Glukozilkeramid beta-1,4-galaktoziltransferaza
(Preusmjereno sa stranice UDP-Gal:glukozilkeramid beta1-4galaktoziltransferaza)
Glukozilkeramid beta-1,4-galaktoziltransferaza (EC 2.4.1.274, laktozilkeramidna sintaza, uridin difosfat-galaktoza:glukozil keramid beta 1-4 galaktoziltransferaza, UDP-Gal:glukozilkeramid beta1->4galaktoziltransferaza, GalT-2, UDP-galaktoza:beta-D-glukozil-(1<->1)-keramid beta-1,4-galaktoziltransferaza) je enzim sa sistematskim imenom UDP-alfa-D-galaktoza:beta-D-glukozil-(1<->1)-keramid 4-beta-D-galaktoziltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
Glukozilkeramid beta-1,4-galaktoziltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.4.1.274 | ||||||||
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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- UDP-alfa-D-galaktoza + beta-D-glukozil-(1<->1)-keramid UDP + beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid
Ovaj enzim učestvuje u sintezi nekoliko različitih klasa glikosfingolipida.
Reference
uredi- ↑ Chatterjee, S. and Castiglione, E. (1987). „UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes”. Biochim. Biophys. Acta 923: 136-142. PMID 3099851.
- ↑ Trinchera, M., Fiorilli, A. and Ghidoni, R. (1991). „Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase”. Biochemistry 30: 2719-2724. PMID 1900430.
- ↑ Chatterjee, S., Ghosh, N. and Khurana, S. (1992). „Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney”. J. Biol. Chem. 267: 7148-7153. PMID 1551920.
- ↑ Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. (1998). „Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain”. J. Biol. Chem. 273: 13570-13577. PMID 9593693.
- ↑ Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. (1999). „cDNA cloning and expression of human lactosylceramide synthase”. Biochim. Biophys. Acta 1438: 301-304. PMID 10320813.
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.