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Literature summary extracted from

  • Roberts, A.; Pelton, J.G.; Wemmer, D.E.
    Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase (2006), Magn. Reson. Chem., 44, S71-S82.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.63 transformed into Escherichia coli BL21(DE3) Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.63 Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.63 on NaCl gradient Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.63 DNA containing 6-O-methylguanine + [protein]-L-cysteine
-
 Methanocaldococcus jannaschii DNA lacking 6-O-methylguanine + [protein]-S-methyl-L-cysteine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.63 More structure analysis by multinuclear multidimensional NMR spectroscopy, a two-domain protein with an alpha/beta fold, N-terminal domain consists of a three-stranded antiparallel beta sheet, N-terminus is somewhat less well defined than the C-terminus, structure is similar to homologs from other organisms that have been determined by crystallography, with some variation in the N-terminal domain, whereas the C-terminal domain is more highly conserved in both sequence and structure Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.1.1.63 MGMT
-
 Methanocaldococcus jannaschii
2.1.1.63 MJ1529
-
 Methanocaldococcus jannaschii
2.1.1.63 O6-methylguanine-DNA methyltransferase
-
 Methanocaldococcus jannaschii