Fosfo-N-acetilmuramoil-pentapeptid-transferaza
Fosfo-N-acetilmuramoil-pentapeptid-transferaza (EC 2.7.8.13, MraY transferaza, UDP-MurNAc-L-Ala-D-gama-Glu-L-Lys-D-Ala-D-Ala:C55-izoprenoid alkoholna transferaza, UDP-MurNAc-Ala-gamaDGlu-Lys-DAla-DAla:undekaprenilfosfat transferaza, fosfo-N-acetilmuramoil pentapeptidna translokaza, fosfo-MurNAc-pentapeptidna transferaza, fosfo-NAc-muramoil-pentapeptidna translokaza (UMP), fosfoacetilmuramoilpentapeptidna translokaza, fosfoacetilmuramoilpentapeptidtransferaza) je enzim sa sistematskim imenom UDP-MurAc(oil-L-Ala-gama-D-Glu-L-Lis-D-Ala-D-Ala):undekaprenil-fosfat fosfo-N-acetilmuramoil-pentapeptid-transferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Fosfo-N-acetilmuramoil-pentapeptid-transferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.8.13 | ||||||||
| CAS broj | 9068-50-2 | ||||||||
| 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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- UDP-Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lys-D-Ala-D-Ala) + undekaprenil fosfat UMP + Mur2Ac(oil-L-Ala-gama-D-Glu-L-Lys-D-Ala-D-Ala)-difosfoundekaprenol
Kod Gram-negativnih i pojedinih Gram-pozitivnih organizama L-lizin je zamenjen meso-2,6-diaminoheptanedioatom.
Reference
uredi- ↑ Heydanek, M.G., Jr. and Neuhaus, F.C. (1969). „The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase”. Biochemistry 8: 1474-1481. PMID 5805290.
- ↑ Higashi, Y., Strominger, J.L. and Sweeley, C.C. (1967). „Structure of a lipid intermediate in cell wall peptidoglycan synthesis: a derivative of a C55 isoprenoid alcohol”. Proc. Natl. Acad. Sci. USA 57: 1878-1884. PMID 5231417.
- ↑ Struve, W.G., Sinha, R.K. and Neuhaus, F.C. (1966). „On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate)”. Biochemistry 5: 82-93. PMID 5938956.
- ↑ van Heijenoort, J. (2001). „Recent advances in the formation of the bacterial peptidoglycan monomer unit”. Nat. Prod. Rep. 18: 503-519. PMID 11699883.
Literatura
uredi- 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.