Literature summary extracted from
Rasimas, J.J.; Kanugula, S.; Dalessio, P.M.; Ropson, I.J.; Fried, M.G.; Pegg, A.E.
Effects of zinc occupancy on human O6-alkylguanine-DNA alkyltransferase (2003), Biochemistry, 42, 980-990.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.1.1.63 |
C5A |
smaller increase in stability on zinc addition than the wild-type hAGT |
Homo sapiens |
2.1.1.63 |
H29A |
does not show the stability enehancement of wild-type hAGT with its intact zinc coordination sphere |
Homo sapiens |
2.1.1.63 |
H85A |
does not show the stability enehancement of wild-type hAGT with its intact zinc coordination sphere |
Homo sapiens |
General Stability
EC Number |
General Stability |
Organism |
---|
2.1.1.63 |
zinc provides conformational stability to hAGT that may influence its regulation |
Homo sapiens |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.1.1.63 |
Zinc |
in bacterial expression systems, recombinant hAGT is produced in increasingly larger quantities when growth media are supplemented with up to 0.1 mM ZnCl2. Metal-enriched hAGT samples have a 5fold increase in repair rate constant over conventionally purified protein samples and a 60fold increase over metal-stripped hAGT. Zinc confers a mechanistic enhancement to repair activity that does not result from an increase in substrate binding affinity. Zinc also provides conformational stability to hAGT that may influence its regulation |
Homo sapiens |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.1.63 |
Homo sapiens |
- |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.1.1.63 |
hAGT |
- |
Homo sapiens |