Substrates: high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position Products: -
Substrates: high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position Products: -
Substrates: protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed Products: -
Substrates: protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed Products: -
Substrates: protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed Products: -
Substrates: protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed Products: -
x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE
x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE
x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE
Dib, R.; Chobert, J.M.; Dalgalarrondo, M.; Barbier, G.; Haertle, T.
Purification, molecular properties and specificity of a thermoactive and thermostable proteinase from Pyrococcus abyssi, strain st 549, hyperthermophilic archaea from deep-sea hydrothermal ecosystem
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