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Literature summary for 3.4.24.72 extracted from

  • Choi, J.; Sapkota, K.; Kim, S.; Kim, S.
    Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential (2014), Biochimie, 105, 45-57.
    View publication on PubMed

Application

Application Comment Organism
medicine starase has the potential to be a potent thrombolytic agent due to its bi-functional properties (containing both direct-acting and plasminogen-activating activities) and lack of hemorrhagic activity Patiria pectinifera

Inhibitors

Inhibitors Comment Organism Structure
4-amidinophenylmethylsulfonyl fluoride 5% residual activity at 2 mM Patiria pectinifera
additional information not inhibited by EDTA and EGTA Patiria pectinifera
phenylmethylsulfonyl fluoride 4% residual activity at 2 mM Patiria pectinifera

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.37
-
D-Val-Leu-Lys-4-nitroanilide at pH 7.4 and 37°C Patiria pectinifera

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme activity is not influenced by Mn2+, Cu2+, Ca2+, Mg2+, Co2+, Zn2+, and Fe2+ Patiria pectinifera

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
1 * 48000, SDS-PAGE Patiria pectinifera

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
fibrinogen + H2O Patiria pectinifera the alpha-chain is rapidly hydrolyzed and the beta-chain is partially digested by 10 ng of starase. With an increase in starase concentration to 120 ng, the gamma-chain is partially degraded, but all the alpha-, beta- and gamma-chains of fibrinogen are completely cleaved by 250 ng and higher concentration of starase fibrin + ?
-
?
plasminogen + H2O Patiria pectinifera
-
plasmin + ?
-
?

Organism

Organism UniProt Comment Textmining
Patiria pectinifera
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sepharose CL6B column chromatography, Sepharose CL4B column chromatography, and Mono Q HR column chromatography Patiria pectinifera

Source Tissue

Source Tissue Comment Organism Textmining
hepatic cecum
-
Patiria pectinifera
-

Storage Stability

Storage Stability Organism
-20°C, 20 mM Tris-HCl buffer, 3 months, 3% loss of enzyme activity Patiria pectinifera
4°C, 20 mM Tris-HCl buffer, 3 months, 5% loss of enzyme activity Patiria pectinifera

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bovine albumin + H2O
-
Patiria pectinifera ?
-
?
bovine gamma-globulin + H2O
-
Patiria pectinifera ?
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O highest activity Patiria pectinifera D-Val-Leu-Lys + 4-nitroaniline
-
?
extracellular matrix component type VII collagen
-
Patiria pectinifera ?
-
?
factor Xa + H2O
-
Patiria pectinifera ?
-
?
fibrinogen + H2O the alpha-chain is rapidly hydrolyzed and the beta-chain is partially digested by 10 ng of starase. With an increase in starase concentration to 120 ng, the gamma-chain is partially degraded, but all the alpha-, beta- and gamma-chains of fibrinogen are completely cleaved by 250 ng and higher concentration of starase Patiria pectinifera fibrin + ?
-
?
additional information the enzyme shows weak amidolytic activity for the substrates Z-D-Arg-Gly-Arg-4-nitroanilide and D-Phe-Pip-Arg-4-nitroanilide Patiria pectinifera ?
-
?
plasminogen + H2O
-
Patiria pectinifera plasmin + ?
-
?
pyroGlu-Gly-Arg-4-nitroanilide + H2O
-
Patiria pectinifera pyroGlu-Gly-Arg + 4-nitroaniline
-
?
thrombin + H2O
-
Patiria pectinifera ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 48000, SDS-PAGE Patiria pectinifera

Synonyms

Synonyms Comment Organism
fibrinolytic protease
-
Patiria pectinifera
starase
-
Patiria pectinifera

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Patiria pectinifera

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Patiria pectinifera