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Kreatin kinaza
	Kreatin kinaza MM, homodimer, Human
Identifikatori
EC broj	2.7.3.2
CAS broj	9001-15-4
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Kreatin kinaza (EC 2.7.3.2, ATP:kreatin fosfotransferaza, CK, MM-CK, MB-CK, BB-CK, kreatinska fosfokinaza, kreatinska fosfotransferaza, fosfokreatinska kinaza, adenozin trifosfat-kreatinska transfosforilaza, Mi-CK, CK-BB, CK-MM, CK-MB, CKMiMi, MiMi-CK) je enzim sa sistematskim imenom ATP:kreatin N-fosfotransferaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + kreatin

\rightleftharpoons

ADP + fosfokreatin

N-etilglikocijamin takođe može da deluje kao akceptor.

Reference

↑ Ennor, A.H., Rosenberg, H. and Armstrong, M.D. (1955). „Specificity of creatine phosphokinase”. Nature 175: 120-120. PMID 13235819.
↑ Keutel, H.J., Jacobs, H.K., Okabe, K., Yue, R.H. and Kuby, S.A. (1968). „Studies on adenosine triphosphate transphosphorylases. VII. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylase from calf brain”. Biochemistry 7: 4283-4290. PMID 5750168.
↑ Kuby, S.A., Noda, L. and Lardy, H.A. (1954). „Adenosine triphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle”. J. Biol. Chem. 209: 191-201. PMID 13192073.
↑ Kuby, S.A. and Noltmann, E.A. (1962). „ATP-creatine transphosphorylase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 515-603.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Kuby, S.A. and Noltmann, E.A. (1962). „ATP-creatine transphosphorylase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 515-603.

Vanjske veze

MeSH Creatine+kinase

[1] Ennor, A.H., Rosenberg, H. and Armstrong, M.D. (1955). „Specificity of creatine phosphokinase”. Nature 175: 120-120. PMID 13235819.

[2] Keutel, H.J., Jacobs, H.K., Okabe, K., Yue, R.H. and Kuby, S.A. (1968). „Studies on adenosine triphosphate transphosphorylases. VII. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylase from calf brain”. Biochemistry 7: 4283-4290. PMID 5750168.

[3] Kuby, S.A., Noda, L. and Lardy, H.A. (1954). „Adenosine triphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle”. J. Biol. Chem. 209: 191-201. PMID 13192073.

[4] Kuby, S.A. and Noltmann, E.A. (1962). „ATP-creatine transphosphorylase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 515-603.

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