|Gene:||treS||Accession Number: G-4281 (MetaCyc)|
Species: Pimelobacter sp. R48
The trehalose synthase from Pimelobacter sp. R48 is the first enzyme that catalyzes the conversion of maltose to trehalose to be isolated. The purified enzyme converted maltose into trehalose and trehalose into maltose, and released a small amount of glucose from both substrates. It was inactive with all other saccharides tested. The equilibrium of this reaction lied far in the direction of trehalose synthesis.
Gene Citations: [Tsusaki96]
Molecular Weight of Polypeptide: 62 kD (experimental) [Nishimoto96a ]
pI: 4.6 [Nishimoto96a]
Relationship Links: CAZy:IN-FAMILY:GH13 , Entrez-Nucleotide:PART-OF:D78198 , InterPro:IN-FAMILY:IPR006047 , InterPro:IN-FAMILY:IPR006589 , InterPro:IN-FAMILY:IPR012810 , InterPro:IN-FAMILY:IPR013780 , InterPro:IN-FAMILY:IPR013781 , InterPro:IN-FAMILY:IPR015902 , InterPro:IN-FAMILY:IPR017853 , Panther:IN-FAMILY:PTHR10357 , Pfam:IN-FAMILY:PF00128 , Smart:IN-FAMILY:SM00642
|MultiFun Terms:||metabolism → biosynthesis of building blocks|
Enzymatic reaction of: trehalose synthase
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
This reaction is reversible.
In Pathways: trehalose biosynthesis IV
T(opt): 20 °C [Nishimoto96a]
pH(opt): 7.5 [Nishimoto96a]
Nishimoto96a: Nishimoto T, Nakano M, Nakada T, Chaen H, Fukuda S, Sugimoto T, Kurimoto M, Tsujisaka Y (1996). "Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48." Biosci Biotechnol Biochem 60(4);640-4. PMID: 8829531
Tsusaki96: Tsusaki K, Nishimoto T, Nakada T, Kubota M, Chaen H, Sugimoto T, Kurimoto M (1996). "Cloning and sequencing of trehalose synthase gene from Pimelobacter sp. R48." Biochim Biophys Acta 1290(1);1-3. PMID: 8645698
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493