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Trimetilamin dehidrogenaza
Identifikatori
EC broj	1.5.8.2
CAS broj	39307-09-0
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

Trimetilamin dehidrogenaza (EC 1.5.8.2, trimetilaminska dehidrogenaza) je enzim sa sistematskim imenom trimetilamin:elektron-transfer flavoprotein oksidoreduktaza (demetilacija).^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju:

trimetilamin + H₂O + elektron-transfer flavoprotein

\rightleftharpoons

dimetilamin + formaldehid + redukovani elektron-transfer flavoprotein

Znata broj alkil-supstituisanih derivata trimetilamina takođe mogu da deluju kao elektronski donori.

Reference

↑ Colby, J. and Zatman, L.J. (1971). „The purification and properties of a bacterial trimethylamine dehydrogenase”. Biochem. J. 121: 9P-10P. PMID 5116569.
↑ Steenkamp, D.J. and Singer, T.P. (1978). „Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis”. Biochem. J. 169: 361-369. PMID 204297.
↑ Huang, L.X., Rohlfs, R.J. and Hille, R. (1995). „The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein”. J. Biol. Chem. 270: 23958-23965. PMID 7592591.
↑ Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. (2002). „Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein”. J. Biol. Chem. 277: 8457-8465. PMID 11756429.
↑ Scrutton, N.S. and Sutcliffe, M.J. (2000). „Trimethylamine dehydrogenase and electron transferring flavoprotein”. Subcell. Biochem. 35: 145-181. PMID 11192721.

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 Trimethylamine+dehydrogenase

[1] Colby, J. and Zatman, L.J. (1971). „The purification and properties of a bacterial trimethylamine dehydrogenase”. Biochem. J. 121: 9P-10P. PMID 5116569.

[2] Steenkamp, D.J. and Singer, T.P. (1978). „Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis”. Biochem. J. 169: 361-369. PMID 204297.

[3] Huang, L.X., Rohlfs, R.J. and Hille, R. (1995). „The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein”. J. Biol. Chem. 270: 23958-23965. PMID 7592591.

[4] Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. (2002). „Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein”. J. Biol. Chem. 277: 8457-8465. PMID 11756429.

[5] Scrutton, N.S. and Sutcliffe, M.J. (2000). „Trimethylamine dehydrogenase and electron transferring flavoprotein”. Subcell. Biochem. 35: 145-181. PMID 11192721.

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