Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.16 neurolysin

Engineering

Engineering on EC 3.4.24.16 - neurolysin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
606A
-
a cleavage site mutant with altered substrate specificity
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
E502A
-
complete loss of enzymatic activity
G608A
-
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
H473A
-
complete loss of enzymatic activity
H474A
-
complete loss of enzymatic activity
H477A
-
complete loss of enzymatic activity
R470E/T499R
-
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
-
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
-
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