3.4.24.16: neurolysin
This is an abbreviated version!
For detailed information about neurolysin, go to the full flat file.
Word Map on EC 3.4.24.16
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3.4.24.16
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bradykinin
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metallopeptidase
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metalloendopeptidase
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dynorphins
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pro-ile
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neuropeptidase
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pro10-tyr11
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neuromedin
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hemopressins
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arg8-arg9
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non-at2
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neurotensin-degrading
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molecular biology
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pharmacology
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medicine
- 3.4.24.16
- bradykinin
- metallopeptidase
- metalloendopeptidase
- dynorphins
- pro-ile
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neuropeptidase
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pro10-tyr11
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neuromedin
- hemopressins
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arg8-arg9
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non-at2
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neurotensin-degrading
- molecular biology
- pharmacology
- medicine
Reaction
Preferential cleavage in neurotensin: Pro10-/-Tyr =
Synonyms
endopeptidase 24.16, endopeptidase 24.16B, endopeptidase 3.4.24.16, EP 24.16, ep24.16, EP24.16c, EP24.16m, MEP, Microsomal endopeptidase, mitochondrial peptidase, MOP, More, NEL, neurolisin, neurolysin, neurotensin endopeptidase, neurotensin-cleaving enzyme, Nln, oligopeptidase M, peptidase, neurotensin endo, peptidase, neurotensin endo-, SABP, soluble angiotensin II-binding protein, Soluble angiotensin-binding protein, thimet oligopeptidase II, thimet peptidase II
ECTree
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Engineering
Engineering on EC 3.4.24.16 - neurolysin
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E475Q
site-directed mutagenesis, the residue Glu475 coordinates a water molecule involved in the nucleophilic attack of the scissile bond and replacing this residue with glutamine (hNLNE475Q) results in a dramatic reduction of enzyme activity
E475A
site-directed mutagenesis, mutation of the catalytic glutamate residue, a catalytically compromised enzyme mutant that sediments more rapidly in the presence of saturating amounts of the dynorphin A(1-8) substrate compared to the wild-type enzyme
G608A
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site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
H160A
site-directed mutagenesis, mutation of a surface histidine involved in a divalent cation-mediated lattice contact in the original neurolysin crystals
R470E/T499R
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site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves neurolysin sites, overview
Y606A
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site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
Y606F
Y610L
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marked change in substrate specificity with 3fold higher binding efficiency to matrix metalloproteinase MMP-2/9 substrate (7-methoxy-coumarin-4-yl)acetyl-RPKPYA-Nva-WMK(2,4-dinitrophenyl)-NH2 with glutamic acid at the P2' amino acid position
additional information
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site-directed mutagenesis, the mutation does not affect the overall fold of the protein, the mutant shows altered substrate specificity and kinetics with fluorogenic peptide substrates compared to the wild-type enzyme
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dominant-negative G protein mutants used to selectively disrupt Gialpha- and Gbetagamma-mediated signaling pathways attenuated strain-dependent increases for the enzyme