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Literature summary for 5.6.2.4 extracted from

  • Curti, E.; Smerdon, S.J.; Davis, E.O.
    Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD (2006), J. Bacteriol., 189, 1542-1555.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.4

Cloned(Commentary)

Cloned (Comment) Organism
histidine-tagged form of the protein is expressed Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0553
-
 ATP pH 7.5, in presence of 1 mM Co2+ Mycobacterium tuberculosis
0.08
-
 ATP pH 7.5, in presence of 1 mM Mg2+ Mycobacterium tuberculosis
0.086
-
 ATP pH 7.5, in presence of 1 mM Mn2+ Mycobacterium tuberculosis
0.128
-
 ATP pH 7.5, in presence of 1 mM Ni2+ Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ supports activity similar to that with Mg2+ Mycobacterium tuberculosis
MgCl2 required, optimal concentration: 5 mM Mycobacterium tuberculosis
Mn2+ supports ATPase activity with 2fold lower efficiency compared to Mg2+ Mycobacterium tuberculosis
NaCl optimal concentration: 50 mM Mycobacterium tuberculosis
Ni2+ supports ATPase activity with 3fold lower efficiency compared to Mg2+ Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
85000
-
 sedimentation equilibrium ultracentrifugation Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WMP9
-
-
Mycobacterium tuberculosis H37Rv P9WMP9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant histidine-tagged form of the protein Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks Mycobacterium tuberculosis ADP + phosphate
-
 ?
ATP + H2O only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks Mycobacterium tuberculosis H37Rv ADP + phosphate
-
 ?
dATP + H2O only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks Mycobacterium tuberculosis dADP + phosphate
-
 ?
dATP + H2O only ATP and dATP support helicase activity. 80% of the duplex is separated in the presence of 1 mM ATP in a 15 min reaction, 58% is unwound in the presence of 1 mM dATP. ATPase activity is dependent upon the presence of DNA. Oligonucleotides of 4 nucleotides are sufficient to promote the ATPase activity. UvrD preferentially unwinds 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein has a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides is required for effective unwinding. UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks Mycobacterium tuberculosis H37Rv dADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 85000, the lack of cooperativity observed for both the ATPase and helicase activities lends support to the view that UvrD monomers are the functional unit Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
UvrD
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.1
-
 ATP pH 7.5, in presence of 1 mM Ni2+ Mycobacterium tuberculosis
19.8
-
 ATP pH 7.5, in presence of 1 mM Mn2+ Mycobacterium tuberculosis
22.2
-
 ATP pH 7.5, in presence of 1 mM Co2+ Mycobacterium tuberculosis
29.8
-
 ATP pH 7.5, in presence of 1 mM Mg2+ Mycobacterium tuberculosis