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Literature summary 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

Cloned(Commentary)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.2.4 0.0553
-
 ATP pH 7.5, in presence of 1 mM Co2+ Mycobacterium tuberculosis
5.6.2.4 0.08
-
 ATP pH 7.5, in presence of 1 mM Mg2+ Mycobacterium tuberculosis
5.6.2.4 0.086
-
 ATP pH 7.5, in presence of 1 mM Mn2+ Mycobacterium tuberculosis
5.6.2.4 0.128
-
 ATP pH 7.5, in presence of 1 mM Ni2+ Mycobacterium tuberculosis

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.6.2.4 85000
-
 sedimentation equilibrium ultracentrifugation Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
5.6.2.4 Mycobacterium tuberculosis P9WMP9
-
-
5.6.2.4 Mycobacterium tuberculosis H37Rv P9WMP9
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.4 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
-
 ?
5.6.2.4 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
-
 ?
5.6.2.4 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
-
 ?
5.6.2.4 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

EC Number Subunits Comment Organism
5.6.2.4 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

EC Number Synonyms Comment Organism
5.6.2.4 UvrD
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.2.4 37
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6.2.4 13.1
-
 ATP pH 7.5, in presence of 1 mM Ni2+ Mycobacterium tuberculosis
5.6.2.4 19.8
-
 ATP pH 7.5, in presence of 1 mM Mn2+ Mycobacterium tuberculosis
5.6.2.4 22.2
-
 ATP pH 7.5, in presence of 1 mM Co2+ Mycobacterium tuberculosis
5.6.2.4 29.8
-
 ATP pH 7.5, in presence of 1 mM Mg2+ Mycobacterium tuberculosis