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Literature summary for 3.4.11.9 extracted from

  • Juarez-Montiel, M.; Ibarra, J.A.; Chavez-Camarillo, G.; Hernandez-Rodriguez, C.; Villa-Tanaca, L.
    Molecular cloning and heterologous expression in Pichia pastoris of X-prolyl-dipeptidyl aminopeptidase from basidiomycete Ustilago maydis (2014), Appl. Biochem. Biotechnol., 172, 2530-2539.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris Ustilago maydis

Inhibitors

Inhibitors Comment Organism Structure
pefabloc
-
Ustilago maydis
phenylmethylsulfonyl fluoride
-
Ustilago maydis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
125000
-
SDS-PAGE Ustilago maydis

Organism

Organism UniProt Comment Textmining
Ustilago maydis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA affinity chromatography Ustilago maydis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Pro-4-nitroanilide + H2O
-
Ustilago maydis Ala + Pro-4-nitroanilide
-
?

Synonyms

Synonyms Comment Organism
dapUm
-
Ustilago maydis
X-prolyl-dipeptidyl aminopeptidase
-
Ustilago maydis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
recombinant protein Ustilago maydis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5 40 stable for 60 min Ustilago maydis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.9
-
native protein Ustilago maydis
7
-
recombinant protein Ustilago maydis