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(Ala)n 4-nitroanilide + H2O
?
-
n: 1,2,3
-
-
?
2-aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Gly-Pro-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Hyp-Gly-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Ala + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage sites: Gly-Ala and Ala-Ser
major products
?
2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Glu + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Lys + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Lys-Ser
-
?
2-aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Ile-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
best of fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser
-
?
Abz-YEFDGKSMQGDDPNK-2,4-dinitrophenyl + H2O
Abz-YEFDGKSMQG + DDPNK-2,4-dinitrophenyl
-
Dentin sialophosphoprotein (Dpp) cleavage site, designated Dspp-FRET
-
-
?
Acetyl-Ala-Ala-Ala methylester + H2O
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Arg-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Lys-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Phe-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ser-Pro-Phe-Arg
-
i.e. nitrobradykinin, chromogenic bradykinin analog
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
bradykinin 1-7 RPPGFSP + H2O
?
partial digestion
-
?
casein + H2O
hydrolyzed casein
Collagen IV + H2O
?
-
-
-
-
?
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Ala-Ala-Arg + Ala-Pro-Leu-Val
Dansyl-Arg-Ala-Pro-Leu + H2O
Dansyl-Arg + Ala-Pro-Leu
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Pro-Leu-Gly
Dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Ser-Leu-Gly
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Gly-Arg + Ala-Pro-Trp-Val
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Leu-Val
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Trp-Val
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Asn + Ala-Pro-Leu-Val
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Tyr + Ala-Pro-Trp-Val
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Pro-Arg + Ala-Pro-Leu-Val
Dansyl-His-His-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-His-His-Leu-Lys-Arg + Ala-Pro-Trp-Val
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Pro-Leu-Gly
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Ser-Leu-Gly
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu-Val
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Trp-Val
Dansyl-Leu-Lys-Arg-Leu-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Leu-Pro-Trp-Val
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Asn + Ala-Pro-Leu-Val
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Lys + Ala-Pro-Trp-Val
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Tyr + Ala-Pro-Trp-Val
Dansyl-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Lys-Arg + Ala-Pro-Leu
Dansyl-Lys-Glu-Thr-Tyr-Ser-Lys + H2O
?
-
poor substrate
-
-
?
Dansyl-Lys-Glu-Thr-Tyr-Ser-Phe + H2O
?
-
poor substrate
-
-
?
Dansyl-Pro-Gln-Gly-Ile-Ala-Gly-(D)-Arg + H2O
?
-
poor substrate
-
-
?
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Pro-Lys-Arg + Ala-Pro-Trp-Val
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Val-Lys-Arg + Ala-Pro-Trp-Val
denatured chains of alpha-tubulin + H2O
hydrolyzed alpha-tubulin chains
denatured chains of beta-tubulin + H2O
hydrolyzed beta-tubulin chains
denatured tubulin + H2O
hydrolyzed tubulin
-
cleavage pattern
-
?
Des-Arg-bradykinin PPGFSPFR + H2O
?
complete digestion
-
?
Fibronectin + H2O
?
-
-
-
-
?
laminin I + H2O
?
-
-
-
-
?
laminin I/nidogen I complex + H2O
?
-
-
-
-
?
Lys-bradykinin KRPPGFSPFR + H2O
?
complete digestion
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
PRPKPQQFFGLM-NH2 + H2O
?
complete digestion
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
Succinyl-(Ala)n 4-nitroanilide + H2O
?
-
n: 2,3,5
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
Succinyl-Ala-Ala-Phe 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ala-Pro 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ala-Val 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Ala-Pro-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
Succinyl-Pro-Ala-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
from calf skin
-
-
?
additional information
?
-
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg
-
-
-
-
?
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Leu-Ser
-
?
Acetyl-Ala-Ala-Ala methylester + H2O
?
-
-
-
-
?
Acetyl-Ala-Ala-Ala methylester + H2O
?
-
-
-
-
?
Acetyl-Ala-Ala-Ala methylester + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
casein + H2O
hydrolyzed casein
-
heat-denatured form
-
-
?
casein + H2O
hydrolyzed casein
-
heat-denatured form
-
?
casein + H2O
hydrolyzed casein
-
heat-denatured form
-
?
casein + H2O
hydrolyzed casein
-
heat-denatured form
-
?
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Ala-Ala-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Ala-Ala-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Arg-Ala-Pro-Leu + H2O
Dansyl-Arg + Ala-Pro-Leu
-
cleavage site: Arg-Ala
-
?
Dansyl-Arg-Ala-Pro-Leu + H2O
Dansyl-Arg + Ala-Pro-Leu
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Pro-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Pro-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Ser-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Ser-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Gly-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Gly-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Asn + Ala-Pro-Leu-Val
-
cleavage site: Asn-Ala
-
?
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Asn + Ala-Pro-Leu-Val
-
cleavage site: Asn-Ala
-
?
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Tyr + Ala-Pro-Trp-Val
-
cleavage site: Tyr-Ala
-
?
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Tyr + Ala-Pro-Trp-Val
-
cleavage site: Tyr-Ala
-
?
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Pro-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Pro-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-His-His-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-His-His-Leu-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-His-His-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-His-His-Leu-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Pro-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Pro-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Ser-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Ser-Leu-Gly
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala, poor substrate
-
?
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala, poor substrate
-
?
Dansyl-Leu-Lys-Arg-Leu-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Leu-Pro-Trp-Val
-
cleavage site: Arg-Leu, poor substrate
-
-
?
Dansyl-Leu-Lys-Arg-Leu-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Leu-Pro-Trp-Val
-
cleavage site: Arg-Leu, poor substrate
-
?
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Asn + Ala-Pro-Leu-Val
-
cleavage site: Asn-Ala
-
?
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Asn + Ala-Pro-Leu-Val
-
cleavage site: Asn-Ala
-
?
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Lys + Ala-Pro-Trp-Val
-
cleavage site: Lys-Ala
-
?
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Lys + Ala-Pro-Trp-Val
-
cleavage site: Lys-Ala
-
?
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Tyr + Ala-Pro-Trp-Val
-
cleavage site: Tyr-Ala
-
?
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Tyr + Ala-Pro-Trp-Val
-
cleavage site: Tyr-Ala
-
?
Dansyl-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Lys-Arg + Ala-Pro-Leu
-
cleavage site: Arg-Ala
-
?
Dansyl-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Lys-Arg + Ala-Pro-Leu
-
cleavage site: Arg-Ala
-
?
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Pro-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Pro-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Val-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Val-Lys-Arg + Ala-Pro-Trp-Val
-
cleavage site: Arg-Ala
-
?
denatured chains of alpha-tubulin + H2O
hydrolyzed alpha-tubulin chains
-
tubulin chains are cleaved only in the denatured state
-
-
?
denatured chains of alpha-tubulin + H2O
hydrolyzed alpha-tubulin chains
-
cleavage sites, overview
-
?
denatured chains of beta-tubulin + H2O
hydrolyzed beta-tubulin chains
-
tubulin chains are cleaved only in the denatured state
-
-
?
denatured chains of beta-tubulin + H2O
hydrolyzed beta-tubulin chains
-
cleavage sites, overview
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
maturation
-
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
cleavage of the C-terminal pro-domain
-
-
?
SQT-3 + H2O
?
-
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
D5FM33
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
D5FM33
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
-
i.e. STANA, poor substrate
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
cleavage specificity, putative substrate binding region and mechanism
-
-
?
additional information
?
-
-
No hydrolysis of dansyl-Gly-Gly-Phe-Ala-Gly, dansyl-Phe-Leu-Ala, dansyl-Pro-Ala-Gly, dansyl-Ala-Phe-Phe-Ala, dansyl-Ala-Ala-Phe-Ala, dansyl-Gly-Gly-Phe-Ala, dansyl-Ala-Phe-Leu-Ala, dansyl-Pro-Leu-Gly-Ile-Ala-Gly-(D)-Arg, carbobenzoxy-Gly-Pro-Gly-Gly-Ala-NH2
-
-
?
additional information
?
-
-
No hydrolysis of Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg, Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg, Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg, Arg-Pro-Pro-Gly-(4-nitro)Phe-Glu-Pro-Phe-Arg
-
-
?
additional information
?
-
-
No hydrolysis of carbobenzoxy-Ala-Ala, Nalpha-benzoyl-DL-Arg 2-naphthylamide (i.e. BANA), benzoyl-L-arginine ethyl ester, N-acetyl-L-tyrosine ethyl ester, Leu-Trp-Met-Arg-Phe-Ala, Gly-Pro-Gly-Gly-Pro-Ala
-
-
?
additional information
?
-
-
hydrolyzes peptide bonds on the amino side of the small uncharged residues Ala, Thr, Ser, Gly and Val
-
-
?
additional information
?
-
optimal astacin substrates comprise at least five amino acids with small aliphatic residues in P'1, proline in P'2, bulky hydrophobic residues in P'3, and basic residues in P1 and P2
-
-
?
additional information
?
-
-
optimal astacin substrates comprise at least five amino acids with small aliphatic residues in P'1, proline in P'2, bulky hydrophobic residues in P'3, and basic residues in P1 and P2
-
-
?
additional information
?
-
-
No hydrolysis of carbobenzoxy-Ala-Ala, Nalpha-benzoyl-DL-Arg 2-naphthylamide (i.e. BANA), benzoyl-L-arginine ethyl ester, N-acetyl-L-tyrosine ethyl ester, Leu-Trp-Met-Arg-Phe-Ala, Gly-Pro-Gly-Gly-Pro-Ala
-
-
?
additional information
?
-
-
No hydrolysis of carbobenzoxy-Ala-Ala, Nalpha-benzoyl-DL-Arg 2-naphthylamide (i.e. BANA), benzoyl-L-arginine ethyl ester, N-acetyl-L-tyrosine ethyl ester, Leu-Trp-Met-Arg-Phe-Ala, Gly-Pro-Gly-Gly-Pro-Ala
-
-
?
additional information
?
-
tosyl-GPK-NA, Suc-AAPF-NA, Suc-AAPL-NA, Cbz-GGL-NA, bradykinin 1-5, and bradykinin 1-6 are no substrates
-
?
additional information
?
-
-
tosyl-GPK-NA, Suc-AAPF-NA, Suc-AAPL-NA, Cbz-GGL-NA, bradykinin 1-5, and bradykinin 1-6 are no substrates
-
?
additional information
?
-
-
no substrate: alpha-1 and alpha-2 chains of triple-helical collagen I
-
-
?
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Ca2+
activates, a positive regulator of BMP-1
Co2+
-
activation of apoenzyme, can replace Zn2+ as catalytic ion yielding 140% of the activity of the zinc-containing enzyme, pentavalent metal coordination
Cu2+
-
activation of apoenzyme, can replace Zn2+ as catalytic ion yielding 37% of the activity of the zinc-containing enzyme, pentavalent metal coordination
K+
secretion of nephrosin can be stimulated by high concentrations of extracellular potassium
Zn2+
zinc metalloprotease
Zn2+
-
zinc metalloenzyme
Zn2+
-
zinc-binding consensus sequence
Zn2+
-
the catalytically active zinc is located at the bottom of the active-site cleft in the center of the molecule
Zn2+
-
pentavalent metal coordination
Zn2+
-
about 1 mol zinc per mol enzyme, atomic absorption spectroscopy
Zn2+
-
very tightly bound, 40 days half-life for metal dissociation
Zn2+
required for activity
Zn2+
-
zinc endopeptidase
Zn2+
zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft
Zn2+
a zinc metalloprotease
Zn2+
-
zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft
Zn2+
zinc metalloproteinase
Zn2+
-
zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft
Zn2+
zinc metalloproteinase
Zn2+
a zinc-dependent metalloprotease
Zn2+
a zinc metalloproteinase, catalytic zinc ion
Zn2+
a zinc metalloproteinase. Molecular modeling of LALP3 reveals that the isoform contains the zinc binding and Met-turn motifs, forming the active site, as has been observed in astacins. Homology three-dimensional structure modeling and structural analysis of LALP3
Zn2+
-
zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft
Zn2+
a zinc metalloprotease
Zn2+
-
zinc metallopeptidase, the enzyme has a zinc-dependent catalytic domain with an extended zinc-binding motif, HEXXHXXGXXH, as well as three large alpha-helices and a five-stranded beta-sheet, as well as two or three disulfide bonds. The zinc-dependent moieties are divided into an N-terminal and a C-terminal sub-domain by an active-site cleft. The catalytic zinc ion resides at the bottom of the active-site cleft
additional information
-
metal content
additional information
-
no apoenzyme activation by Ni2+ or Hg2+ with their octahedral and tetrahedral coordination
additional information
-
no apoenzyme activation by Ni2+ or Hg2+ with their octahedral and tetrahedral coordination
additional information
-
no other metal than Co2+, Zn2+ or Cu2+ detectable by atomic absorption spectroscopy
additional information
in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion
additional information
-
in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion
additional information
-
in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion
additional information
inhibitor coordinates the catalytic zinc ion via carbonyl oxygen of glycine and O atom of hydroxamic acid
additional information
-
in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion
additional information
-
in mature, unbound astacins, a conserved tyrosine acts as an additional zinc ligand, which is swung out upon substrate or inhibitor binding in a tyrosine switch motion
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1,10-o-phenanthroline
-
1 mM, isoform LAST, 10% residual activity, isoform LAST_MAM, 12% residual activity
3-[3-(1-aminoethenyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
6-cyclohexyl-3-[3-(2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
6-cyclohexyl-3-[3-[4-(dihydroxymethyl)pyridin-2-yl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
6-cyclohexyl-N-hydroxy-3-(3-[1-[(methylsulfonyl)amino]ethenyl]-1,2,4-oxadiazol-5-yl)hexanamide
8-Hydroxyquinoline-5-sulfonic acid
-
r
9-Fluorenylmethoxycarbonyl-Pro-Lys-Phe-PSI(PO2HCH2)-Ala-Pro-Leu-Val
-
-
9-fluorenylmethyloxycarbonyl-KFPCAPLV-OH
-
-
9-fluorenylmethyloxycarbonyl-PKFPCAPLV-OH
-
-
9fluorenylmethyloxycarbonyl-F-PSI[PO2CH2]-APLV-OH
-
-
9fluorenylmethyloxycarbonyl-FPCAPLVOH
-
-
9fluorenylmethyloxycarbonyl-KF-PSI[PO2CH2]-APLV-OH
-
-
9fluorenylmethyloxycarbonyl-PKF-PSI[PO2CH2]-APLV-OH
-
-
Acetyl-Arg-Pro-Gly-Tyr-hydroxamate
-
-
alpha-2-Macroglobulin
-
1 mM, isoform LAST, 1,1% residual activity, isoform LAST_MAM, 42% resiudal activity
-
alpha2-Macroglobulin
-
bovine or Astacus astacus hemolymph, ir
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg
-
nitrobradykinin as substrate
Arg-Pro-Pro-Gly-(4-nitro)Phe-Glu-Pro-Phe-Arg
-
nitrobradykinin as substrate
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg
-
nitrobradykinin as substrate
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg
-
nitrobradykinin as substrate
benzyloxycarbonyl-PKF-PSI[PO2CH2]-AGP-O-methyl
-
-
benzyloxycarbonyl-PKF-PSI[PO2CH2]-AP-O-methyl
-
-
benzyloxycarbonyl-PKF-PSI[PO2CH2]-APL-O-methyl
-
-
benzyloxycarbonyl-PKF-PSI[PO2CH2]-GPL-O-methyl
-
-
benzyloxycarbonyl-PKK-PSI[PO2CH2]-APLV-O-methyl
-
-
benzyloxycarbonyl-Pro-Lys-Phe-PSI[PO2CH2]Ala-Pro-O-methyl
-
-
benzyloxycarbonyl-prolyl-leucylglycyl-hydroxamate
-
1 mM, isoform LAST, 83% residual activity, isoform LAST_MAM, 15.5% resiudal activity
Carbobenzoxy-Phe-PSI(PO2H)-Ala-Pro-Phe-NH2
-
-
Dansyl-Gly-Lys-Arg
-
dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val as substrate
Dansyl-Leu-Lys-Arg
-
dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val as substrate
Diethyldithiocarbamic acid sodium salt
-
Ecballium elaterium Astacus protease inhibitor 1
-
i.e. EEAPI1
-
Ecballium elaterium Astacus protease inhibitor 2
-
i.e. EEAPI2
-
fetiun-like protein
-
the enzyme circulates in the blood stream in complex with a specific protein inhibitor, formerly termed nephrosin inhibitor, which is a homologue of fetuin, a large plasma protein with many functions. Fish fetuin, like its mammalian counterpart fetuin A, contains cystatin-like domains and is related to cystatin C-like inhibitors of cysteine cathepsins
-
fetuin
-
following proteolytic processing in hematopoietic tissues, fetuin serves as an endogenous inhibitor of enzyme
-
fluorenylmethyloxycarbonyl-Pro-Lys-Phe-PSI[PO2CH2]Ala-Pro-Leu-Val
-
-
Hydroxamylsuccinyl-Pro-Phe-Arg
-
-
L-prolyl-L-leucyl-N-hydroxyglycinamide
enzyme binding structure modeling
Potato inhibitor d
-
i.e. PoI-d, astacin inhibitor from potato
-
Tyrosin hydroxamate
-
most effective hydroxamate inhibitor
1,10-phenanthroline
-
r; reactivation of apoenzyme by Zn2+ (100%), Cu2+ (70%) or Co2+ (50%); strong, kinetics
1,10-phenanthroline
-
r; strong, kinetics
1,7-phenanthroline
-
weak
1,7-phenanthroline
-
not reversible by addition of Zn2+
3-[3-(1-aminoethenyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
3-[3-(1-aminoethenyl)-1,2,4-oxadiazol-5-yl]-6-cyclohexyl-N-hydroxyhexanamide
-
6-cyclohexyl-3-[3-(2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
6-cyclohexyl-3-[3-(2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
6-cyclohexyl-3-[3-[4-(dihydroxymethyl)pyridin-2-yl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
6-cyclohexyl-3-[3-[4-(dihydroxymethyl)pyridin-2-yl]-1,2,4-oxadiazol-5-yl]-N-hydroxyhexanamide
-
6-cyclohexyl-N-hydroxy-3-(3-[1-[(methylsulfonyl)amino]ethenyl]-1,2,4-oxadiazol-5-yl)hexanamide
-
6-cyclohexyl-N-hydroxy-3-(3-[1-[(methylsulfonyl)amino]ethenyl]-1,2,4-oxadiazol-5-yl)hexanamide
-
actinonin
-
i.e. 3-[[1-[[2-(hydroxymethyl)-1-pyrolidinyl]carbonyl]-2-methylpropyl]carbamoyl]octano hydroxamic acid, weak, kinetics
actinonin
-
1 mM, isoform LAST, 89% residual activity isoform LAST_MAM, 45% resiudal activity
EDTA
-
r (upon dilution or addition of Zn2+); weak, kinetics, t1/2 of enzyme activity at 5 mM EDTA: 6 days
EDTA
-
r (upon dilution or addition of Zn2+)
EDTA
a common inhibitor of several astacin metalloproteases
EDTA
a common inhibitor of several astacin metalloproteases
additional information
the digestive fluid contains heat-stable serine peptidase inhibitors ranging in molecular mass from about 15 to 32 kDa
-
additional information
-
the digestive fluid contains heat-stable serine peptidase inhibitors ranging in molecular mass from about 15 to 32 kDa
-
additional information
-
most effective inhibitors are hydroxamates with aromatic side chains followed in order of decreasing affinity by those with side chains containing sulfur, acidic or basic groups
-
additional information
-
inhibition study
-
additional information
-
no inhibition by dansyl-Ala-Ala-Arg, Ala-Pro-Leu-Val
-
additional information
-
phosphoramidon or TIMP1 (tissue inhibitor of metalloproteinases)
-
additional information
-
polyvalent bovine pancreas inhibitor, porcine pancreas inhibitor, soybean trypsin inhibitor, lima bean trypsin inhibitor, ovomucoid, alpha1-antitrypsin, hirudin, pepstatin
-
additional information
astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs)
-
additional information
-
polyvalent bovine pancreas inhibitor, porcine pancreas inhibitor, soybean trypsin inhibitor, lima bean trypsin inhibitor, ovomucoid, alpha1-antitrypsin, hirudin, pepstatin
-
additional information
-
astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs)
-
additional information
compounds with a hydroxamate functional group are potent inhibitors causing body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
additional information
-
compounds with a hydroxamate functional group are potent inhibitors causing body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
additional information
-
polyvalent bovine pancreas inhibitor, porcine pancreas inhibitor, soybean trypsin inhibitor, lima bean trypsin inhibitor, ovomucoid, alpha1-antitrypsin, hirudin, pepstatin
-
additional information
little or no inhibition by pestatin, PMSF, and iodoacetate
-
additional information
-
little or no inhibition by pestatin, PMSF, and iodoacetate
-
additional information
-
astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs)
-
additional information
D5FM33
compounds with a hydroxamate functional group are potent inhibitors causing body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
additional information
-
compounds with a hydroxamate functional group are potent inhibitors causing body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
additional information
inhibitor coordinates the catalytic zinc ion via carbonyl oxygen of glycine and O atom of hydroxamic acid
-
additional information
-
astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs)
-
additional information
compounds with a hydroxamate functional group are potent inhibitors causing body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
additional information
-
compounds with a hydroxamate functional group are potent inhibitors causing body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
additional information
-
astacin and other members of the astacin family are not inhibited by tissue inhibitors of metalloproteinases (TIMPs)
-
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Alzheimer Disease
Expression, purification and initial characterization of human meprin ? from Pichia pastoris.
Amnesia
Snake toxins with high selectivity for subtypes of muscarinic acetylcholine receptors.
astacin deficiency
Down-regulation of the liver-derived plasma protein fetuin-B mediates reversible female infertility.
Cholera
The effect of opiates on the intestinal immune response to cholera toxin in mice.
Diabetic Nephropathies
Meprin beta metalloprotease gene polymorphisms associated with diabetic nephropathy in the Pima Indians.
Escherichia coli Infections
Zebrafish nephrosin helps host defence against Escherichia coli infection.
Herpes Zoster
A chromosome-level genome of black rockfish, Sebastes schlegelii, provides insights into the evolution of live birth.
Herpes Zoster
A Primary Evaluation of Potential Small-Molecule Inhibitors of the Astacin Metalloproteinase Ovastacin, a Novel Drug Target in Female Infertility Treatment.
Herpes Zoster
Anchoring cortical granules in the cortex ensures trafficking to the plasma membrane for post-fertilization exocytosis.
Herpes Zoster
Association of high fetuin-B concentrations in serum with fertilization rate in IVF: a cross-sectional pilot study.
Herpes Zoster
BaP exposure causes oocyte meiotic arrest and fertilization failure to weaken female fertility.
Herpes Zoster
Brefeldin A impairs porcine oocyte meiotic maturation via interruption of organelle dynamics.
Herpes Zoster
Down-regulation of the liver-derived plasma protein fetuin-B mediates reversible female infertility.
Herpes Zoster
Dynein promotes porcine oocyte meiotic progression by maintaining cytoskeletal structures and cortical granule arrangement.
Herpes Zoster
Exposure to aristolochic acid I compromises the maturational competency of porcine oocytes via oxidative stress-induced DNA damage.
Herpes Zoster
Glycan-Independent Gamete Recognition Triggers Egg Zinc Sparks and ZP2 Cleavage to Prevent Polyspermy.
Herpes Zoster
Hatching gland development and hatching in zebrafish embryos: A role for zinc and its transporters Zip10 and Znt1a.
Herpes Zoster
Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida.
Herpes Zoster
Limited proteolysis by acrosin affects sperm-binding and mechanical resilience of the mouse zona pellucida.
Herpes Zoster
Mammalian gamete fusion depends on the inhibition of ovastacin by fetuin-B.
Herpes Zoster
Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases.
Herpes Zoster
Melamine Impairs Female Fertility via Suppressing Protein Level of Juno in Mouse Eggs.
Herpes Zoster
Melatonin improves the fertilization ability of post-ovulatory aged mouse oocytes by stabilizing ovastacin and Juno to promote sperm binding and fusion.
Herpes Zoster
Melatonin protects oocyte quality from Bisphenol A-induced deterioration in the mouse.
Herpes Zoster
Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy.
Herpes Zoster
Recombinant fetuin-B protein maintains high fertilization rate in cumulus cell-free mouse oocytes.
Herpes Zoster
The E-modulus of the oocyte is a non-destructive measure of zona pellucida hardening.
Herpes Zoster
The protective role of melatonin in porcine oocyte meiotic failure caused by the exposure to benzo(a)pyrene.
Herpes Zoster
Zinc sparks induce physiochemical changes in the egg zona pellucida that prevent polyspermy.
Infections
Identification and activity of inhibitors of the essential nematode-specific metalloprotease DPY-31.
Infections
Zebrafish nephrosin helps host defence against Escherichia coli infection.
Infertility
A Primary Evaluation of Potential Small-Molecule Inhibitors of the Astacin Metalloproteinase Ovastacin, a Novel Drug Target in Female Infertility Treatment.
Infertility, Female
A Primary Evaluation of Potential Small-Molecule Inhibitors of the Astacin Metalloproteinase Ovastacin, a Novel Drug Target in Female Infertility Treatment.
Inflammatory Bowel Diseases
An integrated in silico approach to understand protein-protein interactions: human meprin-? with fetuin-A.
Inflammatory Bowel Diseases
First insight into structure-activity relationships of selective meprin ? inhibitors.
Inflammatory Bowel Diseases
Pharmacophore modeling coupled with molecular dynamic simulation approach to identify new leads for meprin-? metalloprotease.
Leukemia
Identification and characterization of human and mouse ovastacin: a novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish.
Lymphoma
Identification and characterization of human and mouse ovastacin: a novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish.
Myopia
Muscarinic antagonist control of myopia: evidence for m4 and m1 receptor-based pathways in the inhibition of experimentally-induced axial myopia in the tree shrew.
Neoplasms
Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.
Neoplasms
Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3.
Neoplasms
Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease.
Neoplasms
Spit and venom from scytodes spiders: a diverse and distinct cocktail.
Neoplasms
The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesion.
Neoplasms
Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio.
Neurodegenerative Diseases
An integrated in silico approach to understand protein-protein interactions: human meprin-? with fetuin-A.
Neurodegenerative Diseases
Pharmacophore modeling coupled with molecular dynamic simulation approach to identify new leads for meprin-? metalloprotease.
Paralysis
Isolation of neurotoxic peptides from the venom of the 'armed' spider Phoneutria nigriventer.
Renal Insufficiency
First insight into structure-activity relationships of selective meprin ? inhibitors.
Tetanus
The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy.
Tetanus
X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin.
Whooping Cough
Comparison between the vasoactive actions of endothelin and arginine vasopressin in pithed rats after pretreatment with BAY K 8644, nifedipine or pertussis toxin.
Whooping Cough
Pertussis toxin prevents neomycin-induced calcium-dependent electrophysiological effects in rat hippocampal slices.
Whooping Cough
Role of renal sympathetic nerves in regulating renovascular responses to angiotensin II in spontaneously hypertensive rats.
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-
-
brenda
-
isoform LAST
brenda
-
isoform LAST
brenda
-
brenda
-
-
brenda
-
-
brenda
the enzyme Xhe2 is exclusively expressed in hatching gland cells as they first emerge at the lateral edge of the anterior neural plate, and persists in this tissue up to the tadpole stage
brenda
-
-
brenda
-
-
brenda
astacin is synthesized as a preproenzyme in the midgut gland
brenda
-
LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle
brenda
-
brenda
-
-
brenda
the proenzyme is only transiently found within the ducts between the hepatopancreas and the stomach
brenda
-
LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle
brenda
-
deposure of fed astacin
brenda
-
-
brenda
-
deposure of fed astacin
brenda
-
-
brenda
mature enzyme
brenda
-
brenda
-
-
brenda
-
synthesized in (the fibrillar cells (F-cells) of) the hepatopancreas (midgut gland) and stored extracellularly in the cardia
brenda
-
synthesized in the hepatopancreas (midgut gland) and stored extracellularly in the cardia
brenda
-
synthesized in the hepatopancreas (midgut gland) and stored extracellularly in the cardia
brenda
-
-
brenda
-
1 mg astacin/ml
brenda
-
1 mg astacin/ml
brenda
-
1 mg astacin/ml
brenda
-
-
brenda
-
deposure of fed astacin
brenda
-
brenda
-
-
-
brenda
D5FM33
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
additional information
highest enzyme expression level occurs in the adult stage of the parasite
brenda
additional information
-
highest enzyme expression level occurs in the adult stage of the parasite
brenda
additional information
-
LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle
brenda
additional information
-
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
eight astacins with a minimal structure (a signal peptide, an activation domain and a Zn-binding catalytic domain), that are colocalized in large cells organized in a peculiar, not yet morphologically characterized, two-ring-shaped structure located in the middle of the body. A single astacin Smed-ast-8, characterized by a ShK toxin domain in its C-terminal region, has been found to be produced in gastrodermal cells. Smed-ast-1 almost completely colocalizes with Smed-ast-2, Smedast-3, Smed-ast-4, Smed-ast-5, Smed-ast-6, Smed-ast-7 and Smed-ast-9. Planarian astacins are exclusive for post-mitotic differentiated cells
brenda
additional information
developmental expression of enzyme Xhe2 and its regulation by transcription factor Pax3, overview
brenda
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evolution
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the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview
evolution
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the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview
evolution
-
the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview
evolution
-
the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview
evolution
the enzyme belongs to the astacin family of multidomain metallopeptidases, subgroups and domain structure, overall structure of mature astacin catalytic domains, overview
evolution
the enzyme belongs to the family of extracellular zinc peptidases, termed stacin family, and of the metzincin superfamily
evolution
the enzyme is a member of the astacin family of metalloproteases
evolution
structural organization of the astacin-like gene family in planarians, overview. All members of the astacin family are characterized by two key elements: the 18-amino acid zinc-binding motif (HEXXHXXGFXHEXXRXDR), and the methionine-turn (Met-turn) sequence SXMHY
evolution
the enzyme belongs to the astacin family of zinc-dependent endopeptidase. All the members of this family have a protease domain containing approximately 200 amino acids, which shares an amino-acid sequence similarity of 29-99%. Astacin family members are characterized by a unique 18 amino acid signature sequence HEXXHXXGFXHEXXRXDR containing the Zn binding motif HEXXH present in all metalloendopeptidases. Most of the known family members contain a COOH terminal to the protease domain. They are found to contain one or more copies of the EGF (epidermal growth factor) like E and/or CUB (complement subcomponents) domain. Differences in the active sites and inhibitor sites of astacin/BMP1, human meprin alpha, and human meprin beta, overview. The subsites S1, S2, S3, S1', S2', S3' have differences in amino acid residues. Structure homology modelling
evolution
the enzyme encoded by ASTL belongs to the digestive and hatching enzymes cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3LQB) and docking study, and potential binding site, detailed overview
evolution
the enzyme encoded by qcam1 belongs to the digestive and hatching enzymes cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3LQB) and docking study, and potential binding site, detailed overview
malfunction
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heterologous expression of the Haemonchus contortus dpy-31 orthologue in a Caenorhabditis elegans dpy-31 mutant results in the full rescue of the mutant body form
malfunction
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heterologous expression of the Haemonchus contortus dpy-31 orthologue in a Caenorhabditis elegans dpy-31 mutant results in the full rescue of the mutant body form
malfunction
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nas-36 gene from Brugia malayi successfully complements the moult defects associated with Caenorhabditis elegans nas-36, nas-37 and nas-36/nas-37 double mutants
malfunction
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the nas-36 and nas-37 genes in Caenorhabditis elegans encode functionally conserved enzymes of the astacin metalloprotease family which, when mutated, result in a phenotype associated with the late-stage moulting defects, namely the inability to remove the preceding cuticle
malfunction
D5FM33
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
malfunction
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis. Enzyme mutation causes temperature-sensitive lethality and cuticle defects, a DPY-31 enzyme from the ovine gastrointestinal nematode Teladorsagia circumcincta mutant strain TP224 is able to rescue the Caenorhabditis elegans mutant
malfunction
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis. The DPY-31 enzyme from the ovine gastrointestinal nematode Teladorsagia circumcincta mutant is able to rescue the defective Caenorhabditis elegans DPY-31 enzyme mutant
malfunction
ablation of one of the two zinc metalloproteinases, meprin beta and BMP-1, leads to different collagen I associated phenotypes in vivo
malfunction
-
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis
-
malfunction
-
enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis. Enzyme mutation causes temperature-sensitive lethality and cuticle defects, a DPY-31 enzyme from the ovine gastrointestinal nematode Teladorsagia circumcincta mutant strain TP224 is able to rescue the Caenorhabditis elegans mutant
-
malfunction
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enzyme inhibition causes body morphology phenotypes consistent with the inhibition of proteases involved in cuticle collagen synthesis. The DPY-31 enzyme from the ovine gastrointestinal nematode Teladorsagia circumcincta mutant is able to rescue the defective Caenorhabditis elegans DPY-31 enzyme mutant
-
metabolism
the enzyme Xhe2 expression depends entirely on transcription factor Pax3 function. Pax3 can induce premature hatching through the upregulation of several proteolytic enzymes including enzyme Xhe2
metabolism
the zinc metalloproteinases meprin beta and BMP-1 are differentially regulated by CaCl2, overview
physiological function
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effect of astacin on growth and color formation of juvenile red-white ornamental carp, overview. Carotenoid deposition in the skin, head, scale, and fin ray of fish fed diets containing astacin is significantly higher than that those fed the control. The fish are unable to fully synthesize carotenoid pigments and therefore need carotenoid to be added to their diets. Higher astacin content results in a brighter body color, astacin is mainly deposited in the skin, scales, and head
physiological function
the enzyme is a homologue of a vertebrate procollagen C-proteinase and performs a central role in cuticle formation of Caenorhabditis elegans
physiological function
the enzyme promotes Xenopus hatching. Xhe2 overexpression is sufficient to induce early hatching, indicating that Xhe2 is one of the key components of the degradation mechanism responsible for breaking down the vitelline membrane
physiological function
the protease is working at the host–parasite interface and is likely be exposed to the hosts immune response. Recombinant Ace-MTP-2 amplifies the in vitro release of TNFalpha and induces release of IFNgamma by lipopolysaccharide activated THP-1 macrophages, overview
physiological function
an increase in activity is reported under increasing calcium concentrations for BMP-1
physiological function
the astacin gene family of metalloproteinases in planarians, good candidate enzymes for generating dynamicity in the extracellular matrix. Astacins are secreted and membrane-bound metzincin metallopeptidases widespread among different animal phyla and involved in various physiological processes, including digestion, extracellular matrix (ECM) remodeling, morphogenesis, hatching, tissue remodeling, and differentiation
physiological function
the astacin gene family of metalloproteinases in planarians, good candidate enzymes for generating dynamicity in the extracellular matrix. Astacins are secreted and membrane-bound metzincin metallopeptidases widespread among different animal phyla and involved in various physiological processes, including digestion, extracellular matrix (ECM) remodeling, morphogenesis, hatching, tissue remodeling, and differentiation. Morphogenesis of the two-ring-shaped structure by visualization of Smed-ast-2 expression during regeneration. Smed-mmp1 and Smed-mmp2 are specialized in storage and secretion of extracellular matrix degrading enzymes
physiological function
the astacin gene family of metalloproteinases in planarians, good candidate enzymes for generating dynamicity in the extracellular matrix. Astacins are secreted and membrane-bound metzincin metallopeptidases widespread among different animal phyla and involved in various physiological processes, including digestion, extracellular matrix (ECM) remodeling, morphogenesis, hatching, tissue remodeling, and differentiation. Smed-mmp1 and Smed-mmp2 are specialized in storage and secretion of extracellular matrix degrading enzymes
physiological function
the astacin gene family of metalloproteinases in planarians, good candidate enzymes for generating dynamicity in the extracellular matrix. Astacins are secreted and membrane-bound metzincin metallopeptidases widespread among different animal phyla and involved in various physiological processes, including digestion, extracellular matrix (ECM) remodeling, morphogenesis, hatching, tissue remodeling, and differentiation. The ast-8 expression in the digestive system is a feature typically conserved in genes encoding astacins with a ShToxin domain
physiological function
-
the enzyme is a homologue of a vertebrate procollagen C-proteinase and performs a central role in cuticle formation of Caenorhabditis elegans
-
additional information
analysis of the astacin reaction mechanism from the crystal structure by computational methods, Optimized structure of the astacin active site with the model substrate bound, overview. All calculations were performed using density functional theory with the hybrid functional B3LYP, which is composed of Becke's three-parameter hybrid exchange functional (B3) and the correlation functional of Lee, Yang, and Parr. A model of the active site of astacin is built on the basis of the crystal structure of astacin in complex with the Pro-Leu-Gly-hydroxamate inhibitor, PDB entry 1QJJ
additional information
complementation of the Caenorhabditis elegans dpy-31 mutant with the Teladorsagia circumcincta dpy-31 gene
additional information
-
complementation of the Caenorhabditis elegans dpy-31 mutant with the Teladorsagia circumcincta dpy-31 gene
additional information
-
removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket S1'
additional information
-
removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1'
additional information
-
removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1'
additional information
-
removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1'
additional information
removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1'
additional information
the protease has a putative signal peptide, 11 potential phosphorylation sites, and two disulfide bridges revealed by computational analysis
additional information
-
the protease has a putative signal peptide, 11 potential phosphorylation sites, and two disulfide bridges revealed by computational analysis
additional information
molecular modeling of LALP3 reveals that this isoform contains the zinc binding and Met-turn motifs, forming the active site, as has been observed in astacins. LALP3 epitopes are recognized by polyclonal antibodies raised against Loxosceles intermedia whole venom and LALP1 in a conformation-dependent manner
additional information
-
molecular modeling of LALP3 reveals that this isoform contains the zinc binding and Met-turn motifs, forming the active site, as has been observed in astacins. LALP3 epitopes are recognized by polyclonal antibodies raised against Loxosceles intermedia whole venom and LALP1 in a conformation-dependent manner
additional information
structural differences between meprin beta (EC 3.4.24.63) and BMP-1. Molecular dynamics simulation
additional information
-
structural differences between meprin beta (EC 3.4.24.63) and BMP-1. Molecular dynamics simulation
additional information
the hydrogen bonding residues of the enzyme are Ser155, His186, His192, Tyr238, and Asn217, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview
additional information
the hydrogen bonding residues of the enzyme are Tyr60, His84, Glu85, His88, His94, and Asp119, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview
additional information
-
complementation of the Caenorhabditis elegans dpy-31 mutant with the Teladorsagia circumcincta dpy-31 gene
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Brugia malayi, Caenorhabditis elegans, Haemonchus contortus
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Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp)
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26
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Sus scrofa
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-
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Expression and immunological cross-reactivity of LALP3, a novel astacin-like metalloprotease from brown spider (Loxosceles intermedia) venom
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Loxosceles intermedia (C9D7R3), Loxosceles intermedia
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Meprin beta and BMP-1 are differentially regulated by CaCl2
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-
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Structure-activity relationship of astacin metalloproteases A comparative study using EDTA
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14
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2018
Coturnix japonica (P42662), Homo sapiens (Q6HA08)
-
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28
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Schmidtea mediterranea, Schmidtea mediterranea (A0A060Q6V2), Schmidtea mediterranea (A0A060Q6Y6), Schmidtea mediterranea (A0A060Q714), Schmidtea mediterranea (A0A060Q715), Schmidtea mediterranea (A0A060Q750), Schmidtea mediterranea (A0A060Q785), Schmidtea mediterranea (A0A060Q786), Schmidtea mediterranea (I1ZIC3)
brenda