Literature summary for 2.1.1.63 extracted from

Hashimoto, H.; Inoue, T.; Nishioka, M.; Fujiwara, S.; Takagi, M.; Imanaka, T.; Kai, Y.
Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase (1999), J. Mol. Biol., 292, 707-716.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals formed at 20°C by conventional hanging drop-vapor diffusion method	Thermococcus kodakarensis

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the enzyme repairs alkylated DNA by suicidal alkyl transfer from guanine 6-O to its own Cys residue	Thermococcus kodakarensis

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA containing 6-O-methylguanine + [protein]-L-cysteine	the enzyme repairs alkylated DNA by suicidal alkyl transfer from guanine 6-O to its own cysteine residue	Thermococcus kodakarensis	DNA lacking 6-O-methylguanine + [protein]-S-methyl-L-cysteine	-	?

Synonyms

Synonyms	Comment	Organism
Pk-MGMT	-	Thermococcus kodakarensis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	enzyme is extremely thermostable	Thermococcus kodakarensis

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Release 2023.1 (January 2023)