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Literature summary for 3.2.1.28 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
Search for more literature for 3.2.1.28

Protein Variants

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm TreF. TreF can be exported to the periplasm where it is present in a misfolded and inactive form Escherichia coli 5737
-
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
TreA
-
 Escherichia coli
TreF
-
 Escherichia coli