Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.22 extracted from

  • Moosavi-Movahedi, A.A.; Amani, M.; Moosavi-Nejad, S.Z.; Hashemnia, S.; Ahmad, F.; Floris, G.; Mura, A.; Rezaei-Tavirani, M.; Hakimelahi, G.H.; Saboury, A.A.; Yousefi, R.
    Thermal dissection of lentil seedling amine oxidase domains by differential scanning calorimetry (2007), Biosci. Biotechnol. Biochem., 71, 1644-1649.
    View publication on PubMed
Search for more literature for 1.4.3.22

Inhibitors

Inhibitors Comment Organism Structure
aminoguanidine
-
 Lens culinaris

Organism

Organism UniProt Comment Textmining
Lens culinaris
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein deglycosylation has no effect on the thermal stability of the enzyme Lens culinaris

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
 Lens culinaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
putrescine + H2O + O2
-
 Lens culinaris ?
-
 ?

Synonyms

Synonyms Comment Organism
LSAO
-
 Lens culinaris

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 deglycosylation has no effect on the thermal stability of the enzyme. Aminoguanidine raises the stability of the protein Lens culinaris
65
-
 Tm-value of native enzyme Lens culinaris
69
-
 Tm-value of aminoguanidine-inhibited enzyme Lens culinaris