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5-Metiltetrahidrofolat:korinoid/gvožđe-sumpor protein Co-metiltransferaza
5-Metiltetrahidrofolat:korinoid/gvožđe-sumpor protein Co-metiltransferaza
Identifikatori
EC broj	2.1.1.258
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

5-Metiltetrahidrofolat:korinoid/gvožđe-sumpor protein Co-metiltransferaza (EC 2.1.1.258, acsE (gen)) je enzim sa sistematskim imenom 5-metiltetrahidrofolat:korinoid/gvožđe-sumporna proteinska metiltransferaza.^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

[metil-Co(III) korinoidni Fe-S protein] + tetrahidrofolat

\rightleftharpoons

[Co(I) korinoidni Fe-S protein] + 5-metiltetrahidrofolat

Ovaj enzim katalizuje transfer metil grupe sa N⁵ pozicije metiltetrahidrofolata na 5-metoksibenzimidazolilkobamidni kofaktor korinoid/Fe-S proteina.

Reference

^ Roberts, D.L., Zhao, S., Doukov, T. and Ragsdale, S.W. (1994). „The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum”. J. Bacteriol. 176: 6127—6130. PMID 7928975.
^ Doukov, T., Seravalli, J., Stezowski, J.J. and Ragsdale, S.W. (2000). „Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase”. Structure. 8: 817—830. PMID 10997901.
^ Doukov, T.I., Hemmi, H., Drennan, C.L. and Ragsdale, S.W. (2007). „Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases”. J. Biol. Chem. 282: 6609—6618. PMID 17172470.

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.

Spoljašnje veze

5-methyltetrahydrofolate:corrinoid/iron-sulfur+protein+Co-methyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Roberts, D.L., Zhao, S., Doukov, T. and Ragsdale, S.W. (1994). „The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum”. J. Bacteriol. 176: 6127—6130. PMID 7928975.

[2] Doukov, T., Seravalli, J., Stezowski, J.J. and Ragsdale, S.W. (2000). „Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase”. Structure. 8: 817—830. PMID 10997901.

[3] Doukov, T.I., Hemmi, H., Drennan, C.L. and Ragsdale, S.W. (2007). „Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases”. J. Biol. Chem. 282: 6609—6618. PMID 17172470.

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