Laktozilkeramid a-2,6-N-sijaliltransferaza

Laktozilkeramid a-2,6-N-sijaliltransferaza
Identifikatori
EC broj	2.4.99.11
CAS broj	55071-95-9
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Laktozilkeramid a-2,6-N-sijaliltransferaza (EC 2.4.99.11, citidin monofosfoacetilneuraminat-laktozilkeramid sijaliltransferaza, CMP-acetilneuraminat-laktozilkeramid-sijaliltransferaza, CMP-N-acetilneuraminska kiselina:laktozilkeramid sijaliltransferaza, CMP-sijalinska kiselina:laktozilkeramid sijaliltransferaza, CMP-N-acetilneuraminat:laktozilkeramid alfa-2,6-N-acetilneuraminiltransferaza, CMP-N-acetilneuraminat:beta-D-galaktozil-(1->4)-beta-D-glukozil(1<->1)keramid alfa-(2->6)-N-acetilneuraminiltransferaza) je enzim sa sistematskim imenom CMP-N-acetilneuraminat:beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid alfa-(2->6)-N-acetilneuraminiltransferaza.^[1]^[2] Ovaj enzim katalizuje sledeću hemijsku reakciju

CMP-N-acetilneuraminat + beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid

\rightleftharpoons

CMP + alfa-N-acetilneuraminil-(2->6)-beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid

Reference uredi

↑ Albarracin, I., Lassaga, F.E. and Caputto, R. (1988). „Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-)”. Biochem. J. 254: 559-565. PMID 2460092.
↑ Landa, C.A., Maccioni, H.J.F., Arce, A. and Caputto, R. (1977). „The biosynthesis of brain gangliosides. Separation of membranes with different ratios of ganglioside sialylating activity to gangliosides”. Biochem. J. 168: 325-332. PMID 606237.

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.

Spoljašnje veze uredi

MeSH Lactosylceramide+alpha-2,6-N-sialyltransferase

[1] Albarracin, I., Lassaga, F.E. and Caputto, R. (1988). „Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-)”. Biochem. J. 254: 559-565. PMID 2460092.

[2] Landa, C.A., Maccioni, H.J.F., Arce, A. and Caputto, R. (1977). „The biosynthesis of brain gangliosides. Separation of membranes with different ratios of ganglioside sialylating activity to gangliosides”. Biochem. J. 168: 325-332. PMID 606237.

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