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Literature summary for 3.1.3.12 extracted from

  • Avonce, N.; Wuyts, J.; Verschooten, K.; Vandesteene, L.; Van Dijck, P.
    The Cytophaga hutchinsonii ChTPSP: First characterized bifunctional TPS-TPP protein as putative ancestor of all eukaryotic trehalose biosynthesis proteins (2010), Mol. Biol. Evol., 27, 359-369.
    View publication on PubMed
Search for more literature for 3.1.3.12

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae Ostreococcus tauri

Organism

Organism UniProt Comment Textmining
Cytophaga hutchinsonii
-
-
-
Ostreococcus tauri
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 trehalose-6-phosphate phosphatase activity is 30fold higher compared to the corresponding yeast enzyme Cytophaga hutchinsonii

Synonyms

Synonyms Comment Organism
ChTPSP bifunctional enzyme Cytophaga hutchinsonii
OtTPPA
-
 Ostreococcus tauri
RfTPP
-
 Ostreococcus tauri
trehalose 6-phosphate phosphatase
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 Cytophaga hutchinsonii
trehalose 6-phosphate phosphatase
-
 Ostreococcus tauri

General Information

General Information Comment Organism
malfunction complementation assays using different yeast mutants show that ChTPSP possesses trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase activities Cytophaga hutchinsonii
physiological function OtTPPA is approximately 100fold more active than the protein of Arabidopsis thaliana Ostreococcus tauri
physiological function RfTPP is approximately 100fold more active than the protein of Arabidopsis thaliana Ostreococcus tauri