3.4.11.24: aminopeptidase S
This is an abbreviated version!
For detailed information about aminopeptidase S, go to the full flat file.
Word Map on EC 3.4.11.24
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3.4.11.24
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aeromonas
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calcium-activated
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proteolytica
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aminopeptidases
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phosphonate
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double-zinc
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aminolysis
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septatus
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zinc-bound
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amino-terminus
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biotechnology
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analysis
- 3.4.11.24
- aeromonas
-
calcium-activated
- proteolytica
- aminopeptidases
- phosphonate
-
double-zinc
-
aminolysis
- septatus
-
zinc-bound
-
amino-terminus
- biotechnology
- analysis
Reaction
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues =
Synonyms
aminolysin-S, aminopeptidase S, aminopeptidase yscCo-II, AmpS, AP, APCo-II, bacterial leucine aminopeptidase, dinuclear aminopeptidase, dizinc aminopeptidase, double-zinc aminopeptidase, leucine aminopeptidase, M28.003, S9 aminopeptidase, S9AP-St, SAP, SGAP, SGAPase, SSAP, Streptomyces aminopeptidase, Streptomyces dinuclear aminopeptidase, Streptomyces griseus aminopeptidase, Streptomyces griseus leucine aminopeptidase, transaminopeptidase
ECTree
3.4.11.24 aminopeptidase SAdvanced search results
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results (Engineering
Engineering on EC 3.4.11.24 - aminopeptidase S
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D3A/D262G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E131
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E131D
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a general acid-base mutant, thermodynamic parameters for the reaction are similar to the wild-type enzyme, but the kcat of the mutant is 4fold reduced, while the activation energy is elevated compared to the wild-type enzyme
E196A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y246
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site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
F221A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F221G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F221S
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F221A
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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F221G
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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F221S
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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S502C
additional information
S502C
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mutant without aminopeptidase activity but with peptide synthesis activity
S502C
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mutant without aminopeptidase activity but with peptide synthesis activity
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additional information
construction of chimeric enzymes from the enzymes of Streptomyces griseus and Streptomyces septatus by DNA in vivo shuffling and site-directed mutagenesis for calcium activation and binding studies, overview
additional information
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construction of chimeric enzymes from the enzymes of Streptomyces griseus and Streptomyces septatus by DNA in vivo shuffling and site-directed mutagenesis for calcium activation and binding studies, overview
additional information
alteration of leucine aminopeptidase to phenylalanine aminopeptidase by site-directed mutagenesis
additional information
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alteration of leucine aminopeptidase to phenylalanine aminopeptidase by site-directed mutagenesis
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