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Results 1 - 10 of 252 > >>
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
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specific for N-terminal acylmethionine residues
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rapid removal of acetyl-Thr, acetyl-Ala, acetyl-Met, acetyl-Ser and more slowly acetyl-Gly from peptides of different lengths. Other N-acetylated amino acids, Cys, Tyr, Asp, Val, Phe, Ile, Leu, may be removed at 1% or less of the rate of the good substrates
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the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme
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N-acetylated peptides with D-Ala in position 3 or 4 as are good substrates as those containing L-Ala. Peptides with Pro in position 2 are inactive, and most of the peptides with Pro in the third position are very good substrates. Only the peptide acetyl-AAP gives 30% of the activity of acetyl-AAA, which is reduced to 1-2% if additional residues are present at the C-terminus, acety-AAPA or acetyl-AAPAA. The presence of a positive charge in position 2,3,4,5 and 6 gives strong reduction in hydrolase activity, varying with the charge's distance from the N-terminus from 9 to 15-20% of the rate obtained with the reference peptides without positive charges. Deprotonation of His at high pH generates excellent substrates, and removal of the positive charges of Lys by acetylation or succinylation give improved substrate quality. Long peptides with 10-29 residues, are poor substrates, especially when they contain positive charges and Pro
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peptidase activity is only exerted on peptides with Gly or Ala at their N-termini
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the enzyme might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins
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the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
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His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
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catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
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cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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Results 1 - 10 of 252 > >>