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Literature summary for 3.2.1.14 extracted from

  • Patel, A.; Singh, V.; Yadav, R.; Moir, A.; Jagannadham, M.
    Purification and characterization of a new chitinase from latex of Ipomoea carnea (2010), Process Biochem., 45, 675-681.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
allosamidin 0.05 mM, 0.8% residual activity Ipomoea carnea
Hg2+ 0.1 mM, 4% residual activity Ipomoea carnea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30060
-
x * 30060, MALDI-TOF Ipomoea carnea

Organism

Organism UniProt Comment Textmining
Ipomoea carnea
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 5-6% glycocontent Ipomoea carnea

Purification (Commentary)

Purification (Comment) Organism
-
Ipomoea carnea

Source Tissue

Source Tissue Comment Organism Textmining
latex
-
Ipomoea carnea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycol chitin + H2O
-
Ipomoea carnea ?
-
?

Subunits

Subunits Comment Organism
? x * 30060, MALDI-TOF Ipomoea carnea

Synonyms

Synonyms Comment Organism
chitinase II
-
Ipomoea carnea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Ipomoea carnea

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
stable up to Ipomoea carnea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Ipomoea carnea

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 9.5
-
Ipomoea carnea

pI Value

Organism Comment pI Value Maximum pI Value
Ipomoea carnea isoelectric focusing
-
4.6