Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.2.4 extracted from

  • Dixon, E.P.; Pahel, G.L.; Rocque, W.J.; Barnes, J.A.; Lobe, D.C.; Hanlon, M.H.; Alexander, K.A.; Chao, S.F.; Lindley, K.; Phelps, W.C.
    The E1 helicase of human papillomavirus type 11 binds to the origin of replication with low sequence specificity (2000), Virology, 270, 345-357.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D523N DNA binding and ATPase activity is comparable to wild-type enzyme, no in vitro replication activity human papillomavirus 11
D542N DNA binding and ATPase activity is comparable to wild-type enzyme, no in vitro replication activity human papillomavirus 11
K484E mutant enzyme binds the immunoaffinity column poorly, the heparin purified E1/K484E is tested for the above activities. The protein that is recovered shows no activity human papillomavirus 11
P479S DNA binding and ATPase activity is comparable to wild-type enzyme, 50% of in vitro replication activity compared to wild-type enzyme human papillomavirus 11

Organism

Organism UniProt Comment Textmining
human papillomavirus 11 P04014
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
human papillomavirus 11 ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
E1 helicase
-
human papillomavirus 11