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Literature summary for 5.6.2.4 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

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 [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

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/ Products (Substrates)

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

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 and Products (Substrate)

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

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

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

General Information

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