Iduronatna 2-sulfataza
| Iduronatna 2-sulfataza | |||||||||
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| Iduronatna 2-sulfataza dimer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.1.6.13 | ||||||||
| CAS broj | 50936-59-9 | ||||||||
| 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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Iduronatna 2-sulfataza (EC 3.1.6.13, hondroitinsulfataza, idurono-2-sulfataza, iduronid-2-sulfat sulfataza, L-iduronosulfataza, L-idurono sulfatna sulfataza, iduronatna sulfataza, sulfo-L-iduronatna sulfataza, L-iduronat 2-sulfatna sulfataza, sulfoiduronatna sulfohidrolaza, 2-sulfo-L-iduronat 2-sulfataza, iduronat-2-sulfat sulfataza, iduronat sulfatna sulfataza) je enzim sa sistematskim imenom L-iduronat-2-sulfat 2-sulfohidrolaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- hidroliza 2-sulfatnih grupa L-iduronat 2-sulfatnih jedinica dermatan sulfata, heparan sulfata i heparina
Reference
- ↑ Archer, I.M., Harper, P.S. and Wusteman, F.S. (1982). „Multiple forms of iduronate 2-sulphate sulphatase in human tissues and body fluids”. Biochim. Biophys. Acta 708: 134-140. PMID 6816283.
- ↑ Bach, J., Eisenberg, F., Cantz, M. and Neufeld, E.C. (1973). „The defect in the Hunter syndrome: deficiency of sulfoiduronate sulfatase”. Proc. Natl. Acad. Sci. USA 70: 2134-2138. PMID 4269173.
- ↑ DiNatale, P. and Ronsivalle, L. (1981). „Identification and partial characterization of two enzyme forms of iduronate sulfatase from human placenta”. Biochim. Biophys. Acta 661: 106-111. PMID 6945876.
- ↑ Yutaka, T., Fluharty, A.L., Stevens, R.L. and Kihara, H. (1982). „Purification and some properties of human liver iduronate sulfatase”. J. Biochem. (Tokyo) 91: 433-441. PMID 6950934.
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.
Spoljašnje veze
- MeSH Iduronate-2-sulfatase
- p
- r
- u
Holinesteraza (Acetilholinesteraza, Butirilholinesteraza) • Pektinesteraza • 6-fosfoglukonolaktonaza • PAF acetilhidrolaza
Lipaza (Zavisna od žučnih soli, Gastrična/Lingvalna, Pankreasna, Lizozomalna, Hormon-sensitivna, Endotelna, Hepatička, Lipoproteinska, Monoacilglicerolna, Diacilglicerolna)
Fosfolipaza (A1, A2, B)Tioesteraza palmitoil proteina • Ubikvitin karboksilni-terminal hidrolaza L1
Alkalna fosfataza (ALPI, ALPL, ALPP) • Kiselinska fosfataza (Prostatična)/Tartrat-otporna kiselinska fosfataza/Fosfataze purpurne kiseline • Nukleotidaza • Glukoza 6-fosfataza • Fruktoza 1,6-bisfosfataza •
Kalcineurin • Fosfoproteinska fosfataza (PP2A) • OCRL • Piruvat dehidrogenazna fosfataza • Fruktoza 6-P,2-kinaza:fruktoza 2,6-bisfosfataza •PTEN • Fitaza • Inozitol-fosfat fosfataza (IMPA1)
Autotaksin • Fosfolipaza (C, D) • Sfingomijelin fosfodiesteraza (1) • PDE1 • PDE2 • PDE3 • PDE4A/PDE4B • PDE5 • Lecitinaza (Clostridium perfringens alfa toksin) • Fosfodiesteraza cikličnih nukleotida
arilsulfataza (Arilsulfataza A, Arilsulfataza B, Arilsulfataza E, Steroidna sulfataza) • Galaktozamine-6 sulfataza • Iduronat-2-sulfataza • N-acetilglukosamin-6-sulfataza
deoksiribonukleazu i
ribonukleazu)
3.1.11-16: Eksonukleaza |
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3.1.21-31: Endonukleaza |
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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
