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
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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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results (General Information
General Information on EC 3.4.24.70 - oligopeptidase A
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
plants with defective enzyme expression exhibit heightened resistance to exogenous salicylate treatment
metabolism
isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death. TOP1 and TOP2 expression are coordinately regulated during pathogen-associated molecular pattern-triggered plant immunity
physiological function
evolution
the TOP isozymes contain the conserved His-Glu-XX-His (HEXXH) sequence of active-site residues and belong to the M3 family of metallopeptidases
evolution
the TOP isozymes contain the conserved His-Glu-XX-His (HEXXH) sequence of active-site residues and belong to the M3 family of metallopeptidases. TOP1 and TOP2 are located on opposite ends of chromosome 5 and share high homology, indicating the occurrence of a past intra-chromosomal duplication event
physiological function
the enzyme is a target for salicylic acid binding and participate in SA-mediated plant innate immunity. Both isozymes TOP1 and TOP2 seem to play a role in salicylic acid-dependent innate immunity, but through independent pathways
physiological function
the enzyme is a target for salicylic acid binding and participate in SA-mediated plant innate immunity. Both isozymes TOP1 and TOP2 seem to play a role in salicylic acid-dependent innate immunity, they are necessary for the immune response to avirulent pathogens. Isozyme TOP1 induces the augmentation of expression of isozyme TOP2 by the flagellin peptide flg22. Isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death
physiological function
the enzyme is a target for salicylic acid binding and participate in SA-mediated plant innate immunity. Both isozymes TOP1 and TOP2 seem to play a role in salicylic acid-dependent innate immunity, they are necessary for the immune response to avirulent pathogens. Isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death
