Hem oksigenaza (deciklizacija)

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Hem oksigenaza (deciklizacija)
Hem oksigenaza (deciklizacija)
	Heme oxygenase I, dimer, Human
Identifikatori
EC broj	1.14.99.3
CAS broj	9059-22-7
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
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Hem oksigenaza (deciklizacija) (EC 1.14.99.3, proteini, hem oksigenaza, hem oksidaza, hem oksidaza) je enzim sa sistematskim imenom hem,vodonik-donor:kiseonik oksidoreduktaza (alfa-meten-oksidacija, hidroksilacija).^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

hem + 3 ₂ + 3 O₂

\rightleftharpoons

biliverdin + ₂O

Кратке чињенице Identifikatori, EC broj ...

Затвори

Za rad ovog enzima je neophodan i EC 1.6.2.4, -hemoproteinska reduktaza. Terminalni atomi kiseonika koji nisu inkorporirani u karbonilne grupe pirolnih prstena A i B biliverdina su izvedeni dva zasebna molekula kiseonika.

Reference

[1]
Maines, M.D., Ibrahim, N.G. and Kappas, K. (1977). „Solubilization and partial purification of heme oxygenase from rat liver”. J. Biol. Chem. 252: 5900—5903. PMID 18477.
[2]
Sunderman, F.W., Jr., Downs, J.R., Reid, M.C. and Bibeau, L.M. (1982). „Gas-chromatographic assay for heme oxygenase activity”. Clin. Chem. 28: 2026—2032. PMID 6897023.
[3]
Yoshida, T., Takahashi, S. and Kikuchi, J. (1974). „Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes”. J. Biochem. (Tokyo). 75: 1187—1191. PMID 4370250.
[4]
Noguchi, M., Yoshida, T. and Kikuchi, G. (1979). „Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX α”. FEBS Lett. 98: 281—284. PMID 105935.
[5]
Lad, L., Schuller, D.J., Shimizu, H., Friedman, J., Li, H., Ortiz de Montellano, P.R. and Poulos, T.L. (2003). „Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1”. J. Biol. Chem. 278: 7834—7843. PMID 12500973.

Literatura

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

Heme+oxygenase на ()

[1] [1]
Maines, M.D., Ibrahim, N.G. and Kappas, K. (1977). „Solubilization and partial purification of heme oxygenase from rat liver”. J. Biol. Chem. 252: 5900—5903. PMID 18477.

[2] [2]
Sunderman, F.W., Jr., Downs, J.R., Reid, M.C. and Bibeau, L.M. (1982). „Gas-chromatographic assay for heme oxygenase activity”. Clin. Chem. 28: 2026—2032. PMID 6897023.

[3] [3]
Yoshida, T., Takahashi, S. and Kikuchi, J. (1974). „Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes”. J. Biochem. (Tokyo). 75: 1187—1191. PMID 4370250.

[4] [4]
Noguchi, M., Yoshida, T. and Kikuchi, G. (1979). „Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX α”. FEBS Lett. 98: 281—284. PMID 105935.

[5] [5]
Lad, L., Schuller, D.J., Shimizu, H., Friedman, J., Li, H., Ortiz de Montellano, P.R. and Poulos, T.L. (2003). „Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1”. J. Biol. Chem. 278: 7834—7843. PMID 12500973.

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