Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DNA | MtUvrB possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA | Mycobacterium tuberculosis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of MtUvrB ATPase activity in the absence and presence of DNA | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates DNA unwinding activity, required for the ATPase activity | Mycobacterium tuberculosis | |
Mn2+ | activates DNA unwinding activity | Mycobacterium tuberculosis | |
additional information | effect of different metal ions on MtUvrB helicase activity, poor activation of DNA unwinding activity by CA2+, Zn2+, Cu2+, Co2+, and Fe3+ | Mycobacterium tuberculosis | |
NaCl | induces dissociation of MtUvrB-ssDNA complexes | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Mycobacterium tuberculosis | - |
ADP + phosphate | - |
? | |
ATP + H2O | Mycobacterium tuberculosis H37Rv | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WFC7 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WFC7 | - |
- |
no activity in Escherichia coli | - |
Escherichia coli UvrB (EcUvrB) binds weakly to undamaged DNA and has no ATPase activity. EcUvrB does not possess DNA unwinding activity | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Mycobacterium tuberculosis | ADP + phosphate | - |
? | |
ATP + H2O | - |
Mycobacterium tuberculosis H37Rv | ADP + phosphate | - |
? | |
dATP + H2O | - |
Mycobacterium tuberculosis | dADP + phosphate | - |
? | |
dATP + H2O | - |
Mycobacterium tuberculosis H37Rv | dADP + phosphate | - |
? | |
additional information | Mycobacterium tuberculosis UvrB (MtUvrB) possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA. MtUvrB binds to DNA in a structure-dependent manner. MtUvrB substrate specificity is analyzed, revealing that it associates preferentially with single-stranded DNA, duplexes with 3' or 5' overhangs, and linear duplex DNA with splayed arms. MtUvrB possesses DNA unwinding activity characteristic of an ATP-dependent DNA helicase. The helicase activity of MtUvrB proceeds in the 3' to 5' direction and is strongly modulated by a nontranslocating 5' single-stranded tail, indicating that in addition to the translocating strand it also interacts with the 5' end of the substrate. The fraction of DNA unwound by MtUvrB decreases significantly as the length of the duplex increases: it fails to unwind duplexes longer than 70 bp. No or poor activity with GTP, dGTP, CTP, dCTP, UTP, dUTP, ATPgammaS, and AMP-PNP | Mycobacterium tuberculosis | ? | - |
- |
|
additional information | Mycobacterium tuberculosis UvrB (MtUvrB) possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA. MtUvrB binds to DNA in a structure-dependent manner. MtUvrB substrate specificity is analyzed, revealing that it associates preferentially with single-stranded DNA, duplexes with 3' or 5' overhangs, and linear duplex DNA with splayed arms. MtUvrB possesses DNA unwinding activity characteristic of an ATP-dependent DNA helicase. The helicase activity of MtUvrB proceeds in the 3' to 5' direction and is strongly modulated by a nontranslocating 5' single-stranded tail, indicating that in addition to the translocating strand it also interacts with the 5' end of the substrate. The fraction of DNA unwound by MtUvrB decreases significantly as the length of the duplex increases: it fails to unwind duplexes longer than 70 bp. No or poor activity with GTP, dGTP, CTP, dCTP, UTP, dUTP, ATPgammaS, and AMP-PNP | Mycobacterium tuberculosis H37Rv | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
monomer | Mycobacterium tuberculosis UvrB (MtUvrB) exists in solution as a monomer | Mycobacterium tuberculosis |
More | domain structure of MtUvrB, sequence comparisons of UvrB enzymes, comparison with Escherichia coli UvrB enzyme, overview | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
ATP-dependent DNA helicase | - |
Mycobacterium tuberculosis |
DNA-stimulated ATPase | - |
Mycobacterium tuberculosis |
MtUvrB | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
evolution | conserved helicase domains of EcUvrB and MtUvrB | Mycobacterium tuberculosis |
metabolism | the enzyme is involved in the nucleotide excision repair (NER) pathway | Mycobacterium tuberculosis |
physiological function | Mycobacterium tuberculosis UvrB is a robust DNA-stimulated ATPase that also possesses structure-specific ATP-dependent DNA helicase activity. It plays an alternative role in the processing of key DNA replication intermediates | Mycobacterium tuberculosis |