Information on EC 3.4.24.21 - astacin

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The expected taxonomic range for this enzyme is: Bilateria

EC NUMBER
COMMENTARY
3.4.24.21
-
RECOMMENDED NAME
GeneOntology No.
astacin
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of arylamide bond
-
-
-
-
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
astacin
-
-
Astacus proteinase
-
-
-
-
BMP-1
-
-
carp nephrosin
O42326
-
Crayfish small-molecule proteinase
-
-
-
-
EC 3.4.99.6
-
-
formerly
-
LAST_MAM
-
-
MEP1A
-
-
MEP1B
-
-
nas-36
-
nas-36 gene encodes a functionally conserved enzyme of the astacin metalloprotease family
nas-37
-
nas-37 gene encodes a functionally conserved enzyme of the astacin metalloprotease family
nephrosin
O42326
-
CAS REGISTRY NUMBER
COMMENTARY
143179-21-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
crayfish
-
-
Manually annotated by BRENDA team
European crayfish
UniProt
Manually annotated by BRENDA team
European freshwater crayfish; i.e. Astacus fluviatilis
-
-
Manually annotated by BRENDA team
freshwater crayfish
-
-
Manually annotated by BRENDA team
i.e. Astacus fluviatilis
-
-
Manually annotated by BRENDA team
common carp
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
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
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Ala)n 4-nitroanilide + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
-
fluorogenic bradykinin analog substrate, cleavage site: Leu-Ser
-
-
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
show the reaction diagram
-
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
show the reaction diagram
-
best of fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser
-
-
2-aminobenzoyl-YEFDGKSMQGDDPN-2,4-dinitrophenyl + H2O
?
show the reaction diagram
-
Dentin sialophosphoprotein (Dpp) cleavage site, designated Dspp-FRET
-
-
?
Acetyl-Ala-Ala-Ala methylester + H2O
?
show the reaction diagram
-
-
-
-
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
i.e. nitrobradykinin, chromogenic bradykinin analog
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
D2KBH9, -
-
-
-
?
Bradykinin + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
show the reaction diagram
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
bradykinin 1-7 RPPGFSP + H2O
?
show the reaction diagram
-, O42326
partial digestion
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
heat-denatured form
-
-
-
casein + H2O
hydrolyzed casein
show the reaction diagram
-
heat-denatured form
-
-
Collagen + H2O
?
show the reaction diagram
-, Q9U918
-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Ala-Ala-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Ala-Ala-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Arg-Ala-Pro-Leu + H2O
Dansyl-Arg + Ala-Pro-Leu
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Arg-Ala-Pro-Leu + H2O
Dansyl-Arg + Ala-Pro-Leu
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Pro-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Pro-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Ser-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Gly-Arg-Arg + Ala-Ser-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Gly-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Gly-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Asn + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Asn-Ala
-
-
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Lys-Asn + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Asn-Ala
-
-
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Tyr + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Tyr-Ala
-
-
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Gly-Lys-Tyr + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Tyr-Ala
-
-
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Pro-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Gly-Pro-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Pro-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Pro-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Ser-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Dansyl-Leu-Arg-Arg + Ala-Ser-Leu-Gly
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala, poor substrate
-
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala, poor substrate
-
-
Dansyl-Leu-Lys-Arg-Leu-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Leu-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Leu, poor substrate
-
-
-
Dansyl-Leu-Lys-Arg-Leu-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Arg + Leu-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Leu, poor substrate
-
-
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Asn + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Asn-Ala
-
-
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val + H2O
Dansyl-Leu-Lys-Asn + Ala-Pro-Leu-Val
show the reaction diagram
-
cleavage site: Asn-Ala
-
-
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Lys + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Lys-Ala
-
-
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Lys + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Lys-Ala
-
-
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Tyr + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Tyr-Ala
-
-
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val + H2O
Dansyl-Leu-Lys-Tyr + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Tyr-Ala
-
-
Dansyl-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Lys-Arg + Ala-Pro-Leu
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Lys-Arg-Ala-Pro-Leu + H2O
Dansyl-Lys-Arg + Ala-Pro-Leu
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Lys-Glu-Thr-Tyr-Ser-Lys + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Dansyl-Lys-Glu-Thr-Tyr-Ser-Phe + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Dansyl-Pro-Gln-Gly-Ile-Ala-Gly-(D)-Arg + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Pro-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Pro-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Val-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val + H2O
Dansyl-Val-Lys-Arg + Ala-Pro-Trp-Val
show the reaction diagram
-
cleavage site: Arg-Ala
-
-
Denatured chains of alpha-tubulin + H2O
Hydrolyzed alpha-tubulin chains
show the reaction diagram
-
tubulin chains are cleaved only in the denatured state
-
-
-
Denatured chains of alpha-tubulin + H2O
Hydrolyzed alpha-tubulin chains
show the reaction diagram
-
cleavage sites, overview
-
-
Denatured chains of beta-tubulin + H2O
Hydrolyzed beta-tubulin chains
show the reaction diagram
-
tubulin chains are cleaved only in the denatured state
-
-
-
Denatured chains of beta-tubulin + H2O
Hydrolyzed beta-tubulin chains
show the reaction diagram
-
cleavage sites, overview
-
-
Denatured tubulin + H2O
Hydrolyzed tubulin
show the reaction diagram
-
cleavage pattern
-
-
Des-Arg-bradykinin PPGFSPFR + H2O
?
show the reaction diagram
-, O42326
complete digestion
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-, Q9U918
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
D2KBH9, -
-
-
-
?
gelatine + H2O
?
show the reaction diagram
-
-
-
-
?
laminin I + H2O
?
show the reaction diagram
-
-
-
-
?
laminin I/nidogen I complex + H2O
?
show the reaction diagram
-
-
-
-
?
PRPKPQQFFGLM-NH2 + H2O
?
show the reaction diagram
-, O42326
complete digestion
-
?
SQT-3 + H2O
?
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-Ala-4-nitroanilide + H2O
Suc-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Succinyl-(Ala)n 4-nitroanilide + H2O
?
show the reaction diagram
-
n: 2,3,5
-
-
-
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
Succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
-
i.e. STANA, poor substrate
-
-
-
Succinyl-Ala-Ala-Phe 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-Pro 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-Val 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Pro-Ala 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Pro-Ala-Ala 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
Type I collagen + H2O
?
show the reaction diagram
-
from calf skin
-
-
-
Lys-bradykinin KRPPGFSPFR + H2O
?
show the reaction diagram
-, O42326
complete digestion
-
?
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
?
-
-, O42326
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
-
-
-
additional information
?
-
-, Q9U918
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-, Q9U918
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-, Q9U918
-
-
-
?
additional information
?
-
-, Q9U918
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Zn2+
-
about 1 mol zinc per mol enzyme, atomic absorption spectroscopy; mechanism; requirement; very tightly bound, 40 days half-life for metal dissociation; zinc metalloenzyme
Zn2+
-
requirement; zinc-binding consensus sequence; zinc metalloenzyme
Zn2+
-
requirement; the catalytically active zinc is located at the bottom of the active-site cleft in the center of the molecule; zinc-binding consensus sequence; zinc metalloenzyme
Zn2+
-
pentavalent metal coordination; requirement; zinc-binding consensus sequence; zinc metalloenzyme
Zn2+
-
about 1 mol zinc per mol enzyme, atomic absorption spectroscopy; requirement; zinc-binding consensus sequence; zinc metalloenzyme
Zn2+
-
requirement; zinc metalloenzyme
Zn2+
-
zinc endopeptidase
Zn2+
-, O42326
zinc endopeptidase
Zn2+
-, Q9U918
required for activity
K+
-, O42326
secretion of nephrosin can be stimulated by high concentrations of extracellular potassium
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; no other metal than Co2+, Zn2+ or Cu2+ detectable by atomic absorption spectroscopy
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-o-phenanthroline
-
1 mM, isoform LAST, 10% residual activity, isoform LAST_MAM, 12% residual activity
1,10-phenanthroline
-
r; reactivation of apoenzyme by Zn2+ (100%), Cu2+ (70%) or Co2+ (50%); strong, kinetics
1,10-phenanthroline
-
r; strong, kinetics
1,10-phenanthroline
-, O42326
-
1,10-phenanthroline
-
-
1,7-phenanthroline
-
weak
1,7-phenanthroline
-
not reversible by addition of Zn2+
2,2'-dipyridyl
-
r
4-Mercaptoaniline
-
weak
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
-
-
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
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
Captopril
-, O42326
-
Carbobenzoxy-Phe-PSI(PO2H)-Ala-Pro-Phe-NH2
-
-
cysteine
-
weak
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
Diethyldicarbamate
-, O42326
-
-
dipicolinic acid
-
r
Ecballium elaterium Astacus protease inhibitor 1
-
i.e. EEAPI1
-
Ecballium elaterium Astacus protease inhibitor 2
-
i.e. EEAPI2
-
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
-, O42326
-
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
-
-
o-phenanthroline
D2KBH9, -
-
Potato inhibitor d
-
i.e. PoI-d, astacin inhibitor from potato
-
Tyrosin hydroxamate
-
most effective hydroxamate inhibitor
Hydroxamylsuccinyl-Pro-Phe-Arg
-
-
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
-, O42326
little or no inhibition by pestatin, PMSF, and iodoacetate
-
additional information
-, P84748
the digestive fluid contains heat-stable serine peptidase inhibitors ranging in molecular mass from about 15 to 32 kDa
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
isoform LAST, activity increases after incubation with trypsin
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.327
-
2-Aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.044
-
2-Aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.154
-
2-Aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.954
-
2-Aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.867
0.87
2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.867
0.87
2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg
-
dansyl-Leu-Lys-Arg-Ala-Pro-Leu
0.281
-
2-Aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.029
-
2-Aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
-
0.306
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg
-
-
0.209
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg
-
-
0.116
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg
-
-
0.194
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg
-
-
0.085
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg
-
-
1.86
-
azocasein
D2KBH9, -
pH 7.5, 37C, Vmax: 0.281 microM/min
-
0.48
-
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val
-
-
56
-
Dansyl-Arg-Ala-Pro-Leu
-
-
0.39
-
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly
-
-
5
-
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val
-
-
0.017
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val
-
-
0.015
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val
-
-
0.4
-
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val
-
HPLC analysis
0.52
-
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val
-
analyzed by tryptophan fluorescence changes between enzyme-substrate complex and enzyme plus product
0.27
-
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val
-
-
0.53
-
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val
-
-
0.23
-
Dansyl-His-His-Leu-Lys-Arg-Ala-Pro-Trp-Val
-
dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly
0.58
-
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly
-
-
0.67
-
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly
-
-
0.33
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val
-
-
1
-
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val
-
-
0.29
-
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val
-
-
0.28
-
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val
-
-
2
-
Dansyl-Lys-Arg-Ala-Pro-Leu
-
-
0.37
-
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val
-
-
0.25
-
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val
-
dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.1
-
2-Aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
-
15.1
-
2-Aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
-
44.4
-
2-Aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg
-
-
2.8
-
2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-4-nitrophenylalanine-Arg
-
-
14.3
-
2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg
-
-
3.6
-
2-Aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg
-
-
78.4
-
2-Aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
-
834
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg
-
-
0.002
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg
-
-
0.001
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg
-
-
0.004
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg
-
-
78.7
-
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg
-
-
27.9
-
azocasein
D2KBH9, -
pH 7.5, 37C
-
200
-
Dansyl-Ala-Ala-Arg-Ala-Pro-Leu-Val
-
-
0.035
-
Dansyl-Arg-Ala-Pro-Leu
-
-
34
-
Dansyl-Gly-Arg-Arg-Ala-Pro-Leu-Gly
-
-
0.7
-
Dansyl-Gly-Arg-Arg-Ala-Ser-Leu-Gly
-
-
20
-
Dansyl-Gly-Gly-Arg-Ala-Pro-Trp-Val
-
-
2.3
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Leu-Val
-
-
2.2
-
Dansyl-Gly-Lys-Arg-Ala-Pro-Trp-Val
-
-
39
-
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val
-
HPLC analysis
56
-
Dansyl-Gly-Lys-Asn-Ala-Pro-Leu-Val
-
analyzed by tryptophan fluorescence changes between enzyme-substrate complex and enzyme plus product
40
-
Dansyl-Gly-Lys-Tyr-Ala-Pro-Trp-Val
-
-
20
-
Dansyl-Gly-Pro-Arg-Ala-Pro-Leu-Val
-
-
310
-
Dansyl-His-His-Leu-Lys-Arg-Ala-Pro-Trp-Val
-
-
130
-
Dansyl-Leu-Arg-Arg-Ala-Pro-Leu-Gly
-
-
2.7
-
Dansyl-Leu-Arg-Arg-Ala-Ser-Leu-Gly
-
-
43
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu
-
-
120
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Leu-Val
-
-
210
-
Dansyl-Leu-Lys-Arg-Ala-Pro-Trp-Val
-
-
180
-
Dansyl-Leu-Lys-Asn-Ala-Pro-Leu-Val
-
-
210
-
Dansyl-Leu-Lys-Lys-Ala-Pro-Trp-Val
-
-
67
-
Dansyl-Leu-Lys-Tyr-Ala-Pro-Trp-Val
-
-
40
-
Dansyl-Lys-Arg-Ala-Pro-Leu
-
-
380
-
Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val
-
-
190
-
Dansyl-Val-Lys-Arg-Ala-Pro-Trp-Val
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0018
-
9-fluorenylmethyloxycarbonyl-KFPCAPLV-OH
-
pH 8.0, 25C
0.000036
-
9-fluorenylmethyloxycarbonyl-PKFPCAPLV-OH
-
pH 8.0, 25C
0.0036
-
9fluorenylmethyloxycarbonyl-FPCAPLVOH
-
pH 8.0, 25C
0.01
-
benzyloxycarbonyl-PKF-PSI[PO2CH2]-APL-O-methyl
-
pH 8.0, 25C
0.58
-
benzyloxycarbonyl-PKF-PSI[PO2CH2]-GPL-O-methyl
-
pH 8.0, 25C
0.011
-
benzyloxycarbonyl-PKK-PSI[PO2CH2]-APLV-O-methyl
-
pH 8.0, 25C
0.014
-
benzyloxycarbonyl-Pro-Lys-Phe-PSI[PO2CH2]Ala-Pro-O-methyl
-
pH 8.0, 25C
0.000042
-
fluorenylmethyloxycarbonyl-Pro-Lys-Phe-PSI[PO2CH2]Ala-Pro-Leu-Val
-
pH 8.0, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-, O42326
specific activity 18.16 units/mg, one unit of activity is the amount of nephrosin causing the same proteolytic activity as 1 unit of chymotrypsin in the RCM-BSA zymographic assay
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
Ala-Ala-Ala 4-nitroanilide
7.5
-
-
assay at
7.5
-
D2KBH9, -
-
8
-
-
succinyl-Ala-Ala-Ala 4-nitroanilide
additional information
-
-
pI: 4
additional information
-
-
pI: 3.5 (native astacin), pI: 4.8 (urea-denatured astacin)
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
25
-
-
assay at
30
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
synthesized in (the fibrillar cells (F-cells) of) the hepatopancreas (midgut gland) and stored extracellularly in the cardia
Manually annotated by BRENDA team
-
synthesized in the hepatopancreas (midgut gland) and stored extracellularly in the cardia
Manually annotated by BRENDA team
-
isoform LAST
Manually annotated by BRENDA team
-
LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle
Manually annotated by BRENDA team
-, Q9U918
the proenzyme is only transiently found within the ducts between the hepatopancreas and the stomach
Manually annotated by BRENDA team
-
LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle
Manually annotated by BRENDA team
-, Q9U918
mature enzyme
Manually annotated by BRENDA team
-, Q9U918
astacin is synthesized as a preproenzyme in the midgut gland
Manually annotated by BRENDA team
additional information
-
LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22180
-
-
calculation from sequence of cDNA
22610
-
-
Astacus astacus, deduced from amino acid sequence
23000
-
-
-
23000
-
-, O42326
SDS-PAGE
35200
-
D2KBH9, -
calculated from cDNA
50000
-
-
recombinant His-tagged protein
additional information
-
-
amino acid sequence compared to the other enzymes of the astacin family
additional information
-
-
primary structure
additional information
-
-
secondary structure
additional information
-
-
3-dimensional structure; primary structure; sequence alignment of enzymes of astacin family
additional information
-
-
primary structure
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 23000, Astacus astacus, SDS-PAGE
additional information
-
sequence of isoform LAST consists of a signal domain, a prodomain, and a catalytic domain, with the latter including the astacin-typical zinc-binding motif HExxHxxGxxHE and the Met-turn SxMxY. LAST_MAM has an additional N-terminal meprin A5 protein tyrosine phosphatase my domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
putative
proteolytic modification
-
both LAST and LAST_MAM are synthesized as zymogens. LAST-MAM is active in its zymogen form
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
astacin structure compared to those of thermolysin and adamalysin II; Astacus astacus
-
Astacus astacus
-
Astacus astacus; X-ray crystallography
-
Astacus astacus; X-ray crystallography of Cu(II)-astacin, Co(II)-astacin and Ni(II)-astacin
-
proastacin is crystallized by the sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 8000, 0.1 M (NH4)2SO4, 0.01 M MgCl2, 0.05 M MES, pH 5.6
-, Q9U918
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
below, rapid and irreversible inactivation
4
-
-
below, precipitation
4
-
-
below, rapid and irreversible inactivation
8
-
-
resistant to self-degradation for several days at 30C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
resistant to self-degradation for several days at pH 8
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Remarkably stable against proteolytic digestion and autolysis
-
Soluble at concentrations of at least up to 20 mg/ml
-
Very resistant to self-degradation even upon prolonged incubation for several days
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, apoenzyme, at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
multiple immunologically identical forms
-
proastacin is purified by Ni-NTA column chromatography and HEMA-Bio gel filtration
-, Q9U918
recombinant astacin
-
two closely related forms of slightly different electrophoretic mobility
-
using Ni-NTA chromatography
-
-
-, O42326
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNA reverse-transcribed from midgut-gland mRNA, cloned into pET3a vector and used to transform Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-, Q9U918
recombinantly expressed as a His-tagged fusion in Escherichia coli
-
-
-, O42326
recombinantly expressed as a His-tagged fusion in Escherichia coli
-
expression in Hi5 cell
-
recombinantly expressed in Escherichia coli
D2KBH9, -