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Information on EC 6.5.1.1 - DNA ligase (ATP) and Organism(s) Xenopus tropicalis

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EC Tree
IUBMB Comments
The enzyme catalyses 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, 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 5'-(5'-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses 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. RNA can also act as substrate, to some extent. cf. EC 6.5.1.2, DNA ligase (NAD+), EC 6.5.1.6, DNA ligase (ATP or NAD+), and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP).
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Xenopus tropicalis
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Word Map
The taxonomic range for the selected organisms is: Xenopus tropicalis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
dna ligase, dna repair enzyme, dna ligase i, t4 dna ligase, dna ligase iv, dna ligase iii, ligase 1, dna ligase ii, polynucleotide ligase, dna ligase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deoxyribonucleate ligase
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Deoxyribonucleic acid joinase
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Deoxyribonucleic acid ligase
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Deoxyribonucleic acid repair enzyme
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Deoxyribonucleic acid-joining enzyme
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Deoxyribonucleic joinase
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Deoxyribonucleic ligase
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Deoxyribonucleic repair enzyme
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Deoxyribonucleic-joining enzyme
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DNA joinase
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DNA ligase
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DNA ligase I
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DNA ligase II
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DNA ligase III
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DNA ligase IV homolog
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DNA repair enzyme
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DNA-joining enzyme
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Lig(Tk)
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Pfu DNA ligase
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Polydeoxyribonucleotide synthase (ATP)
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Polydeoxyribonucleotide synthase [ATP]
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Polynucleotide ligase
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Sealase
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SYSTEMATIC NAME
IUBMB Comments
poly(deoxyribonucleotide)-3'-hydroxyl:5'-phospho-poly(deoxyribonucleotide) ligase (ATP)
The enzyme catalyses 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, 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 5'-(5'-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses 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. RNA can also act as substrate, to some extent. cf. EC 6.5.1.2, DNA ligase (NAD+), EC 6.5.1.6, DNA ligase (ATP or NAD+), and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP).
CAS REGISTRY NUMBER
COMMENTARY hide
9015-85-4
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
F6WCY3_XENTR
982
0
109365
TrEMBL
other Location (Reliability: 2)
A0A6I8RT82_XENTR
978
0
108668
TrEMBL
other Location (Reliability: 2)
A0A6I8RLW0_XENTR
960
0
108189
TrEMBL
Mitochondrion (Reliability: 2)
Q28EB8_XENTR
911
0
103871
TrEMBL
other Location (Reliability: 2)
B4F6N5_XENTR
893
0
100464
TrEMBL
Mitochondrion (Reliability: 2)
A0A6I8RS22_XENTR
1061
0
118973
TrEMBL
other Location (Reliability: 4)
A0A6I8SX70_XENTR
1006
0
112797
TrEMBL
other Location (Reliability: 3)
A0A6I8QF24_XENTR
879
0
98892
TrEMBL
Mitochondrion (Reliability: 2)
F6WXI9_XENTR
982
0
110405
TrEMBL
Mitochondrion (Reliability: 2)
A0A5S6LXI1_XENTR
800
0
90209
TrEMBL
Mitochondrion (Reliability: 2)
F6SN56_XENTR
911
0
103845
TrEMBL
other Location (Reliability: 2)
A0A6I8REA4_XENTR
1003
0
112456
TrEMBL
other Location (Reliability: 2)
A0A8J0QYK6_XENTR
1040
0
116781
TrEMBL
other Location (Reliability: 2)