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(Citohrom c)-arginin N-metiltransferaza
(Citohrom c)-arginin N-metiltransferaza
Identifikatori
EC broj	2.1.1.124
CAS broj	2613498
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
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(Citohrom c)-arginin N-metiltransferaza (EC 2.1.1.124, S-adenozil-L-metionin:(citohrom c)-arginin omega-N-metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:(citohrom c)-arginin N^omega-metiltransferaza.^[1] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + [citohrom c]-arginin

\rightleftharpoons

S-adenozil-L-homocistein + [citohrom c]-N^omega-metil-arginin

Enzim iz Euglena gracilis metiluje Arg-38 citohroma c u srcu konja, čime se formira Nomega-monometil-argininski derivat.

Reference

^ Farooqui, J.Z., Tuck, M., Paik, W.K. (1985). „Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochrome c”. J. Biol. Chem. 260: 537—545. PMID 2981218.

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

(cytochrome+c)-arginine+N-methyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Farooqui, J.Z., Tuck, M., Paik, W.K. (1985). „Purification and characterization of enzymes from Euglena gracilis that methylate methionine and arginine residues of cytochrome c”. J. Biol. Chem. 260: 537—545. PMID 2981218.

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