Glukuronozil-N-acetilgalaktozaminil-proteoglikan 4-b-N-acetilgalaktozaminiltransferaza
Glukuronozil-N-acetilgalaktozaminil-proteoglikan 4-b-N-acetilgalaktozaminiltransferaza (EC 2.4.1.175, N-acetilgalaktozaminiltransferaza II, UDP-N-acetil-D-galaktozamin:D-glukuronil-N-acetil-1,3-beta-D-galaktozaminilproteoglikan beta-1,4-N-acetilgalaktozaminiltransferaza, hondroitinska sintaza, glukuronil-N-acetilgalaktozaminilproteoglikan beta-1,4-N-acetilgalaktozaminiltransferaza, uridin difosfoacetilgalaktozamin-hondroitinska acetilgalaktozaminiltransferaza II) je enzim sa sistematskim imenom UDP-N-acetil-D-galaktozamin:beta-D-glukuronazil-(1->3)-N-acetil-beta-D-galaktozaminil-proteoglikan 4-beta-N-acetilgalaktozaminiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Glukuronozil-N-acetilgalaktozaminil-proteoglikan 4-b-N-acetilgalaktozaminiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.175 | ||||||||
| CAS broj | 96189-40-1 | ||||||||
| 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-N-acetil-D-galaktozamin + beta-D-glukuronazil-(1->3)-N-acetil-beta-D-galaktozaminil-proteoglikan UDP + N-acetil-beta-D-galaktozaminil-(1->4)-beta-D-glukuronazil-(1->3)-N-acetil-beta-D-galaktozaminil-proteoglikan
Ovaj enzim učestvuje u biosintezi hondroitin sulfata.
Reference
uredi- ↑ Rohrmann, K., Niemann, R. and Buddecke, E. (1985). „Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate”. Eur. J. Biochem. 148: 463-469. PMID 3922754.
- ↑ Kitagawa, H., Uyama, T. and Sugahara, K. (2001). „Molecular cloning and expression of a human chondroitin synthase”. J. Biol. Chem. 276: 38721-38726. PMID 11514575.
- ↑ DeAngelis, P.L. and Padgett-McCue, A.J. (2000). „Identification and molecular cloning of a chondroitin synthase from Pasteurella multocida type F”. J. Biol. Chem. 275: 24124-24129. PMID 10818104.
- ↑ Ninomiya, T., Sugiura, N., Tawada, A., Sugimoto, K., Watanabe, H. and Kimata, K. (2002). „Molecular cloning and characterization of chondroitin polymerase from Escherichia coli strain K4”. J. Biol. Chem. 277: 21567-21575. PMID 11943778.
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.