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Literature summary for 3.1.1.29 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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
C166A site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis
C67S site-directed mutagenesis, the mutant effectively complements the enzyme-defective thermosensitive Escherichia coli mutant strain AA7852 for growth at 42°C Mycobacterium tuberculosis
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
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
H22N site-directed mutagenesis, the mutation affects the enzyme structure, overview Mycobacterium tuberculosis
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

General Stability Organism
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]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 21978, sequence calculation Mycobacterium tuberculosis
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

Synonyms Comment Organism
peptidyl-tRNA hydrolase
-
Mycobacterium tuberculosis
PTH
-
Mycobacterium tuberculosis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
52
-
stable up to Mycobacterium tuberculosis

Turnover Number [1/s]

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