A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 220.127.116.11
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|DNA ligase (ATP or NAD(+)).
- ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) <=> (deoxyribonucleotide)(n+m) + AMP + diphosphate
- NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) <=> (deoxyribonucleotide)(n+m) + AMP + beta-nicotinamide D-nucleotide
- The enzymes from the archaea Thermococcus fumicolans and Thermococcus
onnurineus show high activity with either ATP or NAD(+),
and significantly lower activity with TTP, GTP, and CTP.
- The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and
5'-phosphate termini, forming a phosphodiester and sealing certain
types of single-strand breaks in duplex DNA.
- Catalysis occurs by a three-step mechanism, starting with the
activation of the enzyme by ATP or NAD(+), forming a phosphoramide
bond between adenylate and a lysine residue.
- The adenylate group is then transferred to the 5'-phosphate terminus
of the substrate, forming the capped structure
- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH
terminus on the capped terminus, which results in formation of the
phosphodiester bond and release of the adenylate.
- Different from EC 18.104.22.168, EC 22.214.171.124 and EC 126.96.36.199.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
entries corresponding to 6.5.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.-.-.-