1-pirolin-5-karboksilat dehidrogenaza
| 1-pirolin-5-karboksilat dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.5.1.12 | ||||||||
| CAS broj | 9054-82-4 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
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
- (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
[уреди | уреди извор]- ^ Adams, E. & 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. & 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
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- 1-pyrroline-5-carboxylate+dehydrogenase на US National Library of Medicine Medical Subject Headings (MeSH)
