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Literature summary for 3.2.1.20 extracted from

  • Paul, S.; Chaudhuri, T. K.
    Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coli (2008), J. Appl. Microbiol., 104, 35-41.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli DH5 alpha Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
69000
-
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P21517
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
aggregation of maltodextrin glucosidase in the cytoplasm is partially prevented by the co-expression of GroEL and GroES, and using externally supplemented glycerol or lowering the culture temperature. Co-expression of GroEL and GroES or simultaneous presence of overexpressed GroEL, GroES and externally supplemented glycerol together results significant increase of the activity of maltodextrin glucosidase Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl-alpha-D-maltoside + H2O
-
Escherichia coli p-nitrophenol + alpha-D-maltose
-
?

Synonyms

Synonyms Comment Organism
maltodextrin glucosidase
-
Escherichia coli
MalZ
-
Escherichia coli