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Literature summary for 3.4.22.26 extracted from

  • Mielicki, W.P.
    Biochemistry of cancer procoagulant (2001), Haemostasis, 31 Suppl 1, 8-10.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Ca2+
-
Oryctolagus cuniculus
Ca2+ required, 7 mM Homo sapiens
Cd2+
-
Oryctolagus cuniculus
Cd2+ required, 1 mM Homo sapiens
Mg2+
-
Oryctolagus cuniculus
Mg2+ required, 7 mM Homo sapiens
Mn2+
-
Oryctolagus cuniculus
Mn2+ required, 0.1 mM Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
antipain
-
Homo sapiens
antipain
-
Oryctolagus cuniculus
Cu2+ inactivation Homo sapiens
Cu2+ inactivation Oryctolagus cuniculus
Fe2+ inactivation Homo sapiens
Fe2+ inactivation Oryctolagus cuniculus
iodoacetamide
-
Homo sapiens
iodoacetamide
-
Oryctolagus cuniculus
leupeptin
-
Homo sapiens
leupeptin
-
Oryctolagus cuniculus
Mercuric chloride
-
Homo sapiens
Mercuric chloride
-
Oryctolagus cuniculus
additional information no inhibition by alpha2-macroglobulin, alpha1-antiprotease, antithrombin III/heparin, cystatin, cysteamine, alpha1-anichymotrypsin, the effectiveness of most of the inhibitors increase in presence of reducing agents Homo sapiens
p-chloromercuric benzoate
-
Homo sapiens
Peptidyl diazomethyl ketones
-
Homo sapiens
Peptidyl diazomethyl ketones
-
Oryctolagus cuniculus
PMSF
-
Homo sapiens
PMSF
-
Oryctolagus cuniculus
Sn2+ inactivation Homo sapiens
Sn2+ inactivation Oryctolagus cuniculus
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane i.e. E-64, reversible, competitive Homo sapiens
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane ie.e. E-64, reversible, competitive Oryctolagus cuniculus
Zn2+ inactivation Homo sapiens
Zn2+ inactivation Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Homo sapiens 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information divalent metal ions are responsible for correct conformation of the enzyme, enzyme contains 2 metal binding sites: 1 for Ca2+ and Mg2+ binding, and 1 for Mn2+ and Cd2+ binding Homo sapiens
additional information divalent metal ions are responsible for correct conformation of the enzyme, enzyme contains 2 metal binding sites: 1 for Ca2+ and Mg2+ binding, and 1 for Mn2+ and Cd2+ binding Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
68000
-
-
Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor X + H2O Homo sapiens cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade factor Xa
-
?
factor X + H2O Oryctolagus cuniculus cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade factor Xa
-
?
additional information Homo sapiens enzyme seems to be regulated allosterically ?
-
?
PAR-1 receptor + H2O Homo sapiens
-
?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Oryctolagus cuniculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein
-
Homo sapiens
no glycoprotein
-
Oryctolagus cuniculus

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
amnion
-
Homo sapiens
-
carcinoma cell V2 carcinoma cell Oryctolagus cuniculus
-
chorion
-
Homo sapiens
-
leukemia cell
-
Homo sapiens
-
additional information produced by malignant and fetal cells Homo sapiens
-
additional information produced by malignant and fetal cells Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Ala-Pro-Arg-4-nitroanilide + H2O
-
Homo sapiens D-Ala-Pro-Arg + 4-nitroaniline
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
-
Homo sapiens D-Ile-Pro-Arg + 4-nitroaniline
-
?
factor X + H2O cleavage of Arg-Ile bond Oryctolagus cuniculus factor Xa
-
?
factor X + H2O cleavage of Arg-Ile bond in factor X heavy chain Homo sapiens factor Xa
-
?
factor X + H2O cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade Homo sapiens factor Xa
-
?
factor X + H2O cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade Oryctolagus cuniculus factor Xa
-
?
Glu-Glu-Pro-Arg-4-nitroanilide + H2O
-
Homo sapiens Glu-Glu-Pro-Arg + 4-nitroaniline
-
?
additional information substrate recognition depends on the secondary and tertiary configuration of the protein substrate rather than on the primary sequence alone, no activity with substrates containing the sequence Xaa-Lys-ProP2-TyrP1- Homo sapiens ?
-
?
additional information enzyme seems to be regulated allosterically Homo sapiens ?
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
-
Homo sapiens N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
?
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
-
Homo sapiens N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
?
PAR-1 receptor + H2O
-
Homo sapiens ?
-
?
PAR-1 receptor + H2O enzyme competes with thrombin for the same protease-activated receptor, i.e. PAR-1, on the blood platelet surface Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 68000 Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
cancer procoagulant
-
Homo sapiens
cancer procoagulant
-
Oryctolagus cuniculus
CP
-
Homo sapiens
CP
-
Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.128
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
Homo sapiens

pI Value

Organism Comment pI Value Maximum pI Value
Oryctolagus cuniculus
-
-
4.8