Izvorni kod stranice Hem oksigenaza (deciklizacija)

{{Infobox Enzim
| Name = Hem oksigenaza (deciklizacija)
| EC_number = 1.14.99.3
| CAS_number = 9059-22-7
| IUBMB_EC_number = 1/14/99/3
| GO_code = 
| image = 1twn.jpg
| width = 270
| caption = Dimer hem oksigenaze I (čovjek)
}}
'''Hem oksigenaza (deciklizacija)''' ({{EC broj|1.14.99.3}}, ''ORP33 proteini'', ''hem oksigenaza'', ''hem oksidaza'', ''hem oksidaza'') je [[enzim]] sa sistematskim imenom ''hem,vodonik-donor:kiseonik oksidoreduktaza (alfa-meten-oksidacija, hidroksilacija)''.<ref>{{cite journal | title = Solubilization and partial purification of heme oxygenase from rat liver |author = Maines, M.D., Ibrahim, N.G. and Kappas, K. |journal = J. Biol. Chem. |date = 1977 |volume = 252 |pages = 5900-5903 |pmid = 18477}}</ref><ref>{{cite journal | title = Gas-chromatographic assay for heme oxygenase activity | url = https://archive.org/details/sim_clinical-chemistry_1982-10_28_10/page/2026 |author = Sunderman, F.W., Jr., Downs, J.R., Reid, M.C. and Bibeau, L.M. |journal = Clin. Chem. |date = 1982 |volume = 28 |pages = 2026-2032 |pmid = 6897023}}</ref><ref>{{cite journal | title = Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes |author = Yoshida, T., Takahashi, S. and Kikuchi, J. |journal = J. Biochem. (Tokyo) |date = 1974 |volume = 75 |pages = 1187-1191 |pmid = 4370250}}</ref><ref>{{cite journal | title = Specific requirement of NADPH-cytochrome ''c'' reductase for the microsomal heme oxygenase reaction yielding biliverdin IX &alpha; |author = Noguchi, M., Yoshida, T. and Kikuchi, G. |journal = FEBS Lett. |date = 1979 |volume = 98 |pages = 281-284 |pmid = 105935}}</ref><ref>{{cite journal | title = Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1 |author = Lad, L., Schuller, D.J., Shimizu, H., Friedman, J., Li, H., Ortiz de Montellano, P.R. and Poulos, T.L. |journal = J. Biol. Chem. |date = 2003 |volume = 278 |pages = 7834-7843 |pmid = 12500973}}</ref> Ovaj enzim [[Kataliza|katalizuje]] sledeću [[hemijska reakcija|hemijsku reakciju]]

: [[hem]] + 3 AH<sub>2</sub> + 3 O<sub>2</sub> <math>\rightleftharpoons</math> [[biliverdin]] + Fe<sup>2+</sup> + CO + 3 A + 3H<sub>2</sub>O

Za rad ovog enzima je neophodan NAD(P)H i [[EC 1.6.2.4]], NADPH-hemoproteinska reduktaza. Terminalni atomi kiseonika koji nisu inkorporirani u karbonilne grupe pirolnih prstena A i B [[biliverdin]]a su izvedeni dva zasebna molekula kiseonika.

== Reference ==
{{reflist}}

== Literatura ==
{{refbegin|2}}
* {{PriceEnzymology3rd}}
* {{TooneAdvancesInEnzymology}}
* {{Branden ProteinStructure2nd}}
* {{SegelEnzymeKinetics}}
* {{CopelandEvaluationOfEnzymeInhibitors2nd}}
* {{MichalBiochemicalPathways}}
{{refend}}

== Vanjske veze ==
* {{MeshName|Heme+oxygenase}}

{{Enzimi}}

[[Kategorija:EC 1.14.99]]