Literature summary for 3.4.11.4 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.

Search for more literature for 3.4.11.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
C25S	mutant enzyme shows no loss or decrease of enzymatic activity	Bacillus subtilis
DELTA1-119	inactive mutant enzyme	Bacillus subtilis
DELTA1-159	inactive mutant enzyme	Bacillus subtilis
DELTA1-208	inactive mutant enzyme	Bacillus subtilis
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
DELTA211-410	inactive mutant enzyme	Bacillus subtilis
DELTA271-410	inactive mutant enzyme	Bacillus subtilis
DELTA291-410	inactive mutant enzyme	Bacillus subtilis
DELTA361-410	inactive mutant enzyme	Bacillus subtilis

General Stability

General Stability	Organism
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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	activates, half-maximal activity at 1700 nM	Bacillus subtilis
Mn2+	activates	Bacillus subtilis
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

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bacillus subtilis

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
PepT	-	Bacillus subtilis

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)