TET2 peptidase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.11 Aminopeptidases > 3.4.11.B9 TET2 peptidase
TET2 peptidase is a Pyrococcus horikoshii exopeptidase that functions as an aminopeptidase with a clear preference for leucine as the N-terminal amino acid, but can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner; it has neither carboxypeptidase nor endoproteolytic activity and is devoid of N-terminal deblocking activity, and is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids. By breaking proteasome-derived oligopeptides down to amino acids it completes archaeal protein turnover. It is taxonomically restricted to Pyrococcus horikoshii.
TET2 peptidase is a Pyrococcus horikoshii exopeptidase that functions as an aminopeptidase with a clear preference for leucine as the N-terminal amino acid, but can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner; it has neither carboxypeptidase nor endoproteolytic activity and is devoid of N-terminal deblocking activity, and is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids. By breaking proteasome-derived oligopeptides down to amino acids it completes archaeal protein turnover. It is taxonomically restricted to Pyrococcus horikoshii.
References:
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