PROFILPELAJAR.COM

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Sukcinat dehidrogenaza
Sukcinat dehidrogenaza
	Sukcinatna dehidrogenaza, 1YQ3
Identifikatori
EC broj	1.3.99.1
CAS broj	2593986
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

Sukcinat dehidrogenaza (EC 1.3.99.1, sukcinski dehidrogenaza, fumaratna reduktaza, fumarinska hidrogenaza, sukcinodehidrogenaza, dehidrogenaza sukcinske kiseline, sukcinatna oksidoreduktaza, sukcinilna dehidrogenaza, sukcinat:(akceptor) oksidoreduktaza) je enzim sa sistematskim imenom sukcinat:akceptor oksidoreduktaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju:

sukcinat + akceptor

\rightleftharpoons

fumarat + redukovani akceptor

Ovaj flavoprotein (FAD) sadrži gvožđe-sumporne centre. On je komponenta enzima EC 1.3.5.1, sukcinatne dehidrogenaze (ubihinon).

Reference

^ Hatefi, Y., Ragan, C.I. and Galante, Y.M. (1985). „The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system”. Ур.: Martonosi, A. The Enzymes of Biological Membranes. 4 (2nd изд.). New York: Plenum Press. стр. 1—70.
^ Singer, T.P. & Kearney, E.B. (1963). „Succinate dehydrogenase”. Ур.: Boyer, P.D., Lardy, H.; Myrb; auml & ck, K. The Enzymes. 7 (2nd изд.). New York: Academic Press. стр. 383—445.
^ Singer, T.P., Kearney, E.B. and Bernath, P. (1956). „Studies of succinic dehydrogenase. II. Isolation and properties of the dehydrogenase from beef heart”. J. Biol. Chem. 223: 599—613. PMID 13385208.
^ Warringa, M.G.P.J. & Giuditta, A. (1958). „Studies on succinic dehydrogenase. IX. Characterization of the enzyme from Micrococcus lactilyticus”. J. Biol. Chem. 230: 111—123. PMID 13502379.

Literatura

Hatefi, Y., Ragan, C.I. and Galante, Y.M. (1985). „The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system”. Ур.: Martonosi, A. The Enzymes of Biological Membranes. 4 (2nd изд.). New York: Plenum Press. стр. 1—70.
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.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

Succinate+dehydrogenase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Hatefi, Y., Ragan, C.I. and Galante, Y.M. (1985). „The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system”. Ур.: Martonosi, A. The Enzymes of Biological Membranes. 4 (2nd изд.). New York: Plenum Press. стр. 1—70.

[2] Singer, T.P. & Kearney, E.B. (1963). „Succinate dehydrogenase”. Ур.: Boyer, P.D., Lardy, H.; Myrb; auml & ck, K. The Enzymes. 7 (2nd изд.). New York: Academic Press. стр. 383—445.

[3] Singer, T.P., Kearney, E.B. and Bernath, P. (1956). „Studies of succinic dehydrogenase. II. Isolation and properties of the dehydrogenase from beef heart”. J. Biol. Chem. 223: 599—613. PMID 13385208.

[4] Warringa, M.G.P.J. & Giuditta, A. (1958). „Studies on succinic dehydrogenase. IX. Characterization of the enzyme from Micrococcus lactilyticus”. J. Biol. Chem. 230: 111—123. PMID 13502379.

[1]

[2]

[3]

[4]