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Galaktozilksilozilprotein 3-b-galaktoziltransferaza
Identifikatori
EC broj	2.4.1.134
CAS broj	56626-19-8&title= 56626-21-2, 56626-19-8
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

Galaktozilksilozilprotein 3-b-galaktoziltransferaza (EC 2.4.1.134, galaktoziltransferaza II, uridin difosfogalaktoza-galaktozilksilozna galaktoziltransferaza, UDP-galaktoza:4-beta-D-galaktozil-O-beta-D-ksilozilprotein 3-beta-D-galaktoziltransferaza) je enzim sa sistematskim imenom UDP-alfa-D-galaktoza:4-beta-D-galaktozil-O-beta-D-ksilosilprotein 3-beta-D-galaktoziltransferaza.^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

UDP-alfa-D-galaktoza + 4-beta-D-galaktozil-O-beta-D-ksilozil-[protein]

\rightleftharpoons

UDP + 3-beta-D-galaktozil-4-beta-D-galaktozil-O-beta-D-ksilozil-[protein]

Ovaj enzim učestvuje u biosintezi veznog regiona glikozaminoglikanskih lanaca tokom proteoglikanske biosinteze (hondroitin, dermatan i heparan sulfati). Za njegov rad je neophodan Mn²⁺.

Reference

↑ Robinson, J.A. and Robinson, H.C. (1985). „Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II”. Biochem. J. 227: 805-814. PMID 3924029.
↑ Schwartz, N.B. and Roden, L. (1975). „Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase”. J. Biol. Chem. 250: 5200-5207. PMID 1150655.
↑ Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. (2001). „Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6)”. J. Biol. Chem. 276: 48189-48195. PMID 11551958.

Literatura

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.

Vanjske veze

MeSH Galactosylxylosylprotein+3-beta-galactosyltransferase

[1] Robinson, J.A. and Robinson, H.C. (1985). „Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II”. Biochem. J. 227: 805-814. PMID 3924029.

[2] Schwartz, N.B. and Roden, L. (1975). „Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase”. J. Biol. Chem. 250: 5200-5207. PMID 1150655.

[3] Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. (2001). „Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6)”. J. Biol. Chem. 276: 48189-48195. PMID 11551958.

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