1-pirolin-5-karboksilat dehidrogenaza
1-pirolin-5-karboksilat dehidrogenaza (EC 1.5.1.12, Delta1-pirolidin-5-karboksilat dehidrogenaza, 1-pirolidinska dehidrogenaza, pirolidin-5-karboksilatna dehidrogenaza, pirolidin-5-karboksilna kiselina dehidrogenaza, L-pirolidin-5-karboksilat-NAD+ oksidoreduktaza, 1-pirolidin-5-karboksilat:NAD+ oksidoreduktaza, Delta1-pirolidin-5-karboksilna kiselina dehidrogenaza) je enzim sa sistematskim imenom (S)-1-pirolidin-5-karboksilat:NAD+ oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 1-pirolin-5-karboksilat dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.5.1.12 | ||||||||
| CAS broj | 9054-82-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (S)-1-pirolidin-5-karboksilat + NAD(P)+ + 2H2O L-glutamat + NAD(P)H + H+
Ovaj enzim može da oksiduje brojne 1-pirolidine, e.g. 3-hidroksi-1-pirolidin-5-karboksilat se konvertuje u 4-hidroksiglutamat i (R)-1-pirolidin-5-karboksilat se konvertuje u D-glutamat.
Reference uredi
- ↑ Adams, E. and Goldstone, A. (1960). „Hydroxyproline metabolism. IV. Enzymatic synthesis of γ-hydroxyglutamate from Δ1-pyrroline-3-hydroxy-5-carboxylate”. J. Biol. Chem. 235: 3504-3512. PMID 13681370.
- ↑ Strecker, H.J. (1960). „The interconversion of glutamic acid and proline. III. Δ1-Pyrroline-5-carboxylic acid dehydrogenase”. J. Biol. Chem. 235: 3218-3223.
- ↑ Forlani, G., Scainelli, D. and Nielsen, E. (1997). „Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato (purification and properties)”. Plant Physiol. 113: 1413-1418. PMID 12223682.
- ↑ Brown, E.D. and Wood, J.M. (1992). „Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli”. J. Biol. Chem. 267: 13086-13092. PMID 1618807.
- ↑ Inagaki, E., Ohshima, N., Sakamoto, K., Babayeva, N.D., Kato, H., Yokoyama, S. and Tahirov, T.H. (2007). „New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+”. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63: 462-465. PMID 17554163.
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.