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Results 1 - 10 of 13 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8more PhTET1 activity cannot be detected by using chromogenic aminoacyl compounds (7-amino-4-methylcoumarin (AMC) or p-nitroanilide), probably because the X-AMC and X-4-nitroanilide molecules cannot fit into the active site pocket or because these compounds fit but are not hydrolyzed. HPLC analysis of Ala-Ala-p-nitroanilide degradation by the two PhTET1 oligomers shows that the generation of Ala-4-nitroanilide is not linear with time, suggesting product inhibition. PhTET1 can cleave the N-terminal amino acid of larger peptides, even when the 4-nitroanilide moiety is in the C-terminal position, and can also hydrolyze dipeptides like Ala-Ala or Asp-Ala. Therefore, PhTET1 seems to be unable to cleave a peptidic bond when 4-nitroanilide or 7-amino-4-methylcoumarin is in the P1' position, making activity assays difficult. Activity of the dodecamer enzyme form increases with substrate chain length. No hydrolytic activity toward N-acetyl-Leu-4-nitroanilide and N-succinyl-Ala-Ala 4-nitroanilide Pyrococcus horikoshii ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8more PhTET1 activity cannot be detected by using chromogenic aminoacyl compounds (7-amino-4-methylcoumarin (AMC) or p-nitroanilide), probably because the X-AMC and X-4-nitroanilide molecules cannot fit into the active site pocket or because these compounds fit but are not hydrolyzed. HPLC analysis of Ala-Ala-p-nitroanilide degradation by the two PhTET1 oligomers shows that the generation of Ala-4-nitroanilide is not linear with time, suggesting product inhibition. PhTET1 can cleave the N-terminal amino acid of larger peptides, even when the 4-nitroanilide moiety is in the C-terminal position, and can also hydrolyze dipeptides like Ala-Ala or Asp-Ala. Therefore, PhTET1 seems to be unable to cleave a peptidic bond when 4-nitroanilide or 7-amino-4-methylcoumarin is in the P1' position, making activity assays difficult. Activity of the dodecamer enzyme form increases with substrate chain length. No hydrolytic activity toward N-acetyl-Leu-4-nitroanilide and N-succinyl-Ala-Ala 4-nitroanilide Pyrococcus horikoshii OT-3 ? - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala + H2O - Pyrococcus horikoshii Ala + Ala - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala + H2O - Pyrococcus horikoshii OT-3 Ala + Ala - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala 4-nitroanilide + H2O the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide Pyrococcus horikoshii Ala + Ala 4-nitroanilide - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala-Ala 4-nitroanilide + H2O best substraet for the dodecameric form of the enzyme Pyrococcus horikoshii Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala-Ala 4-nitroanilide + H2O best substrat for the dodecameric form of the enzyme Pyrococcus horikoshii Ala + Ala 4-nitroanilide + Ala-Ala 4-nitroanilide - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala-Ala + H2O the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide Pyrococcus horikoshii Ala + Ala-Ala - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala-Ala + H2O the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala-4-nitroanilide Pyrococcus horikoshii Ala + Ala-Ala - ?
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.B8Ala-Ala-Ala + H2O the tetracosameric complex shows maximal activity against Ala-Ala-Ala and Ala-Ala 4-nitroanilide Pyrococcus horikoshii OT-3 Ala + Ala-Ala - ?
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