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Literature summary for 3.4.23.28 extracted from

  • Takahashi, K.
    Acrocylindropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 91-92.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme, repeated crystallization Acrocylindrium sp.

Inhibitors

Inhibitors Comment Organism Structure
1,2-epoxy-3-(4-nitrophenoxy)propane i.e. EPNP Acrocylindrium sp.
Diazoacetyl-DL-norleucine methyl ester i.e. DAN, in presence of cupric ions Acrocylindrium sp.
pepstatin strong inhibition Acrocylindrium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Acrocylindrium sp.
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 6 H2O Acrocylindrium sp. i.e. insulin B chain, cleavage site specificity FVNQHL + CGSHL + VEAL + L-Tyr + LVCGERGF + L-Phe + YTPKA
-
?
Glucagon + H2O Acrocylindrium sp.
-
?
-
?
insulin A chain + H2O Acrocylindrium sp. cleavage site specificity ?
-
?

Organism

Organism UniProt Comment Textmining
Acrocylindrium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from cell culture medium by successive acetone precipitation, ammonium sulfate fractionation, and adsorption chromatography, to homogeneity Acrocylindrium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Acrocylindrium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O high activity Acrocylindrium sp. ?
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 6 H2O i.e. insulin B chain, cleavage site specificity Acrocylindrium sp. FVNQHL + CGSHL + VEAL + L-Tyr + LVCGERGF + L-Phe + YTPKA
-
?
Glucagon + H2O
-
Acrocylindrium sp. ?
-
?
insulin A chain + H2O cleavage site specificity Acrocylindrium sp. ?
-
?
additional information the enzyme prefers Tyr, Phe, or Leu at P1 or P1' positions Acrocylindrium sp. ?
-
?

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the A1 peptidase family Acrocylindrium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Acrocylindrium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
stable below Acrocylindrium sp.
70
-
inactivation above Acrocylindrium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2
-
substrate casein Acrocylindrium sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
2.5 5 highly stable, unstable below pH 0.7 and above pH 5.6 Acrocylindrium sp.