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Literature summary extracted from

  • Thakur, M.; Kumar, M.B.; Muniyappa, K.
    Mycobacterium tuberculosis UvrB is a robust DNA-stimulated ATPase that also possesses structure-specific ATP-dependent DNA helicase activity (2016), Biochemistry, 55, 5865-5883 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.6.2.4 DNA MtUvrB possesses intrinsic ATPase activity that is greatly stimulated by both single- and double-stranded DNA Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.2.4 additional information
-
 additional information kinetics of MtUvrB ATPase activity in the absence and presence of DNA Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.4 Mg2+ activates DNA unwinding activity, required for the ATPase activity Mycobacterium tuberculosis
5.6.2.4 Mn2+ activates DNA unwinding activity Mycobacterium tuberculosis
5.6.2.4 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
5.6.2.4 NaCl induces dissociation of MtUvrB-ssDNA complexes Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.2.4 ATP + H2O Mycobacterium tuberculosis
-
 ADP + phosphate
-
 ?
5.6.2.4 ATP + H2O Mycobacterium tuberculosis H37Rv
-
 ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.4 Mycobacterium tuberculosis P9WFC7
-
-
5.6.2.4 Mycobacterium tuberculosis H37Rv P9WFC7
-
-
5.6.2.4 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.4 ATP + H2O
-
 Mycobacterium tuberculosis ADP + phosphate
-
 ?
5.6.2.4 ATP + H2O
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate
-
 ?
5.6.2.4 dATP + H2O
-
 Mycobacterium tuberculosis dADP + phosphate
-
 ?
5.6.2.4 dATP + H2O
-
 Mycobacterium tuberculosis H37Rv dADP + phosphate
-
 ?
5.6.2.4 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 ?
-
-
5.6.2.4 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

EC Number Subunits Comment Organism
5.6.2.4 monomer Mycobacterium tuberculosis UvrB (MtUvrB) exists in solution as a monomer Mycobacterium tuberculosis
5.6.2.4 More domain structure of MtUvrB, sequence comparisons of UvrB enzymes, comparison with Escherichia coli UvrB enzyme, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
5.6.2.4 ATP-dependent DNA helicase
-
 Mycobacterium tuberculosis
5.6.2.4 DNA-stimulated ATPase
-
 Mycobacterium tuberculosis
5.6.2.4 MtUvrB
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
5.6.2.4 evolution conserved helicase domains of EcUvrB and MtUvrB Mycobacterium tuberculosis
5.6.2.4 metabolism the enzyme is involved in the nucleotide excision repair (NER) pathway Mycobacterium tuberculosis
5.6.2.4 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