Note: a dashed line (without arrowheads) between two compound names is meant to imply that the two names are just different instantiations of the same compound -- i.e. one may be a specific name and the other a general name, or they may both represent the same compound in different stages of a polymerization-type pathway. This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Degradation/Utilization/Assimilation → Protein Degradation|
Expected Taxonomic Range: Viridiplantae
Wound-induction in plants results in a cascade of pathways that are triggered as defense response. These protease-controlled pathways are critical for plant development and stress response. The role of the Ubiquitin-mediated proteolysis events in wound and defense response is suggested by the up-regulation of genes encoding a ubiquitin in response to infection [Gu99].
Peptidases such as aminopeptidases, carboxypeptidases, endo and exopeptidases occur in response to wound induction and as a defense response. The turnover of mis-folded or damaged proteins that accumulate as a result of oxidative burst associated with wound response, would require recycling by the action of these peptidases [Gu96].
Lap -A is found only in a few Solanaceae members and has acidic pI. Two alleles are known (LAP-A1 and LAP-A2), both of which are expressed during flower and fruit development. Lap A was shown to accumulate in response to wound induction [NarvaezVasquez08], Pseudomonas syringae pv. tomato infection, and Phytophthora parasitica infection [Tu03].
Gu99: Gu YQ, Holzer FM, Walling LL (1999). "Overexpression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato." Eur J Biochem 263(3);726-35. PMID: 10469136
Josch03: Josch C, Klotz LO, Sies H (2003). "Identification of cytosolic leucyl aminopeptidase (EC 126.96.36.199) as the major cysteinylglycine-hydrolysing activity in rat liver." Biol Chem 384(2);213-8. PMID: 12675513
McCulloch94: McCulloch R, Burke ME, Sherratt DJ (1994). "Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination." Mol Microbiol 12(2);241-51. PMID: 8057849
Strater99: Strater N, Sun L, Kantrowitz ER, Lipscomb WN (1999). "A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase." Proc Natl Acad Sci U S A 96(20);11151-5. PMID: 10500145
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