Peptidoglikan glikoziltransferaza
| Peptidoglikan glikoziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.129 | ||||||||
| CAS broj | 79079-04-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Peptidoglikan glikoziltransferaza (EC 2.4.1.129, PG-II, baktoprenildifosfo-N-acetilmuramoil-(N-acetil-D-glukozaminil)-pentapeptid:peptidoglikan N-acetilmuramoil-N-acetil-D-glukozaminiltransferaza, penicilin vezujući protein (3 ili 1B), peptidoglikanska transglikozilaza, undekaprenildifosfo-(N-acetil-D-glukozaminil-(1->4)-N-acetil-D-muramoilpentapeptid):undekaprenildifosfo-(N-acetil-D-glukozaminil-(1->4)-N-acetil-D-muramoilpentapeptid) disaharidtransferaza) je enzim sa sistematskim imenom (poli-N-acetil-D-glukozaminil-(1->4)-(N-acetil-D-muramoilpentapeptid))-difosfoundekaprenol:(N-acetil-D-glukozaminil-(1->4)-N-acetil-D-muramoilpentapeptid)-difosfoundekaprenol disaharidtransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- [GlcNAc-(1->4)-Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lys-D-Ala-D-Ala)]n-difosfoundekaprenol + GlcNAc-(1->4)-Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lys-D-Ala-D-Ala)-difosfoundekaprenol [GlcNAc-(1->4)-Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-difosfoundekaprenol + undekaprenil difosfat
Ovaj enzim takođe deluje kad je lizinski ostatak zamenjen meso-2,6-diaminoheptandioatom (meso-2,6-diaminopimelat, A2pm).
Reference
- ↑ Taku, A., Stuckey, M. and Fan, D.P. (1982). „Purification of the peptidoglycan transglycosylase of Bacillus megaterium”. J. Biol. Chem. 257: 5018-5022. PMID 6802846.
- ↑ Goffin, C. and Ghuysen, J.-M. (1998). „Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs”. Microbiol. Mol. Biol. Rev. 62: 1079-1093. PMID 9841666.
- ↑ van Heijenoort, J. (2001). „Formation of the glycan chains in the synthesis of bacterial peptidoglycan”. Glycobiology 11: 25-25. PMID 11320055.
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 Peptidoglycan+glycosyltransferase
- 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
