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Mgmt |
Protein FULL name:
methylated-DNA--protein-cysteine methyltransferase [Mus musculus].
Mgmt (Mus musculus) is product of expression of Mgmt gene.
FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine.
COFACTOR: Binds 1 zinc ion (By similarity).
SUBCELLULAR LOCATION: Nucleus (Probable).
MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocytalyst that acts repeatedly and over many reaction cycles.
SIMILARITY: Belongs to the MGMT family.
| NCBI GenPept GI number(s): |
6678878 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | P26187 |
P26187 |
| PFAM: | - |
P26187 (Link - using uniprot id) |
| InterPro: | - |
P26187 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MAETCKMKYSVLDSPLGKMELSGCERGLHGIRLLSGKTPNTDPTEAPATP EVLGGPEGVPEPLVQCTAWLEAYFREPAATEGLPLPALHHPVFQQDSFTR QVLWKLLKVVKFGETVSYQQLAALAGNPKAARAVGGAMRSNPVPILIPCH RVVRSDGAIGHYSGGGQAVKEWLLAHEGIPTGQPASKGLGLTGTWLKSSF ESTSSEPSGRN |
Mgmt (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| Characterization of cDNA encoding mouse DNA repair protein O6-methylguanine-DNA methyltransferase and high-level expression of the wild-type and mutant proteins in Escherichia coli. | Shiota S, von Wronski MA, Tano K, Bigner DD, Brent TP, Mitra S | Biochemistry Jan. 25, 1992 |
| The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). | Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J | Genome Res Oct. 1, 2004 |
Last modification of this entry: Oct. 6, 2010.
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