DNK (citozin-5-)-metiltransferaza

DNK (citozin-5-)-metiltransferaza
Identifikatori
EC broj	2.1.1.37
CAS broj	9037-42-7
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

DNK (citozin-5-)-metiltransferaza (EC 2.1.1.37, EcoRI metilaza, DNK 5-citozinska metilaza, DNK citozinska C5 metilaza, DNK citozinska metilaza, DNK metilaza, DNK metiltransferaza, DNK transmetilaza, DNK-citozinska 5-metilaza, DNK-citozinska metiltransferaza, HpaII metilaza, HpaII' metilaza, M.BsuRIa, M.BsuRIb, Tip II DNK metilaza, citozinska 5-metiltransferaza, citozinska DNK metilaza, citozinska DNK metiltransferaza, citozin-specifična DNK metiltransferaza, dezoksiribonukleinska metilaza, dezoksiribonukleinska metiltransferaza, dezoksiribonukleinska (citozin-5-)-metiltransferaza, dezoksiribonukleinska kiselina (citozin-5-)-metiltransferaza, dezoksiribonukleinska kiselina metilaza, dezoksiribonukleinska kiselina metiltransferaza, metilaza modifikacije dezoksiribonukleinske kiseline, dezoksiribonukleinska metilaza, metilfosfotriester-DNK metiltransferaza, modifikaciona metilaza, restrikciono-modifikacioni sistem, site-specifična DNK-metiltransferaza (citozin-specifična), DNK-(citozin C5)-metilaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:DNK (citozin-5-)-metiltransferaza.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8]^[9] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + DNK citozin

\rightleftharpoons

S-adenozil-L-homocistein + DNK 5-metilcitozin

Reference

↑ Gold, M. and Hurwitz, J. (1964). „The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. V. Purification and properties of the deoxyribonucleic acid-methylating activity of Escherichia coli”. J. Biol. Chem. 239: 3858-2865. PMID 14257620.
↑ Kalousek, F. and Morris, N.R. (1969). „The purification and properties of deoxyribonucleic acid methylase from rat spleen”. J. Biol. Chem. 244: 1157-1163. PMID 4975067.
↑ Roy, P.H. and Weissbach, A. (1975). „DNA methylase from HeLa cell nuclei”. Nucleic Acids Res. 2: 1669-1684. PMID 1187340.
↑ Simon, D., Grunert, F., Acken, U.Y., Döring, H.P. and Kröger, H. (1978). „DNA-methylase from regenerating rat liver: purification and characterisation”. Nucleic Acids Res. 5: 2153-2167. PMID 673848.
↑ Sneider, T.W., Teague, W.M. and Rogachewsky, L.M. (1975). „S-Adenosylmethionine: DNA-cytosine 5-methyltransferase from a Novikoff rat hepatoma cell line”. Nucleic Acids Res. 2: 1685-1700. PMID 171625.
↑ Turnbull, J.F. and Adams, R.L.P. (1976). „DNA methylase: purification from ascites cells and the effect of various DNA substrates on its activity”. Nucleic Acids Res. 3: 677-695. PMID 131936.
↑ Kessler, C. and Manta, V. (1990). „Specificity of restriction endonucleases and DNA modification methyltransferases: a review”. Gene 92: 1-248. PMID 2172084.
↑ Roberts, R.J. (1990). „Restriction enzymes and their isoschizomers”. Nucleic Acids Res. 18: 2331-2365. PMID 2159140.
↑ Yuan, R. (1981). „Structure and mechanism of multifunctional restriction endonucleases”. Annu. Rev. Biochem. 50: 285-319. PMID 6267988.

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 DNA+(cytosine-5-)-methyltransferase

[1] Gold, M. and Hurwitz, J. (1964). „The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. V. Purification and properties of the deoxyribonucleic acid-methylating activity of Escherichia coli”. J. Biol. Chem. 239: 3858-2865. PMID 14257620.

[2] Kalousek, F. and Morris, N.R. (1969). „The purification and properties of deoxyribonucleic acid methylase from rat spleen”. J. Biol. Chem. 244: 1157-1163. PMID 4975067.

[3] Roy, P.H. and Weissbach, A. (1975). „DNA methylase from HeLa cell nuclei”. Nucleic Acids Res. 2: 1669-1684. PMID 1187340.

[4] Simon, D., Grunert, F., Acken, U.Y., Döring, H.P. and Kröger, H. (1978). „DNA-methylase from regenerating rat liver: purification and characterisation”. Nucleic Acids Res. 5: 2153-2167. PMID 673848.

[5] Sneider, T.W., Teague, W.M. and Rogachewsky, L.M. (1975). „S-Adenosylmethionine: DNA-cytosine 5-methyltransferase from a Novikoff rat hepatoma cell line”. Nucleic Acids Res. 2: 1685-1700. PMID 171625.

[6] Turnbull, J.F. and Adams, R.L.P. (1976). „DNA methylase: purification from ascites cells and the effect of various DNA substrates on its activity”. Nucleic Acids Res. 3: 677-695. PMID 131936.

[7] Kessler, C. and Manta, V. (1990). „Specificity of restriction endonucleases and DNA modification methyltransferases: a review”. Gene 92: 1-248. PMID 2172084.

[8] Roberts, R.J. (1990). „Restriction enzymes and their isoschizomers”. Nucleic Acids Res. 18: 2331-2365. PMID 2159140.

[9] Yuan, R. (1981). „Structure and mechanism of multifunctional restriction endonucleases”. Annu. Rev. Biochem. 50: 285-319. PMID 6267988.

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p r u Proteini: enzimi
Teme	Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6