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

BRENDA support

Literature summary for 1.14.18.1 extracted from

  • Chevalier, T.; de Rigal, D.; Mbeguie-A-Mbeguie, D.; Gauillard, F.; Richard.Forget, F.; Fils-Lycaon, B.R.
    Molecular cloning and characterization of apricot fruit polyphenol oxidase (1999), Plant Physiol., 119, 1261-1269.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloning of cDNA Prunus armeniaca

Metals/Ions

Metals/Ions Comment Organism Structure
copper enzyme contains 2 copper-binding domains Prunus armeniaca

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56200
-
x * 56200, mature enzyme, deduced from amino acid sequence Prunus armeniaca

Organism

Organism UniProt Comment Textmining
Prunus armeniaca
-
apricot, var Bergeron
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein enzyme contains 1 putative glycosylation site Prunus armeniaca

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfat, Phenyl Sepharose, DEAE-Sepharose Prunus armeniaca

Source Tissue

Source Tissue Comment Organism Textmining
fruit expressed at the immature-green stage of fruit development Prunus armeniaca
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3432
-
-
Prunus armeniaca

Subunits

Subunits Comment Organism
? x * 56200, mature enzyme, deduced from amino acid sequence Prunus armeniaca