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Literature summary for 3.4.21.53 extracted from

  • Lin, Y.C.; Lee, H.C.; Wang, I.; Hsu, C.H.; Liao, J.H.; Lee, A.Y.; Chen, C.; Wu, S.H.
    DNA-binding specificity of the Lon protease alpha-domain from Brevibacillus thermoruber WR-249 (2009), Biochem. Biophys. Res. Commun., 388, 62-66.
    View publication on PubMed
Search for more literature for 3.4.21.53

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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-
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Brevibacillus thermoruber
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 WR-249
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Brevibacillus thermoruber WR-249
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 WR-249
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Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Bacillus subtilis ?
-
 ?
additional information the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Escherichia coli ?
-
 ?
additional information the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Brevibacillus thermoruber ?
-
 ?
additional information the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Brevibacillus thermoruber WR-249 ?
-
 ?

General Information

General Information Comment Organism
physiological function the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Bacillus subtilis
physiological function the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Escherichia coli
physiological function the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence Brevibacillus thermoruber