Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.19.5: beta-aspartyl-peptidase

This is an abbreviated version!
For detailed information about beta-aspartyl-peptidase, go to the full flat file.

Word Map on EC 3.4.19.5

Reaction

Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide =

Synonyms

ASNase3, asparaginase, asparaginase-like protein 1, asparagine beta-amidohydrolase, ASRGL1, beta-aspartyl dipeptidase, beta-aspartyl peptidase, CpsIadA, dipeptidase, beta-aspartyl, EC 3.4.13.10, EcAIII, hASRGL1, IAD, isoaspartyl aminopeptidase, isoaspartyl aminopeptidase/asparaginase, isoaspartyl dipeptidase, isoaspartyl peptidase, isoaspartyl peptidase/L-asparaginase, LlA, Ntn-hydrolase, potassium-independent asparaginase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.5 beta-aspartyl-peptidase

Engineering

Engineering on EC 3.4.19.5 - beta-aspartyl-peptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E166A
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
E166K
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
E80Q
the mutant has no catalytic activity toward beta-Asp-Leu, but its CD spectra and denaturation temperature are similar to wild-type, indicating that this mutation affects catalytic activity but not the overall folding and integrity of the enzyme
Y140F
the mutant has a significant reduction rate of catalysis confirming that this tyrosine residue is important for enzymatic catalysis. It shows less than 10% catalytic activity toward beta-Asp-Leu and the CD spectrum is not significantly different to the wild-type enzyme. Unlike the wild-type enzyme and the other mutants Y140F has a tendency to aggregate during purification and storage, but soluble Y140F is the most thermally stable
E166A
-
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
-
E166K
-
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
-
E80Q
-
the mutant has no catalytic activity toward beta-Asp-Leu, but its CD spectra and denaturation temperature are similar to wild-type, indicating that this mutation affects catalytic activity but not the overall folding and integrity of the enzyme
-
Y140F
-
the mutant has a significant reduction rate of catalysis confirming that this tyrosine residue is important for enzymatic catalysis. It shows less than 10% catalytic activity toward beta-Asp-Leu and the CD spectrum is not significantly different to the wild-type enzyme. Unlike the wild-type enzyme and the other mutants Y140F has a tendency to aggregate during purification and storage, but soluble Y140F is the most thermally stable
-
D285A
kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value
D285N
kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value
E77D
kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value
E77Q
kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value
R169K
kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value
R169M
kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value
R233K
kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value
R233M
kcat/Km for beta-Asp-Leu is 170fold lower than wild-type value
S289A
kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value
T179A
does not undergo autoprocessing
Y137A
kcat/Km for beta-Asp-Leu is 927fold lower than wild-type value
Y137F
kcat/Km for beta-Asp-Leu is 850fold lower than wild-type value
T168A
mutant does not show enzymatic activity