Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.14.18.1	cloning of cDNA	Prunus armeniaca

Metals/Ions

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

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.14.18.1	56200	-	x * 56200, mature enzyme, deduced from amino acid sequence	Prunus armeniaca

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.18.1	Prunus armeniaca	-	apricot, var Bergeron	-

Posttranslational Modification

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

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.14.18.1	3432	-	-	Prunus armeniaca

Subunits

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

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Release 2023.1 (January 2023)