3-Galaktozil-N-acetilglukozaminid 4-a-L-fukoziltransferaza
3-Galaktozil-N-acetilglukozaminid 4-a-L-fukoziltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.4.1.65 | ||||||||
CAS broj | 37277-69-3 | ||||||||
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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3-Galaktozil-N-acetilglukozaminid 4-a-L-fukoziltransferaza (EC 2.4.1.65, (Lea)-zavisna (alfa-3/4)-fukoziltransferaza, alfa(1,3/1,4) fukoziltransferaza III, alfa-(1->4)-L-fukoziltransferaza, alfa-4-L-fukoziltransferaza, beta-acetilglukozaminilsaharid fukoziltransferaza, FucT-II, Luisova alfa-(1->3/4)-fukoziltransferaza, Luisova krvno grupna alfa-(1->3/4)-fukoziltransferaza, Luis (Le) krvno grupni gen-zavisna alfa-(1->3/4)-L-fukoziltransferaza, krvno grupna Luisova alfa-4-fukoziltransferaza, krvno-grupna supstanca Lea-zavisna fukoziltransferaza, guanozin difosfofukoza-beta-acetilglukozaminilsaharidna 4-alfa-L-fukoziltransferaza, guanozin difosfofukoza-glikoproteinska 4-alfa-L-fukoziltransferaza, guanozin difosfofukoza-glikoproteinska 4-alfa-fukoziltransferaza, 3-alfa-galaktozil-N-acetilglukozaminidna 4-alfa-L-fukoziltransferaza, GDP-beta-L-fukoza:3-beta-D-galaktozil-N-acetil-D-glukozaminil-R 4I-alfa-L-fukoziltransferaza, GDP-L-fukoza:3-beta-D-galaktozil-N-acetil-D-glukozaminil-R 4I-alfa-L-fukoziltransferaza) je enzim sa sistematskim imenom GDP-beta-L-fukoza:beta-D-galaktozil-(1->3)-N-acetil-D-glukozaminil-R 4I-alfa-L-fukoziltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- GDP-beta-L-fukoza + beta-D-galaktozil-(1->3)-N-acetil-D-glukozaminil-R GDP + beta-D-galaktozil-(1->3)-[alfa-L-fukozil-(1->4)]-N-acetil-beta-D-glukozaminil-R
Ovaj enzim je produkt Luisovog krvno grupnog gena.
Reference[uredi | uredi kod]
- ↑ Prieels, J.-P., Monnom, D., Dolmans, M., Beyer, T.A. and Hill, R.L. (1981). „Co-purification of the Lewis blood group N-acetylglucosaminide α1→4 fucosyltransferase and an N-acetylglucosaminide α1→3 fucosyltransferase from human milk”. J. Biol. Chem. 256: 10456-10463. PMID 7287719.
- ↑ Rasko, D.A., Wang, G., Palcic, M.M. and Taylor, D.E. (2000). „Cloning and characterization of the α(1,3/4) fucosyltransferase of Helicobacter pylori”. J. Biol. Chem. 275: 4988-4994. PMID 10671538.
- ↑ Wilson, I.B.H. (2001). „Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase”. Glycoconj. J. 18: 439-447. PMID 12084979.
- ↑ Ma, B., Wang, G., Palcic, M.M., Hazes, B. and Taylor, D.E. (2003). „C-terminal amino acids of Helicobacter pylori α1,3/4 fucosyltransferases determine type I and type II transfer”. J. Biol. Chem. 278: 21893-21900. PMID 12676935.
Literatura[uredi | uredi kod]
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- 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.
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