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Literature summary extracted from

  • Cha, M.H.; Yong, W.M.; Lee, S.M.; Lee, Y.S.; Chung, I.Y.
    The biochemical and molecular characterization of recombinant Bacillus subtilis tripeptidase (PepT) as a zinc-dependent metalloenzyme (2000), Mol. Cells, 10, 423-431.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.4 expression in Escherichia coli Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.4 C25S mutant enzyme shows no loss or decrease of enzymatic activity Bacillus subtilis
3.4.11.4 DELTA1-119 inactive mutant enzyme Bacillus subtilis
3.4.11.4 DELTA1-159 inactive mutant enzyme Bacillus subtilis
3.4.11.4 DELTA1-208 inactive mutant enzyme Bacillus subtilis
3.4.11.4 DELTA1-66 mutant enzyme requires a concentration of Zn2+ ion at least ten-fold higher to reach maximal activity without significantly affecting kinetic parameters such as Km and Vmax compared to the full length tripeptidase Bacillus subtilis
3.4.11.4 DELTA211-410 inactive mutant enzyme Bacillus subtilis
3.4.11.4 DELTA271-410 inactive mutant enzyme Bacillus subtilis
3.4.11.4 DELTA291-410 inactive mutant enzyme Bacillus subtilis
3.4.11.4 DELTA361-410 inactive mutant enzyme Bacillus subtilis

General Stability

EC Number General Stability Organism
3.4.11.4 denaturation by guanidine hydrochloride at room temperature. Zn2+ makes the enzyme become much more refractory to the denaturing effect of guanidine hydrochloride than Co2+ Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.4 EDTA 0.1 mM, 90% inhibition Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.4 3.3
-
 Met-Ala-Ser pH 7.4, 55°C, in presence of 0.004 mM Zn2+ Bacillus subtilis
3.4.11.4 3.5
-
 Met-Ala-Ser pH 7.4, 55°C, in presence of 0.004 mM Co2+ Bacillus subtilis
3.4.11.4 5.1
-
 Met-Ala-Ser pH 7.4, 55°C, without metal Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.4 Co2+ activates, half-maximal activity at 1700 nM Bacillus subtilis
3.4.11.4 Mn2+ activates Bacillus subtilis
3.4.11.4 Zn2+ activates, half-maximal activity at 650 nM. The enzyme is likely to be a Zn2+-dependent metalloenzyme, N-terminal region stabilizes Zn2+-binding. Atomic absorption spectroscopy reveals 0.26 atoms of Zn2+ per molecule. When the enzyme is denatured with 6 M guanidine hydrochloride and refolded in the presence of 4 mM Zn2+, it contains 0.53 atoms of Zn2+ per molecule with 1.5fold increase in activity Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.4 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.4
-
 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.4 Met-Ala-Ser + H2O
-
 Bacillus subtilis Met + Ala-Ser
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.4 PepT
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.4 additional information
-
 additional information
-
 Bacillus subtilis