Arginin kinaza

Arginin kinaza
Identifikatori
EC broj	2.7.3.3
CAS broj	9026-70-4
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

Arginin kinaza (EC 2.7.3.3, argininska fosfokinaza, adenozinska 5'-trifosfat:L-argininska fosfotransferaza, adenozin 5'-trifosfat-arginin fosfotransferaza, ATP:L-arginin N-fosfotransferazal ATP:L-arginin omega-N-fosfotransferaza) je enzim sa sistematskim imenom ATP:L-arginin N^omega-fosfotransferaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

ATP + L-arginin

\rightleftharpoons

ADP + N^omega-fosfo-L-arginin

Reference uredi

↑ Elödi, P. and Szörényi, E.T. (1956). „Properties of crystalline arginine phosphoferase isolated from crustacean muscle”. Acta Physiol. Acad. Sci. (Hung.) 9: 367-379. PMID 13339436.
↑ Morrison, J.F., Griffiths, D.E. and Ennor, A.H. (1957). „The purification and properties of arginine phosphokinase”. Biochem. J. 65: 143-153. PMID 13403885.
↑ Szörényi, E.T., Dvornikova, P.D. and Degtyar, P.G. (1949). „[Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.]”. Dokl. Akad. Nauk SSSR. 67: 341-344.
↑ Virden, R., Watts, D.C. and Baldwin, E. (1965). „Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle: purification and properties”. Biochem. J. 94: 536-544. PMID 14340045.

Literatura uredi

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.

Vanjske veze uredi

MeSH Arginine+kinase

[1] Elödi, P. and Szörényi, E.T. (1956). „Properties of crystalline arginine phosphoferase isolated from crustacean muscle”. Acta Physiol. Acad. Sci. (Hung.) 9: 367-379. PMID 13339436.

[2] Morrison, J.F., Griffiths, D.E. and Ennor, A.H. (1957). „The purification and properties of arginine phosphokinase”. Biochem. J. 65: 143-153. PMID 13403885.

[3] Szörényi, E.T., Dvornikova, P.D. and Degtyar, P.G. (1949). „[Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.]”. Dokl. Akad. Nauk SSSR. 67: 341-344.

[4] Virden, R., Watts, D.C. and Baldwin, E. (1965). „Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle: purification and properties”. Biochem. J. 94: 536-544. PMID 14340045.

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