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Literature summary extracted from

  • Schmidt, A.E.; Sun, M.F.; Ogawa, T.; Bajaj, S.P.; Gailani, D.
    Functional role of residue 193 (chymotrypsin numbering) in serine proteases: influence of side chain length and beta-branching on the catalytic activity of blood coagulation factor XIa (2008), Biochemistry, 47, 1326-1335.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.27 expression of wild-type and mutant enzymes in HEK-293 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.27 G193A site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites Homo sapiens
3.4.21.27 G193D site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 1.6-36fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites Homo sapiens
3.4.21.27 G193E site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites Homo sapiens
3.4.21.27 G193K site-directed mutagenesis, the mutant shows reduced catalytic activity and binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate impaired 35-478fold, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites Homo sapiens
3.4.21.27 G193R site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites Homo sapiens
3.4.21.27 G193V site-directed mutagenesis, the mutant shows reduced catalytic activity and impaired binding of inhibitors 4-aminobenzamidine and diisopropylfluorophosphate, respectively, indicating distortion of, or altered accessibility to, the S1 and oxyanion-binding sites Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.27 4-aminobenzamidine beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview Homo sapiens
3.4.21.27 amyloid beta-precursor protein Kunitz domain beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview Homo sapiens
3.4.21.27 antithrombin in presence of heaprin Homo sapiens
3.4.21.27 diisopropylfluorphosphate beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, beta-branching causes steric conflicts with the FXIa 140-loop, overview Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.27 additional information
-
 additional information kinetics of recombinant wild-type and mutant enzymes, overview Homo sapiens
3.4.21.27 0.26
-
 pyroGlu-Pro-Arg-4-nitroanilide recombinant wild-type enzyme, pH 7.5, 37°C Homo sapiens
3.4.21.27 0.34
-
 D-Ile-Pro-Arg-4-nitroanilide recombinant wild-type enzyme, pH 7.5, 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.27 Ca2+
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.27 Homo sapiens P03951
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.27 recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.27 D-Ile-Pro-Arg-4-nitroanilide + H2O substrate S-2288 Homo sapiens D-Ile-Pro-Arg + 4-nitroaniline
-
 ?
3.4.21.27 factor IX + H2O cleavage at Ala145 and Ala180 Homo sapiens activated factor IX + ?
-
 ?
3.4.21.27 additional information beta-branching of the side chain of residue 193 is deleterious for interactions with 4-aminobenzamidine, diisopropylfluorphosphate, and amidolytic substrates, situations where no S2'-P2' interactions are involved, overview Homo sapiens ?
-
 ?
3.4.21.27 pyroGlu-Pro-Arg-4-nitroanilide + H2O substrate S-2366 Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.27 blood coagulation factor XIa
-
 Homo sapiens
3.4.21.27 factor XIa
-
 Homo sapiens
3.4.21.27 FXIa
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.27 37
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.27 110.2
-
 D-Ile-Pro-Arg-4-nitroanilide recombinant wild-type enzyme, pH 7.5, 37°C Homo sapiens
3.4.21.27 145
-
 pyroGlu-Pro-Arg-4-nitroanilide recombinant wild-type enzyme, pH 7.5, 37°C Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.27 7.5
-
 assay at Homo sapiens