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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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MetaCyc Pathway: wound-induced proteolysis I

Enzyme View:

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

Some taxa known to possess this pathway include ? : Solanum lycopersicum , Solanum tuberosum

Expected Taxonomic Range: Viridiplantae

Summary:
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].

Solanum lycopersicum plants express four classes of Leucine Aminopeptidase (LAP)-related proteins - two LAP-like proteins with molecular weights 66 kDa and 77 kDa, Lap-A and Lap-N [Chao00].

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].

Credits:
Created 31-Jul-2008 by Pujar A , Cornell University


References

Chao00: Chao WS, Pautot V, Holzer FM, Walling LL (2000). "Leucine aminopeptidases: the ubiquity of LAP-N and the specificity of LAP-A." Planta 210(4);563-73. PMID: 10787049

Gu96: Gu YQ, Chao WS, Walling LL (1996). "Localization and post-translational processing of the wound-induced leucine aminopeptidase proteins of tomato." J Biol Chem 271(42);25880-7. PMID: 8824220

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

NarvaezVasquez08: Narvaez-Vasquez J, Tu CJ, Park SY, Walling LL (2008). "Targeting and localization of wound-inducible leucine aminopeptidase A in tomato leaves." Planta 227(2);341-51. PMID: 17896114

Tu03: Tu CJ, Park SY, Walling LL (2003). "Isolation and characterization of the neutral leucine aminopeptidase (LapN) of tomato." Plant Physiol 132(1);243-55. PMID: 12746529

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Hiroi92: Hiroi Y, Endo Y, Natori Y (1992). "Purification and properties of an aminopeptidase from rat-liver cytosol." Arch Biochem Biophys 294(2);440-5. PMID: 1314542

Josch03: Josch C, Klotz LO, Sies H (2003). "Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver." Biol Chem 384(2);213-8. PMID: 12675513

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Sopanen75: Sopanen T, Mikola J (1975). "Purification and Partial Characterization of Barley Leucine Aminopeptidase." Plant Physiol 55(5);809-814. PMID: 16659173

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

Taylor93: Taylor A (1993). "Aminopeptidases: structure and function." FASEB J 7(2);290-8. PMID: 8440407


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13B.