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Literature summary for 3.4.21.4 extracted from

  • Willett, W.S.; Gillmor, S.A.; Perona, J.J.; Flettrick, R.J.; Craik, C.S.
    Engineered metal regulation of trypsin specificity (1995), Biochemistry, 34, 2172-2180.
    View publication on PubMed
Search for more literature for 3.4.21.4

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
N143H/E151H the mutant enzyme with the engineered metal binding site hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0141
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide wild-type enzyme Rattus norvegicus
0.0162
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide mutant enzyme E151Q Rattus norvegicus
0.0177
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide mutant enzyme N143H Rattus norvegicus
0.0182
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide mutant enzyme E151H Rattus norvegicus
0.086
-
 Benzyloxycarbonyl-Lys-thiobenzyl ester wild-type enzyme Rattus norvegicus
2.1
-
 Benzyloxycarbonyl-Lys-thiobenzyl ester mutant D189H Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ trypsin N143H/E151H hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency Rattus norvegicus
Zn2+ trypsin N143H/E151H hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AGPYAHSS + H2O trypsin N143H/E151H hydrolyzes the peptide exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency Rattus norvegicus ?
-
 ?
benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
 Rattus norvegicus ?
-
 ?
benzyloxycarbonyl-Lys-thiobenzyl ester + H2O
-
 Rattus norvegicus benzyloxycarbonyl-Lys + phenylmethanethiol
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
12.3
-
 Benzyloxycarbonyl-Lys-thiobenzyl ester mutant D189H Rattus norvegicus
44.5
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide mutant enzyme N143H Rattus norvegicus
49.3
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide mutant enzyme E151Q Rattus norvegicus
58.3
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide wild-type enzyme Rattus norvegicus
69.3
-
 benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumarin 7-amide mutant enzyme E151H Rattus norvegicus
112
-
 alpha-N-benzyloxycarbonyl-Lys-thiobenzyl ester wild-type enzyme Rattus norvegicus