Cholest-4-en-3-one 26-monooxygenase

Cholest-4-en-3-one 26-monooxygenase
Identifiers
EC number 1.14.13.141
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Cholest-4-en-3-one 26-monooxygenase (EC 1.14.13.141, CYP125, CYP125A1, cholest-4-en-3-one 27-monooxygenase) is an enzyme with systematic name cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxylating).[1][2][3][4] This enzyme catalyses the following chemical reaction

cholest-4-en-3-one + NADH + H+ + O2 \rightleftharpoons 26-hydroxycholest-4-en-3-one + NAD+ + H2O

Cholest-4-en-3-one 26-monooxygenase is a heme thiolate (P450) enzyme.

References

  1. Rosloniec, K.Z., Wilbrink, M.H., Capyk, J.K., Mohn, W.W., Ostendorf, M., van der Geize, R., Dijkhuizen, L. and Eltis, L.D. (2009). "Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHA1". Mol. Microbiol. 74 (5): 1031–1043. doi:10.1111/j.1365-2958.2009.06915.x. PMID 19843222.
  2. McLean, K.J., Lafite, P., Levy, C., Cheesman, M.R., Mast, N., Pikuleva, I.A., Leys, D. and Munro, A.W. (2009). "The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection". J. Biol. Chem. 284 (51): 35524–35533. doi:10.1074/jbc.M109.032706. PMC 2790982. PMID 19846552.
  3. Capyk, J.K., Kalscheuer, R., Stewart, G.R., Liu, J., Kwon, H., Zhao, R., Okamoto, S., Jacobs, W.R., Jr., Eltis, L.D. and Mohn, W.W. (2009). "Mycobacterial cytochrome P450 125 (cyp125) catalyzes the terminal hydroxylation of C27 steroids". J. Biol. Chem. 284 (51): 35534–35542. doi:10.1074/jbc.M109.072132. PMC 2790983. PMID 19846551.
  4. Ouellet, H., Guan, S., Johnston, J.B., Chow, E.D., Kells, P.M., Burlingame, A.L., Cox, J.S., Podust, L.M. and de Montellano, P.R. (2010). "Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one". Mol. Microbiol. 77 (3): 730–742. doi:10.1111/j.1365-2958.2010.07243.x. PMC 2909382. PMID 20545858.

External links

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