(Izocitrat dehidrogenaza (NADP+)) kinaza

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

(izocitrat dehidrogenaza (NADP⁺)) kinaza
(izocitrat dehidrogenaza (NADP+)) kinaza
Identifikatori
EC broj	2.7.11.5
CAS broj	83682-93-3
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

(izocitrat dehidrogenaza (NADP⁺)) kinaza (EC 2.7.11.5, (izocitratna dehidrogenaza (NADP⁺)) kinaza, ICDH kinaza/fosfataza, IDH kinaza, IDH kinaza/fosfataza, IDH-K/P, IDHK/P, izocitrat dehidrogenaza kinaza (fosforilacija), izocitrat dehidrogenaza kinaza/fosfataza, STK3) je enzim sa sistematskim imenom ATP:(izocitrat dehidrogenaza (NADP⁺)) fosfotransferaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + [izocitrat dehidrogenaza (NADP⁺)]

\rightleftharpoons

ADP + [izocitrat dehidrogenaza (NADP⁺)] fosfat

Ovaj enzim nema aktivirajuće jedinjenje, ali je specifičan za svoj supstrat.

Reference

^ Wang, J.Y.J. & Koshland, D.E., Jr. (1982). „The reversible phosphorylation of isocitrate dehydrogenase of Salmonella typhimurium”. Arch. Biochem. Biophys. 218: 59—67. PMID 6756316.
^ Miller, S.P., Karschnia, E.J., Ikeda, T.P. and LaPorte, D.C. (1996). „Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins”. J. Biol. Chem. 271: 19124—19128. PMID 8702587.
^ Singh, S.K., Matsuno, K., LaPorte, D.C. and Banaszak, L.J. (2001). „Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase”. J. Biol. Chem. 276: 26154—26163. PMID 11290745.
^ Oudot, C., Cortay, J.C., Blanchet, C., Laporte, D.C., Di Pietro, A., Cozzone, A.J. and Jault, J.M. (2001). „T'he "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases”. Biochemistry. 40: 3047—3055. PMID 11258918.

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.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

(isocitrate+dehydrogenase+(NADP+))+kinase на US National Library of Medicine Medical Subject Headings (MeSH)

Категорија

[1] Wang, J.Y.J. & Koshland, D.E., Jr. (1982). „The reversible phosphorylation of isocitrate dehydrogenase of Salmonella typhimurium”. Arch. Biochem. Biophys. 218: 59—67. PMID 6756316.

[2] Miller, S.P., Karschnia, E.J., Ikeda, T.P. and LaPorte, D.C. (1996). „Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins”. J. Biol. Chem. 271: 19124—19128. PMID 8702587.

[3] Singh, S.K., Matsuno, K., LaPorte, D.C. and Banaszak, L.J. (2001). „Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase”. J. Biol. Chem. 276: 26154—26163. PMID 11290745.

[4] Oudot, C., Cortay, J.C., Blanchet, C., Laporte, D.C., Di Pietro, A., Cozzone, A.J. and Jault, J.M. (2001). „T'he "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases”. Biochemistry. 40: 3047—3055. PMID 11258918.

[1]

[2]

[3]

[4]

п р у Enzimi
Teme	Aktivno mesto Alosterna regulacija Mesto vezivanja Katalitički perfektan enzim Koenzim Kofaktor Kooperativnost EC broj Enzimska kataliza Inhibicija enzima Enzimska kinetika Lajnviver—Berkov dijagram Mihaelis—Mentenina kinetika Spisak enzima
Tipovi	EC1 Oksidoreduktaze /spisak EC2 Transferaze /spisak EC3 Hidrolaze /spisak EC4 Lijaze /spisak EC5 Izomeraze /spisak EC6 Ligaze /spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

(Izocitrat dehidrogenaza (NADP+)) kinaza

Reference

Literatura

Spoljašnje veze

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