MetaCyc Enzyme: trehalose synthase

Gene: treS Accession Number: G-4681 (MetaCyc)

Species: Thermus aquaticus

A thermostable trehalose synthase was isolated from T. aquaticus, that was stable from pH 9.5 and up to 80oC for 60 minutes. The yield of trehalose from maltose was independent of the substrate concentration, and was higher at lower temperatures. Maximum yield reached 82% at 30-40oC [Nishimoto96].

Gene Citations: [Tsusaki97]

Molecular Weight of Polypeptide: 105 kD (experimental) [Nishimoto96 ]

pI: 4.6 [Nishimoto96]

Relationship Links: CAZy:IN-FAMILY:GH13 , Entrez-Nucleotide:PART-OF:D86216

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

MultiFun Terms: metabolism carbon utilization carbon compounds

Enzymatic reaction of: trehalose synthase

EC Number:

maltose <=> α,α-trehalose

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: trehalose biosynthesis IV

Inhibitors (Unknown Mechanism): Cu2+ [Nishimoto96] , Hg2+ [Nishimoto96] , Zn2+ [Nishimoto96] , tris [Nishimoto96]

T(opt): 65 °C [Nishimoto96]

pH(opt): 6.5 [Nishimoto96]


Nishimoto96: Nishimoto, T., Nakada, T., Chaen, H., Fukuda, S., Sugimoto, T., Kurimoto, M., Tsujisaka, Y. (1996). "Purification and characterization of a thermostable trehalose synthase from Thermus aquaticus." Biosci. Biotech. Biochem. 60(5):835-839.

Tsusaki97: Tsusaki K, Nishimoto T, Nakada T, Kubota M, Chaen H, Fukuda S, Sugimoto T, Kurimoto M (1997). "Cloning and sequencing of trehalose synthase gene from Thermus aquaticus ATCC33923." Biochim Biophys Acta 1334(1);28-32. PMID: 9042362

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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