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Literature summary extracted from

  • Uhland, K.; Mondigler, M.; Spiess, C.; Prinz, W.; Ehrmann, M.
    Determinants of translocation and folding of TreF, a trehalase of Escherichia coli (2000), J. Biol. Chem., 275, 23439-23445.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.28 additional information enzymatic activity of TreA/TreF hybrids Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.28 0.16
-
 alpha,alpha-trehalose signal sequenceless TreA Escherichia coli
3.2.1.28 0.31
-
 alpha,alpha-trehalose periplasmic TreA Escherichia coli
3.2.1.28 1.5
-
 alpha,alpha-trehalose cytoplsmic wild-type treF Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.28 cytoplasm TreF. TreF can be exported to the periplasm where it is present in a misfolded and inactive form Escherichia coli 5737
-
3.2.1.28 periplasm TreA. TrA can fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence Escherichia coli
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.28 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.28 alpha,alpha-trehalose + H2O
-
 Escherichia coli alpha-D-glucopyranose + D-glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.28 More TrA can fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.2.1.28 TreA
-
 Escherichia coli
3.2.1.28 TreF
-
 Escherichia coli