3.4.21.111: aqualysin 1
This is an abbreviated version!
For detailed information about aqualysin 1, go to the full flat file.
Word Map on EC 3.4.21.111
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3.4.21.111
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thermus
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aquaticus
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subtilisin-type
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proteinase
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vibrio
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pro-sequence
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subtilisin-like
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subtilisins
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vpr
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cooh-terminal
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heat-stable
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psychrotrophic
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psychrophilic
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subtilase
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p-nitroanilides
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baking
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bake
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subtilisin-related
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food industry
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biotechnology
- 3.4.21.111
- thermus
- aquaticus
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subtilisin-type
- proteinase
- vibrio
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pro-sequence
-
subtilisin-like
- subtilisins
- vpr
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cooh-terminal
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heat-stable
-
psychrotrophic
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psychrophilic
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subtilase
- p-nitroanilides
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baking
-
bake
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subtilisin-related
- food industry
- biotechnology
Reaction
exhibits low specificity towards esters of amino acids with small hydrophobic or aromatic residues at the P1 position =
Synonyms
Aq1, AQN, aqualysin I, S08.051
ECTree
3.4.21.111 aqualysin 1Advanced search results
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results (Engineering
Engineering on EC 3.4.21.111 - aqualysin 1
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C194S
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6% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
C99S
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69% of wild type activity at 40°C, almost as stable as the wild type enzyme, similar secondary structure as the wild type enzyme
C99S/C194S
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3% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
D17N
site-sirected mutagenesis, the mutant is less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis
D183N
site-sirected mutagenesis, the disruption of a salt bridge common to proteinase K subfamily enzymes in the D183N mutant results in a significant reduction in thermal stability, and a massive change in the content of the secondary structure compared to the wild-type enzyme
D212N
site-sirected mutagenesis, thermal stability of D212N is similar to that of the wild-type enzyme at 70°C, but it is inactivated rapidly at 80°C, the mutant is more prone to unfolding at 80°C than the wild-type enzyme
E237Q
site-sirected mutagenesis, the mutant is less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis. Disruption of a salt bridge in E237Q results in a rapid decrease of activity during incubation at 70°C and 80°C
G101A
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catalytic efficiencies for bulky amino acid residues in P2 site such as valine and lucine drastically decreased
G131D
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reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
G131H
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reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
G131K
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reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
P240N
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no effect on the specific activity, almost no effect on the thermostability of the protein
P268T
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no effect on the specific activity, mutation reduces the thermostability of the protein
P5N
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no effect on the specific activity, mutation reduces the thermostability of the protein
P7I
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no effect on the specific activity mutation strongly reduces the thermostability of the protein
S102E
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reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
S102H
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reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
S102K
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reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
C194S
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6% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
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C99S
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69% of wild type activity at 40°C, almost as stable as the wild type enzyme, similar secondary structure as the wild type enzyme
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C99S/C194S
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3% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
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D17N
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site-sirected mutagenesis, the mutant is less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis
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D183N
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site-sirected mutagenesis, the disruption of a salt bridge common to proteinase K subfamily enzymes in the D183N mutant results in a significant reduction in thermal stability, and a massive change in the content of the secondary structure compared to the wild-type enzyme
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P240N
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no effect on the specific activity, almost no effect on the thermostability of the protein
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P268T
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no effect on the specific activity, mutation reduces the thermostability of the protein
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P5N
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no effect on the specific activity, mutation reduces the thermostability of the protein
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P7I
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no effect on the specific activity mutation strongly reduces the thermostability of the protein
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additional information
additional information
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when the structure of VPR, a subtilisin-like protease isolated from Vibrio-strain PA44, is compared to a homology model of the more closely related aqualysin I a putative salt bridge between Asp17 and Arg259 is identified in the thermophilic protein, but not in VPR which has Asn15 and Lys257 in corresponding sites
additional information
amino acid residues participating in salt bridges common to proteinase K subfamily members and intrinsic to the enzyme are replaced to disrupt the bridges one at a time
additional information
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amino acid residues participating in salt bridges common to proteinase K subfamily members and intrinsic to the enzyme are replaced to disrupt the bridges one at a time
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