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Literature summary extracted from

  • Liu, J.H.; Shang, X.D.; Liu, J.Y.; Tan, Q.
    Changes in trehalose content, enzyme activity and gene expression related to trehalose metabolism in Flammulina velutipes under heat shock (2016), Microbiology, 162, 1274-1285 .
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.231 Flammulina velutipes A0A0G2SWS6
-
-
2.4.1.231 Flammulina velutipes A0A0G2SWS6 bifunctional trehalose synthase/trehalose phosphorylase
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.231 fruit body
-
 Flammulina velutipes
-
2.4.1.231 mycelium
-
 Flammulina velutipes
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.231 alpha,alpha-trehalose + phosphate
-
 Flammulina velutipes alpha-D-glucose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.231 alpha-D-glucose + alpha-D-glucose 1-phosphate
-
 Flammulina velutipes alpha,alpha-trehalose + phosphate
-
 r

General Information

EC Number General Information Comment Organism
2.4.1.231 physiological function heat shock can induce a stress response in the mycelia through the regulation of genes related to trehalose metabolism and the subsequent promotion and control of the transcription and translation of enzymes. The degradation of trehalose is stronger than its synthesis under heat stress Flammulina velutipes
2.4.1.231 physiological function intracellular trehalose significantly accumulates in the mycelia in response to 37 °C heat shock. For the trehalose phosphorylase, the degradation of trehalose is stronger than its synthesis under heat stress Flammulina velutipes