1,8-Cineol 2-endo-monooksigenaza

Izvor: Wikipedia
1,8-Cineol 2-endo-monooksigenaza
Identifikatori
EC broj 1.14.13.156
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures

1,8-Cineol 2-endo-monooksigenaza (EC 1.14.13.156, P450cin, CYP176A, CYP176A1) je enzim sa sistematskim imenom 1,8-cineol,NADPH:kiseonik oksidoreduktaza (2-endo-hidroksilacija).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

1,8-cineol + NADPH + H+ + O2 \rightleftharpoons 2-endo-hidroksi-1,8-cineol + NADP+ + H2O

Ovaj enzim je hem-tiolatni protein (P-450) koji koristi flavodoksinu sličnog redoks partnera da redukuje gvožđehema.

Reference[uredi - уреди]

  1. Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. (2002). "Cytochrome P450cin (CYP176A), isolation, expression, and characterization". J. Biol. Chem. 277: 27725–27732. PMID 12016226. 
  2. Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. (2004). "Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam". Biochemistry 43: 9487–9494. PMID 15260491. 
  3. Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. (2007). "Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin". J. Biol. Chem. 282: 27006–27011. PMID 17606612. 
  4. Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. (2008). "The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin". J. Biol. Chem. 283: 10804–10812. PMID 18270198. 

Literatura[uredi - уреди]

Spoljašnje veze[uredi - уреди]