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Literature summary for 5.4.99.16 extracted from

  • Nishimoto, T.; Nakano, M.; Nakada, T.; Chaen, H.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.
    Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48 (1996), Biosci. Biotechnol. Biochem., 60, 640-644.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Pimelobacter sp.
Hg2+
-
Pimelobacter sp.
Ni2+
-
Pimelobacter sp.
Tris
-
Pimelobacter sp.
Zn2+
-
Pimelobacter sp.

Organism

Organism UniProt Comment Textmining
Pimelobacter sp.
-
-
-
Pimelobacter sp. R48
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pimelobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltose r Pimelobacter sp. alpha,alpha-trehalose
-
?
maltose r Pimelobacter sp. R48 alpha,alpha-trehalose
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
-
Pimelobacter sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
pH 7.0, 60 min, stable up to Pimelobacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Pimelobacter sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 20°C, 60 min, stable Pimelobacter sp.