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Literature summary for 3.4.21.6 extracted from

  • Chattopadhyay, R.; Iacob, R.; Sen, S.; Majumder, R.; Tomer, K.B.; Lentz, B.R.
    Functional and structural characterization of factor Xa dimer in solution (2009), Biophys. J., 96, 974-986.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.6

Inhibitors

Inhibitors Comment Organism Structure
1,2-dicaproyl-sn-glycero-3-phospho-L-serine presence of 1,2-dicaproyl-sn-glycero-3-phospho-L-serine and 5 mM Ca2+ results in dimerization with concomitant decrease in kcat value. Binding of 1,2-dicaproyl-sn-glycero-3-phospho-L-serine exposes residues K351. K242, and K420 Homo sapiens
Ca2+ the strength of the dimer interaction is strongly Ca2+-concentration-dependent, such that significant dimer forms in solution only at or above 5 mM Ca2+ Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00026
-
 prothrombin dimer, presence of 5 mM Ca2+ Homo sapiens
0.0004
-
 prothrombin monomer, presence of 5 mM Ca2+ Homo sapiens
0.000605
-
 prothrombin monomer, presence of 3 mM Ca2+ Homo sapiens
0.000985
-
 prothrombin dimer, presence of 3 mM Ca2+ Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arg-Gly-Arg-4-nitroanilide + H2O
-
 Homo sapiens Arg-Gly-Arg + 4-nitroaniline
-
 ?
prothrombin + H2O
-
 Homo sapiens thrombin + ?
-
 ?

Subunits

Subunits Comment Organism
dimer and monomer. Dimer is about 1000000fold less active toward prothrombin than the monomer. Dimerization results in substantial change in tertiary or quarternary strucutre with a concomitant decrease in alpha-helix Homo sapiens
monomer and dimer. Dimer is about 1000000fold less active toward prothrombin than the monomer. Dimerization results in substantial change in tertiary or quarternary strucutre with a concomitant decrease in alpha-helix Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 prothrombin and monomer. Dimer is about 1000000fold less active toward prothrombin than the monomer, mainly due to a substantial decrease in kcat. Dimerization results in substantial change in tertiary or quarternary structure with a concomitant decrease in alpha-helix Homo sapiens
0.0000000018
-
 prothrombin dimer, presence of 3 mM Ca2+ Homo sapiens
0.000000002
-
 prothrombin dimer, presence of 5 mM Ca2+ Homo sapiens
0.0029
-
 prothrombin monomer, presence of 3 mM Ca2+ Homo sapiens
0.004
-
 prothrombin monomer, presence of 5 mM Ca2+ Homo sapiens