaza, manozilfosforildolihol sintaza) je enzim sa sistematskim imenom GDP-manoza:dolihil-fosfat beta-D-manoziltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Dolihil-fosfat b-D-manoziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.83 | ||||||||
| CAS broj | 62213-44-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- GDP-manoza + dolihil fosfat GDP + dolihil D-manozil fosfat
Ovaj enzim deluje samo na dugolančane poliprenil fosfate i alfa-dihidropoliprenil fosfate koji su suži od C35.
Reference uredi
- ↑ Babczinski, P., Haselbeck, A. and Tanner, W. (1980). „Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme”. Eur. J. Biochem. 105: 509-515. PMID 6989607.
- ↑ Bretthauer, R.K., Wu, S. and Irwin, W.E. (1973). „Enzymatic transfer of mannose from guanosine diphosphate mannose to dolichol phosphate in yeast (Hansenula holstii). A possible step in mannan synthesis”. Biochim. Biophys. Acta 304: 736-747. PMID 4726855.
- ↑ Haselbeck, A. (1989). „Purification of GDP mannose:dolichyl-phosphate O-β-D-mannosyltransferase from Saccharomyces cerevisiae”. Eur. J. Biochem. 181: 663-668. PMID 2659345.
- ↑ Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. (1980). „Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives”. Eur. J. Biochem. 105: 517-523. PMID 6445267.
- ↑ Richards, J.B. and Hemming, F.W. (1972). „The transfer of mannose from guanosine diphosphate mannose to dolichol phosphate and protein by pig liver endoplasmic reticulum”. Biochem. J. 130: 77-93. PMID 4655455.
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.