Proteolytic Enzymes IV

Specificity:

Similar to that of papain

Inhibitors:

Cystatin, C8917
E-64, E3132
Iodoacetic Acid, I2512
N-a-p-Tosyl-L-lysine chloromethyl ketone Hydrochloride, T7254
N-a-p-Tosyl-L-phenylalanine chloromethyl ketone Hydrochloride, T4376
N-Ethylmaleimide, E3876

Specificity:

Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg bonds, where Xaa can by any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors

Specificity:

Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-Xaa, -Lys-Xaa >> -Phe-Xaa in small molecule substrates

Synthethic Substrates:

N-CBZ-GLY-PRO-ARG 7-AMIDO-4-METHYLCOUMARIN, C0855
N-CBZ-GLY-PRO-ARG 7-AMIDO-4-TRIFLUOROMETHYLCOUMARIN, C0980

Specificity:

Preferential cleavage: -Asp-Xaa >> -Asn-Xaa > -Met-Xaa, -Ser-Xaa

Synthethic Substrates:

Z-Gly-Pro-Arg 4-methoxy-2-naphthylamide, C1105
N-Acetyl-Ile-Glu-Thr-Asp-7-Amido-4-methylcoumarin, A4188
N-Acetyl-Ile-Glu-Pro-Asp-7-amido-4-methylcoumarin, A6220
N-Acetyl-Ile-Glu-Pro-Asp-p-nitroaniline, A6470
N-Acetyl-Ile-Glu-Thr-Asp-p-nitroanilide, A9968
Z-Ile-Glu-Thr-Asp 7-amido-4-trifluoromethylcoumarin, C5599

Inhibitors:

Antipain, A6191
3,4-Dichloroisocoumarin, D7910

Specificity:

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro

Synthethic Substrates:

HIV Protease Substrate I , H6660
HIV Protease Substrate V, H5410
HIV Protease Substrate VIII, H5785
Anthranilyl-HIV Protease Substrate V, H6035
Anthranilyl-HIV Protease Substrate VI, H6160

Specificity:

Hydrolyzes Pro-Pro-|-Y-Pro

Specificity:

Preferential cleavage of Arg-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-Xaa or Leu-Xaa . The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg bonds

Synthethic Substrates:

N-Benzoyl-Pro-Phe-Arg-p-nitroanilide hydrochloride, B2133
Z-Phe-Arg 7-amido-4-methylcoumarin hydrochl, C9521
Kininogen, low molecular weight from human plasma, K3628
D-Val-Leu-Arg 7-amido-4-methylcoumarin, V2763
D-Val-Leu-Arg 7-amido-4-trifluoromethylcoumarin, V2888

Inhibitors:

Aprotinin, A1153
Antithrombin III, Human, A2221
Antithrombin III, Bovine, A9141
Benzamidine Hydrochloride, B6506
Diisopropyl fluorophosphate, D0879
3,4-Dichloroisocoumarin, D7910
Leupeptin, L2023

Inhibitors:

Actinonin, A6671
Bestatin Hydrochloride, B8385

Specificity:

Release of an N-terminal amino acid, Xaa Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Xbb may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low

Synthethic Substrates:

L-Leucine p-Nitroanilide, L9125
N-Succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin, S9761

Inhibitors:

Amastatin Hydrochloride, A1276
(2S,3R)-3-Amino-2-hydroxy-4-(4-nitro«-»phenyl)butanoyl-L-leucine Hydrochloride, A5921
Actinonin, A6671
Bestatin Hydrochloride, B8385
Diethylenetriaminepentaacetic acid Free Acid, D6518
3,4-Dichloroisocoumarin, D7910
EDTA, ED2SS
EGTA, E4378
1,10-Phenanthroline Monohydrate, P9375

Specificity:

Release of an N-terminal amino acid, Xaa Xbb- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide

Synthethic Substrates:

L-Leucine p-Nitroanilide, L9125
N-Succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin, S9761

Inhibitors:

Amastatin Hydrochloride, A1276
Actinonin, A6671
Bestatin Hydrochloride, B8385

Specificity:

Specificity is MMP type specific

Synthethic Substrates:

7-Methoxycoumarin-4-acetyl-Pro-Leu-Gly-Leu-b-(2,4-dinitrophenylamino)Ala-Ala-Arg amide, M6412

Inhibitors:

Actinonin, A6671
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala hydroxamic acid, A4336
Dichloromethylenediphosphonic acid disodium salt, D4434
Isoamylphosphonyl-Gly-Pro-Ala dipotassium salt, I7029
N-[(2S)-(Methoxycarbonylmethyl)-4-methylpentanoyl]-L-tryptophan-methylamide, M5939
Z-Pro-Leu-Gly hydroxamate, C8537
Pro-Leu-Gly hydroxamate hydrochloride, P5298
Tissue Inhibitor of Metalloproteinase-1 from human fibroblasts, T8947
Tissue Inhibitor of Metalloproteinase-4 from human fibroblasts, T9322

Specificity:

Hydrolysis of N-terminal methionine

Specificity:

Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'

Synthethic Substrates:

Na-Benzoyl-L-arginine 7-amido-4-methylcoumarin Hydrochloride, B7260

Inhibitors:

Antipain, A6191
Chymostatin, C7268
Cystatin, C8917
3,4-Dichloroisocoumarin, D7910
E-64, E3132
Ebselen, E3520
Gly-Gly-Tyr-Arg, G5386
Leupeptin, L2023
a2-Macroglobulin, M6159
N-a-p-Tosyl-L-lysine chloromethyl ketone Hydrochloride, T7254
N-a-p-Tosyl-L-phenylalanine chloromethyl ketone Hydrochloride, T4376

Specificity:

Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1 Val, Gln4 His, Glu13 Ala, Ala14 Ala, Ala14 Leu, Leu15 Tyr, Tyr16 Leu, Gly23 Phe, Phe24 Phe and Phe25 Tyr bonds in the B chain of insulin

Inhibitors:

Pepstatin A, P5318