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Literature summary for 3.4.11.1 extracted from

  • Ogiwara, N.; Amano, T.; Satoh, M.; Shioi, Y.
    Leucine aminopeptidase from etiolated barley seedlings: characterization and partial purification of isoforms (2005), Plant Sci., 168, 575-581.
    View publication on PubMed
Search for more literature for 3.4.11.1

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate inhibition of isozymes LAP1, LAP2, and LAP3 Hordeum vulgare

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
 1 * 57000, isozymes LAP1, LAP2, and LAP3 Hordeum vulgare

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
 three isozymes LAP1, LAP2, and LAP3
-

Purification (Commentary)

Purification (Comment) Organism
partial purification of isozymes from etiolated seedlings Hordeum vulgare

Source Tissue

Source Tissue Comment Organism Textmining
coleoptile
-
 Hordeum vulgare
-
leaf
-
 Hordeum vulgare
-
root
-
 Hordeum vulgare
-
seedling etiolated and green Hordeum vulgare
-

Subunits

Subunits Comment Organism
monomer 1 * 57000, isozymes LAP1, LAP2, and LAP3 Hordeum vulgare

Synonyms

Synonyms Comment Organism
LAP
-
 Hordeum vulgare
leucine aminopeptidase
-
 Hordeum vulgare

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
51
-
 50% remainin activity, isozyme LAP1 Hordeum vulgare
54
-
 50% remainin activity, isozyme LAP2 Hordeum vulgare
56
-
 50% remainin activity, isozyme LAP3 Hordeum vulgare

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 isozymes LAP1 and LAP2 Hordeum vulgare
8
-
 isozyme LAP3 Hordeum vulgare