AGT II
O6-alkylguanine DNA alkyltransferase II (O6 AGT II) previously known as O6 Guanine transferase (ogt) is a bacterial protein that is involved in DNA repair together with Ada ( also known as O6 AGT I).[1]
Like AGT I, AGT II is responsible for the removal of alkyl groups from O6-alkyl guanine, O4-alkyl thymine and alkyl phosphotriester in the sugar-phosphate backbone of DNA.[1] AGT II shows a greater preference for O4-alkyl thymine than O6-alkyl guanine and alkyl phosphotriester.[1][2]
Unlike Ada, AGT II is expressed constitutively in cells.[1][3] Therefore, AGT II will repair alkylated DNA adducts even before Ada is fully induced. AGT II is similar to Ada in its suicide inactivation in that AGT II transfers the alkyl group to a cysteine residue in its own structure, thereby inactivating itself.[1] The human equivalent of AGT II is O6-alkylguanine DNA alkyltransferase, a protein that in humans is encoded by the O6-methylguanine DNA methyltransferase (MGMT) gene. In humans, O6-alkylguanine DNA alkyltransferase preferentially removes alkyl groups from O6-alkyl guanine rather than from O6–alkyl thymine.[1]
References
^ abcdef Friedberg E, Walker GC, Siede W, Wood RD, Schultz RA, Ellenberger T (2006). DNA Repair and Mutagenesis (2 ed.). Washington, DC: ASM Press. ISBN 1-55581-319-4. OCLC 59360087..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
^ Sassanfar M, Dosanjh MK, Essigmann JM, Samson L (February 1991). "Relative efficiencies of the bacterial, yeast, and human DNA methyltransferases for the repair of O6-methylguanine and O4-methylthymine. Suggestive evidence for O4-methylthymine repair by eukaryotic methyltransferases". The Journal of Biological Chemistry. 266 (5): 2767–71. PMID 1993655.
^ Rebeck GW, Samson L (March 1991). "Increased spontaneous mutation and alkylation sensitivity of Escherichia coli strains lacking the ogt O6-methylguanine DNA repair methyltransferase". Journal of Bacteriology. 173 (6): 2068–76. PMC 207742. PMID 2002008.
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
