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
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3.4.19.5
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asrgl1s
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asparaginases
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plant-type
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autoproteolytic
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circularly
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acylases
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autoprocessing
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glycosylasparaginases
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dihydroorotases
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medicine
- 3.4.19.5
- asrgl1s
- asparaginases
-
plant-type
-
autoproteolytic
-
circularly
- acylases
-
autoprocessing
- glycosylasparaginases
- dihydroorotases
- medicine
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
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Engineering
Engineering on EC 3.4.19.5 - beta-aspartyl-peptidase
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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
Colwellia psychrerythraea ATCC BAA-681
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the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
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E166K
Colwellia psychrerythraea ATCC BAA-681
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the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
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E80Q
Colwellia psychrerythraea ATCC BAA-681
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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
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Y140F
Colwellia psychrerythraea ATCC BAA-681
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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
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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
R169M
kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value
S289A
kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value