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Literature summary extracted from

  • Bal, N.C.; Agrawal, H.; Meher, A.K.; Arora, A.
    Characterization of peptidyl-tRNA hydrolase encoded by open reading frame Rv1014c of Mycobacterium tuberculosis H37Rv (2007), Biol. Chem., 388, 467-479.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.29 gene pth, orf Rv1014c, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant C-terminally His-tagged enzymes in Escherichia coli strain BL21(DE3) and in Escherichia coli thermosensitive strain AA7852, the mutant strain is able to grow at the nonpermissive temperature of 42°C, at 39°C, overexpression of MtPth in AA7852 cells allowed the cells to remain viable in the presence of up to 200 mg/ml erythromycin, overview Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.29 C166A site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis
3.1.1.29 C67S site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis
3.1.1.29 D95N site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis
3.1.1.29 H22N site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis
3.1.1.29 H22N site-directed mutagenesis, the mutation affects the enzyme structure, overview Mycobacterium tuberculosis
3.1.1.29 N12D site-directed mutagenesis, the catalytic residue mutant is not able to complement the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis

General Stability

EC Number General Stability Organism
3.1.1.29 urea/guanidinium chloride-induced unfolding curve for MtPth indicates a simple two-state unfolding process without any intermediates, pH 6.5, 25°C Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.29 additional information
-
additional information Michaelis-Menten kinetics Mycobacterium tuberculosis
3.1.1.29 0.0007
-
diacetyl-lysyl-tRNALys
-
Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.29 21978
-
x * 21978, sequence calculation Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.29 diacetyl-lysyl-tRNALys + H2O Mycobacterium tuberculosis
-
diacetyl-lysine + tRNALys
-
?
3.1.1.29 diacetyl-lysyl-tRNALys + H2O Mycobacterium tuberculosis H37Rv
-
diacetyl-lysine + tRNALys
-
?
3.1.1.29 additional information Mycobacterium tuberculosis the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria ?
-
?
3.1.1.29 additional information Mycobacterium tuberculosis H37Rv the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.29 Mycobacterium tuberculosis
-
gene pth, orf Rv1014c
-
3.1.1.29 Mycobacterium tuberculosis H37Rv
-
gene pth, orf Rv1014c
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.29 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.29 diacetyl-lysyl-tRNALys + H2O
-
Mycobacterium tuberculosis diacetyl-lysine + tRNALys
-
?
3.1.1.29 diacetyl-lysyl-tRNALys + H2O
-
Mycobacterium tuberculosis H37Rv diacetyl-lysine + tRNALys
-
?
3.1.1.29 additional information the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria Mycobacterium tuberculosis ?
-
?
3.1.1.29 additional information the enzyme and its conserved active-site residues N12, H22 and D95 are essential for the viability of the bacteria Mycobacterium tuberculosis H37Rv ?
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.29 ? x * 21978, sequence calculation Mycobacterium tuberculosis
3.1.1.29 More 3D fold based on NMR and a structural model based on the Escherichia coli Pth crystal structure are generated for Mycobacterium tuberculosis Pth, structure comparison, molecular modeling, construction of a model of structural changes associated with enzyme action on the basis of the plasticity of the molecule, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
3.1.1.29 peptidyl-tRNA hydrolase
-
Mycobacterium tuberculosis
3.1.1.29 PTH
-
Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.29 additional information
-
thermally-induced unfolding curve for MtPth indicates a simple two-state unfolding process without any intermediates, thermodynamic stability of the enzyme, pH 6.5, 25°C, overview Mycobacterium tuberculosis
3.1.1.29 52
-
stable up to Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.29 1.22
-
diacetyl-lysyl-tRNALys
-
Mycobacterium tuberculosis