N-acetillaktozamin sintaza

N-acetillaktozamin sintaza
Identifikatori
EC broj 2.4.1.90
CAS broj 9054-94-8
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

N-acetillaktozamin sintaza (EC 2.4.1.90, UDP-galaktoza N-acetilglukozamin beta-D-galaktoziltransferaza, uridin difosfogalaktoza-acetilglukozamin galaktoziltransferaza, beta-1,4-galaktoziltransferaza, acetillaktozamin sintetaza, laktozamin sintaza, laktozamin sintetaza, laktoza sintetaza A protein, N-acetillaktozamin sintetaza, UDP-galaktoza N-acetilglukozamin beta-4-galaktoziltransferaza, UDP-galaktoza-acetilglukozamin galaktoziltransferaza, UDP-galaktoza-N-acetilglukozamin beta-1,4-galaktoziltransferaza, UDP-galaktoza-N-acetilglukozamin galaktoziltransferaza, beta1-4-galaktoziltransferaza, UDP-Gal:N-acetilglukozamin beta1-4-galaktoziltransferaza, beta1-4GalT, NAL sintetaza, UDP-beta-1,4-galaktoziltransferaza, Gal-T, UDP-galaktoza:N-acetilglukozaminide beta1-4-galaktoziltransferaza, UDPgalaktoza:N-acetilglukozaminil(beta1-4)galaktoziltransferaza, beta-N-acetilglukozaminide beta1-4-galaktoziltransferaza, UDP-galaktoza:N-acetil-D-glukozamin 4-beta-D-galaktoziltransferaza) je galaktozil-transferazni enzim sa sistematskim imenom UDP-alfa-D-galaktoza:N-acetil-D-glukozamin 4-beta-D-galaktoziltransferaza.[1][2][3][4][5][6] On je komponenta laktozne sintaze.[7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju

UDP-alfa-D-galaktoza + N-acetil-D-glukozamin ⇌ {\displaystyle \rightleftharpoons } UDP + N-acetillaktozamin

Ovu reakciju katalizuje komponenta enzima EC 2.4.1.22 (laktozna sintaze), koja je identična sa EC 2.4.1.38 (beta-N-acetilglukozaminil-glikopeptid beta-1,4-galaktoziltransferazom), i enzim iz Goldžijevog aparata životinjskih tkiva.

Povezano

  • N-Acetilglukozamin

Reference

  1. ↑ Deshmukh, D.S., Bear, W.D. and Soifer, D. (1978). „Isolation and characterization of an enriched Golgi fraction from rat brain”. Biochim. Biophys. Acta 542: 284-295. PMID 99178. 
  2. ↑ Helting, T. and Erbing, B. (1973). „Galactosyl transfer in mouse mastocytoma: purification and properties of N-acetyllactosamine synthetase”. Biochim. Biophys. Acta 293: 94-104. PMID 4631039. 
  3. ↑ Hill, R.L. and Brew, K. (1975). „Lactose synthetase”. Adv. Enzymol. Relat. Areas Mol. Biol. 43: 411-490. PMID 812340. 
  4. ↑ Humphreys-Beher, M.G. (1984). „Isolation and characterization of UDP-galactose:N-acetylglucosamine 4 β-galactosyltransferase activity induced in rat parotid glands treated with isoproterenol”. J. Biol. Chem. 259: 5797-5802. PMID 6201486. 
  5. ↑ Schachter, H., Jabbal, I., Hudgin, R.L., Pinteric, L., McGuire, E.J. and Roseman, S. (1970). „Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction”. J. Biol. Chem. 245: 1090-1100. PMID 4392041. 
  6. ↑ Naoyuki Taniguchi, Koichi Honke, Minoru Fukuda (2002). Handbook of glycosyltransferases and related genes (1st ed izd.). Springer. 
  7. ↑ Webb, Edwin C. (1992). Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes. San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press. ISBN 0-12-227164-5. 
  8. ↑ Funderburgh, James L. (2000). „Mini reveiw, Keratan sulfate: structure, biosynthesis, and function”. Glycobiology 10: 951-958. DOI:10.1093/glycob/10.10.951. 

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. 
  • Webb, Edwin C. (1992). Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes. San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press. ISBN 0-12-227164-5. 
  • Naoyuki Taniguchi, Koichi Honke, Minoru Fukuda (2002). Handbook of glycosyltransferases and related genes (1st ed izd.). Springer. 

Spoljašnje veze

  • MeSH N-acetyllactosamine+synthase
  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6