3.4.24.70: oligopeptidase A
This is an abbreviated version!
For detailed information about oligopeptidase A, go to the full flat file.
Word Map on EC 3.4.24.70
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3.4.24.70
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prolyl
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typhimurium
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dipeptidyl
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carboxypeptidase
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neuropeptides
-
endopeptidases
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oxyanion
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subtilisin
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octapeptide
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post-proline
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thimet
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neurolysin
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z-pro-prolinal
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bell-shaped
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product-like
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scissile
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3.4.24.15
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arrhenius
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metallopeptidase
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bradykinin
- 3.4.24.70
-
prolyl
- typhimurium
-
dipeptidyl
- carboxypeptidase
- neuropeptides
- endopeptidases
-
oxyanion
- subtilisin
- octapeptide
-
post-proline
-
thimet
- neurolysin
- z-pro-prolinal
-
bell-shaped
-
product-like
-
scissile
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3.4.24.15
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arrhenius
- metallopeptidase
- bradykinin
Reaction
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but additional information distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5 =
Synonyms
68000-M Signalpeptide hydrolase, More, oligopeptidase A, OpdA, prlC, TOP, Top1, Top2
ECTree
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Engineering
Engineering on EC 3.4.24.70 - oligopeptidase A
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Y607A
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the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme
Y607F
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the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme
additional information
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supressors of the protein-localization defect conferred by certain signal sequence mutations