Beta-galaktofuranozidaza
| Beta-galaktofuranozidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.146 | ||||||||
| CAS broj | 52357-57-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Beta-galaktofuranozidaza (EC 3.2.1.146, ekso-beta-galaktofuranozidaza, ekso-beta-D-galaktofuranozidaza, beta-D-galaktofuranozidaza) je enzim sa sistematskim imenom beta-D-galaktofuranozid hidrolaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- hidroliza terminalnih neredukujućih beta-D-galaktofuranozida, čime se oslobađa galaktoza
Enzim iz Helminthosporium sacchari detoksifikuje helmintosporozid.
Reference
- ↑ Rietschel-Berst, M., Jentoft, N.H., Rick, P.D., Pletcher, C., Fang, F. and Gander, J.E. (1977). „Extracellular exo-β-galactofuranosidase from Penicillium charlesii: isolation, purification, and properties”. J. Biol. Chem. 252: 3219-3226. PMID 863879.
- ↑ Daley, L.S. and Strobel, G.A. (1983). „β-Galactofuranosidase activity in Helminthosporium sacchari and its relationship to the production of helminthosporoside”. Plant Sci. Lett. 30: 145-154.
- ↑ Cousin, M.A., Notermans, S., Hoogerhout, P. and Van Boom, J.H. (1989). „Detection of β-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl β-D-galactofuranoside”. J. Appl. Bacteriol. 66: 311-317. PMID 2502527.
- ↑ Miletti, L.C., Marino, C., Marino, K., de Lederkremer, R.M., Colli, W. and Alves, M.J.M. (1999). „Immobilized 4-aminophenyl-1-thio-β-D-galactofuranoside as a matrix for affinity purification of an exo-β-D-galactofuranosidase”. Carbohydr. Res. 320: 176-182. PMID 10573856.
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 Beta-galactofuranosidase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
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
