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BRENDA support

Literature summary for 6.5.1.2 extracted from

  • Feng, H.; Parker, J.M.; Lu, J.; Cao, W.
    Effects of deletion and site-directed mutations on ligation steps of NAD+-dependent DNA ligase: a biochemical analysis of BRCA1 C-terminal domain (2004), Biochemistry, 43, 12648-12659.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A644I mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
E654A mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
G617I mutation in BRCT domain, mutant enzyme does not shows any detectable ligation with nicked substrate in excess Thermus sp. AK16D
G634I mutation in BRCT domain, ligation activity is about 15% of the activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
G638I mutation in BRCT domain, ligation activity is 30-40% lower than that with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
K619R mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
K640R mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
L647A mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
R606A mutation in BRCT domain, ligation activity is 30-40% lower than that with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
S623A mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
T599A mutation in BRCT domain, ligation activity is 30-40% lower than that with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D
V624A mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess Thermus sp. AK16D

Organism

Organism UniProt Comment Textmining
Thermus sp. AK16D
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