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Sterol 24-C-metiltransferaza
Identifikatori
EC broj	2.1.1.41
CAS broj	37257-07-1
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

Sterol 24-C-metiltransferaza (EC 2.1.1.41, Delta24-metiltransferaza, Delta24-sterol metiltransferaza, zimosterol-24-metiltransferaza, S-adenozil-4-metionin:sterol Delta24-metiltransferaza, SMT1, 24-sterol C-metiltransferaza, S-adenozil-L-metionin:Delta24(23)-sterol metiltransferaza, fitosterol metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:zimosterol 24-C-metiltransferaza.^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + 5alfa-holesta-8,24-dien-3beta-ol

\rightleftharpoons

S-adenozil-L-homocistein + 24-metilin-5alfa-holest-8-en-3beta-ol

Za dejstvo ovog enzima je neophodan glutation. On deluje na opseg sterola sa 24(25)-dvostrukom vezom u bočnom lancu.

Reference

↑ Moore, J.T., Jr. and Gaylor, J.L. (1969). „Isolation and purification of an S-adenosylmethionine: Δ²⁴-sterol methyltransferase from yeast”. J. Biol. Chem. 244: 6334-6340. PMID 5354959.
↑ Venkatramesh, M., Guo, D., Jia, Z. and Nes, W.D. (1996). „Mechanism and structural requirements for transformations of substrates by the S-adenosyl-L-methionine:Δ²⁴⁽²⁵⁾-sterol methyl transferase enzyme from Saccharomyces cerevisiae”. Biochim. Biophys. Acta 1299: 313-324. PMID 8597586.
↑ Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins, M.D., Zhou, W., Lopez, M. and Nes, W.D. (1997). „, Stereochemical features of C-methylation on the path to Δ²⁴⁽²⁸⁾-methylene and Δ²⁴⁽²⁸⁾-ethylidene sterols: studies on the recombinant phytosterol methyl transferase from Arabidopsis thaliana”. Tetrahedron Lett. 38: 6115-6118.
↑ Bouvier-Navé, P., Husselstein, T. and Benveniste, P. (1998). „Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant biosynthesis”. Eur. J. Biochem. 256: 88-96. PMID 9746350.
↑ Nes, W.D., McCourt, B.S., Zhou, W., Ma, J., Marshall, J.A., Peek, L.A. and Brennan, M. (1998). „Overexpression, purification, and stereochemical studies of the recombinant S-adenosyl-L-methionine:Δ²⁴⁽²⁵⁾- to Δ²⁴⁽²⁸⁾-sterol methyl transferase enzyme from Saccharomyces cerevisiae sterol methyl transferase”. Arch. Biochem. Biophys. 353: 297-311. PMID 9606964.

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.

Vanjske veze

MeSH Sterol+24-C-methyltransferase

[1] Moore, J.T., Jr. and Gaylor, J.L. (1969). „Isolation and purification of an S-adenosylmethionine: Δ²⁴-sterol methyltransferase from yeast”. J. Biol. Chem. 244: 6334-6340. PMID 5354959.

[2] Venkatramesh, M., Guo, D., Jia, Z. and Nes, W.D. (1996). „Mechanism and structural requirements for transformations of substrates by the S-adenosyl-L-methionine:Δ²⁴⁽²⁵⁾-sterol methyl transferase enzyme from Saccharomyces cerevisiae”. Biochim. Biophys. Acta 1299: 313-324. PMID 8597586.

[3] Tong, Y., McCourt, B.S., Guo, D., Mangla, A.T., Zhou, W.X., Jenkins, M.D., Zhou, W., Lopez, M. and Nes, W.D. (1997). „, Stereochemical features of C-methylation on the path to Δ²⁴⁽²⁸⁾-methylene and Δ²⁴⁽²⁸⁾-ethylidene sterols: studies on the recombinant phytosterol methyl transferase from Arabidopsis thaliana”. Tetrahedron Lett. 38: 6115-6118.

[4] Bouvier-Navé, P., Husselstein, T. and Benveniste, P. (1998). „Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant biosynthesis”. Eur. J. Biochem. 256: 88-96. PMID 9746350.

[5] Nes, W.D., McCourt, B.S., Zhou, W., Ma, J., Marshall, J.A., Peek, L.A. and Brennan, M. (1998). „Overexpression, purification, and stereochemical studies of the recombinant S-adenosyl-L-methionine:Δ²⁴⁽²⁵⁾- to Δ²⁴⁽²⁸⁾-sterol methyl transferase enzyme from Saccharomyces cerevisiae sterol methyl transferase”. Arch. Biochem. Biophys. 353: 297-311. PMID 9606964.

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