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PubMed	članci
NCBI	proteini

(Citohrom c)-metionin S-metiltransferaza
(Citohrom c)-metionin S-metiltransferaza
Identifikatori
EC broj	2.1.1.123
CAS broj	93585-98-9
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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NCBI	proteini

(Citohrom c)-metionin S-metiltransferaza (EC 2.1.1.123, (cytochrome-c)-methionine S-methyltransferase) je enzim sa sistematskim imenom S-adenozil-L-metionin:(citohrom c)-metionin S-metiltransferaza.^[1] Ovaj enzim katalizuje sledeću hemijsku reakciju

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

\rightleftharpoons

S-adenozil-L-homocistein + [citohrom c]-S-metil-metionin

Enzim iz Euglena gracilis metiluje Met-65 citohroma c u srcu konja.

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)-methionine+S-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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