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Literature summary for 3.4.24.21 extracted from

  • Becker-Pauly, C.; Bruns, B.C.; Damm, O.; Schuette, A.; Hammouti, K.; Burmester, T.; Stoecker, W.
    News from an ancient world: two novel astacin metalloproteases from the horseshoe crab (2009), J. Mol. Biol., 385, 236-248.
    View publication on PubMed
Search for more literature for 3.4.24.21

Activating Compound

Activating Compound Comment Organism Structure
additional information isoform LAST, activity increases after incubation with trypsin Limulus polyphemus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Hi5 cell Limulus polyphemus

Inhibitors

Inhibitors Comment Organism Structure
1,10-o-phenanthroline 1 mM, isoform LAST, 10% residual activity, isoform LAST_MAM, 12% residual activity Limulus polyphemus
actinonin 1 mM, isoform LAST, 89% residual activity isoform LAST_MAM, 45% resiudal activity Limulus polyphemus
alpha-2-Macroglobulin 1 mM, isoform LAST, 1,1% residual activity, isoform LAST_MAM, 42% resiudal activity Limulus polyphemus
benzyloxycarbonyl-prolyl-leucylglycyl-hydroxamate 1 mM, isoform LAST, 83% residual activity, isoform LAST_MAM, 15.5% resiudal activity Limulus polyphemus

Organism

Organism UniProt Comment Textmining
Limulus polyphemus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification both LAST and LAST_MAM are synthesized as zymogens. LAST-MAM is active in its zymogen form Limulus polyphemus

Source Tissue

Source Tissue Comment Organism Textmining
brain isoform LAST Limulus polyphemus
-
eye isoform LAST Limulus polyphemus
-
additional information LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle Limulus polyphemus
-
muscle LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle Limulus polyphemus
-
proventriculus LAST_MAM signals are detected in all investigated tissues, most dominantly in the proventriculus and muscle Limulus polyphemus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Collagen IV + H2O
-
 Limulus polyphemus ?
-
 ?
Fibronectin + H2O
-
 Limulus polyphemus ?
-
 ?
Gelatin + H2O
-
 Limulus polyphemus ?
-
 ?
laminin I + H2O
-
 Limulus polyphemus ?
-
 ?
laminin I/nidogen I complex + H2O
-
 Limulus polyphemus ?
-
 ?
additional information no substrate: alpha-1 and alpha-2 chains of triple-helical collagen I Limulus polyphemus ?
-
 ?

Subunits

Subunits Comment Organism
More 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 Limulus polyphemus

Synonyms

Synonyms Comment Organism
LAST
-
 Limulus polyphemus
LAST_MAM
-
 Limulus polyphemus