Metilamin dehidrogenaza (amicijanin)
Metilamin dehidrogenaza (amicijanin) (EC 1.4.9.1, aminska dehidrogenaza, primarna aminska dehidrogenaza, amin: (akceptor) oksidoreduktaza (deaminacija), primarni-amin:(akceptor) oksidoreduktaza (deaminacija)) je enzim sa sistematskim imenom metilamin:amicijanin oksidoreduktaza (deaminacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju:
| Metilamin dehidrogenaza (amicijanin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.4.9.1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- metilamin + H2O + amicijanin formaldehid + amonijak + redukovani amicijanin
Ovaj enzim sadrži triptofan triptofilhinon (TTQ) kofaktor. On oksiduje alifatične monoamine i diamine, histamin i etanolamin, a ne deluje na sekundarne i tercijarne amine, kvaternarne amonijum soli, i aromatične amine.
Reference uredi
- ↑ De Beer, R., Duine, J.A., Frank, J., Jr. and Large, P.J. (1980). „The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1: evidence for a quinone structure”. Biochim. Biophys. Acta 622: 370-374. PMID 6246962.
- ↑ Eady, R.R. and Large, P.J. (1968). „Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine”. Biochem. J. 106: 245-255. PMID 4388687.
- ↑ Eady, R.R. and Large, P.J. (1971). „Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1”. Biochem. J. 123: 757-771. PMID 5124384.
- ↑ Cavalieri, C., Biermann, N., Vlasie, M.D., Einsle, O., Merli, A., Ferrari, D., Rossi, G.L. and Ubbink, M. (2008). „Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus”. Biochemistry 47: 6560-6570. PMID 18512962.
- ↑ Meschi, F., Wiertz, F., Klauss, L., Cavalieri, C., Blok, A., Ludwig, B., Heering, H.A., Merli, A., Rossi, G.L. and Ubbink, M. (2010). „Amicyanin transfers electrons from methylamine dehydrogenase to cytochrome c-551i via a ping-pong mechanism, not a ternary complex”. J. Am. Chem. Soc. 132: 14537-14545. PMID 20873742.
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.