Saharoza—1,6-a-glukan 3(6)-a-glukoziltransferaza
(Preusmjereno sa stranice GTF-I)
Saharoza—1,6-a-glukan 3(6)-a-glukoziltransferaza | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 2.4.1.125 | ||||||||
CAS broj | 81725-87-3 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
|
Saharoza—1,6-a-glukan 3(6)-a-glukoziltransferaza (EC 2.4.1.125, u vodi rastvorna glukanska sintaza, GTF-I, GTF-S, GTF-SI, saharoza-1,6-alfa-glukan 3(6)-alfa-glukoziltransferaza, saharoza:1,6-alfa-D-glukan 3-alfa- and 6-alfa-glukoziltransferaza, saharoza:1,6-, 1,3-alfa-D-glukan 3-alfa- and 6-alfa-D-glukoziltransferaza, saharoza:1,6-alfa-D-glukan 3(6)-alfa-D-glukoziltransferaza, gtfB (gen), gtfC (gen), gtfD (gen)) je enzim sa sistematskim imenom saharoza:(1->6)-alfa-D-glukan 3(6)-alfa-D-glukoziltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) saharoza + [(1->6)-alfa-D-glukozil]n D-fruktoza + [(1->6)-alfa-D-glukozil]n+1
- (2) saharoza + [(1->6)-alfa-D-glukozil]n D-fruktoza + (1->3)-alfa-D-glukozil[(1->6)-alfa-D-glukozil]n
Ovaj enzim je izolovan iz bakterije dentalnog karijesa Streptococcus mutans.
- ↑ Mukasa, H., Shimamura, A. and Tsumori, H. (1982). „Purification and characterization of basic glucosyltransferase from Streptococcus mutans serotype c”. Biochim. Biophys. Acta 719: 81-89. PMID 6216919.
- ↑ Shimamura, A., Tsumori, H. and Mukasa, H. (1982). „Purification and properties of Streptococcus mutans extracellular glucosyltransferase”. Biochim. Biophys. Acta 702: 72-80. PMID 6461359.
- ↑ Tsumori, H., Shimamura, A. and Mukasa, H. (1985). „Purification and properties of extracellular glucosyltransferase synthesizing 1,6-, 1,3-α-D-glucan from Streptococcus mutans serotype a”. J. Gen. Microbiol. 131: 3347-3353. PMID 2937877.
- ↑ Fujiwara, T., Tamesada, M., Bian, Z., Kawabata, S., Kimura, S. and Hamada, S. (1996). „Deletion and reintroduction of glucosyltransferase genes of Streptococcus mutans and role of their gene products in sucrose dependent cellular adherence”. Microb Pathog 20: 225-233. PMID 8737492.
- ↑ Monchois, V., Willemot, R.M. and Monsan, P. (1999). „Glucansucrases: mechanism of action and structure-function relationships”. FEMS Microbiol. Rev. 23: 131-151. PMID 10234842.
- ↑ Ito, K., Ito, S., Shimamura, T., Weyand, S., Kawarasaki, Y., Misaka, T., Abe, K., Kobayashi, T., Cameron, A.D. and Iwata, S. (2011). „Crystal structure of glucansucrase from the dental caries pathogen Streptococcus mutans”. J. Mol. Biol. 408: 177-186. PMID 21354427.
- 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.