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
-
3.4.11.24
-
aeromonas
-
calcium-activated
-
proteolytica
-
aminopeptidases
-
phosphonate
-
double-zinc
-
aminolysis
-
septatus
-
zinc-bound
-
amino-terminus
-
biotechnology
-
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
Advanced search results
Reaction
Reaction on EC 3.4.11.24 - aminopeptidase S
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
-
-
-
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic mechanism, Asp160, Met161, Gly201, Arg202, and Phe219 are involved, active site structure, modeling of enzyme-substrate complex
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic mechanism, high preference towards large hydrophobic amino terminus residues, active site structure, Glu131 is involved in the catalytic mechanism, enzyme-substrate and enzyme-product complex modeling
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
hydrolyses peptide bonds formed by terminal hydrophobic amino acids such as leucine, methionine, and phenylalanine
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
M161 is involved in substrate binding at the active site cleft
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
preference for hydrophobic residues at the ultimate and the penultimate positions, D-amino acids at these positions reduce the activity, activity is not restricted by the length of substrate chains
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic pathway and reaction mechanism, catalytic residues are Glu131 and Tyr246, Tyr246 is involved in stabilization of the reaction transition state intermediate, also residue Glu151 is involved
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
raction mechanism, catalytic residues are Glu131 and Tyr246, residues Arg202 and Asp160 stabilize the reaction intermediate together with Glu131
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
structure and reaction mechanism
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
the enzyme prefers large hydrophobic aminoterminal residues, Glu131, Asp160, and Arg202 are involved in binding of the N-terminal substrate amino acid, substrate binding and reaction mechanism, tetrahedral reaction intermediate, modelling of the enzyme-substrate and enzyme-product complexes
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
catalytic reaction mechanism, a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5, involvement of a zinc-bound hydroxide as the reaction nucleophile, Tyr246 polarizes the carbonyl carbon and stabilizes the transition state, enzyme-substrate interaction, overview
-
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
structure and reaction mechanism
-
-