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Literature summary for 3.1.3.2 extracted from

  • Vogel, A.; Borchers, T.; Marcus, K.; Meyer, H.E.; Krebs, B.; Spener, F.
    Heterologous expression and characterization of recombinant purple acid phosphatase from red kidney bean (2002), Arch. Biochem. Biophys., 401, 164-172.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in High Five insect cells Phaseolus vulgaris

Inhibitors

Inhibitors Comment Organism Structure
H2O2 native and recombinant enzyme Phaseolus vulgaris

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ native enzyme with an iron-zinc center is not activated upon reduction of the enzyme with ferrous ions and ascorbate, but the activity of recombinant enzyme is increased about 4fold Phaseolus vulgaris
Iron native enzyme with an iron-zinc center is not activated upon reduction of the enzyme with ferrous ions and ascorbate, but the activity of recombinant enzyme is increased about 4fold Phaseolus vulgaris
Zinc native enzyme with an iron-zinc center is not activated upon reduction of the enzyme with ferrous ions and ascorbate, but the activity of recombinant enzyme is increased about 4fold Phaseolus vulgaris

Organism

Organism UniProt Comment Textmining
Phaseolus vulgaris O24319
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme contains five N-linked glycosylation sites at Asn81, Asn109, Asn143, Asn211 and Asn396 Phaseolus vulgaris

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Phaseolus vulgaris

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
265.8
-
-
Phaseolus vulgaris

Synonyms

Synonyms Comment Organism
kbPAP
-
Phaseolus vulgaris
purple acid phosphatase
-
Phaseolus vulgaris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1
-
native and recombinant enzyme Phaseolus vulgaris