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Literature summary for 3.2.1.28 extracted from

  • Mori, H.; Lee, J.H.; Okuyama, M.; Nishimoto, M.; Ohguchi, M.; Kim, D.; Kimura, A.; Chiba, S.
    Catalytic reaction mechanism based on alpha-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase (2009), Biosci. Biotechnol. Biochem., 73, 2466-2473.
    View publication on PubMed
Search for more literature for 3.2.1.28

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha,alpha-trehalose + H2O Apis mellifera the enzyme, an anomer-inverting glycosylase, hydrolyzes alpha,alpha-trehalase to equimolar amounts of alpha- and beta-D-glucose. It is also capable of synthesizing trehalose from D-glucose in the reverse reaction alpha-D-glucose + beta-D-glucose
-
 r

Organism

Organism UniProt Comment Textmining
Apis mellifera
-
-
-

Reaction

Reaction Comment Organism Reaction ID
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose nucleophilic double, not single, displacement catalytic forward reaction mechanism via oxocarbenium ion intermediate, detailed overview Apis mellifera
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha,alpha-trehalose + H2O
-
 Apis mellifera alpha-D-glucose + beta-D-glucose
-
 r
alpha,alpha-trehalose + H2O the enzyme, an anomer-inverting glycosylase, hydrolyzes alpha,alpha-trehalase to equimolar amounts of alpha- and beta-D-glucose. It is also capable of synthesizing trehalose from D-glucose in the reverse reaction Apis mellifera alpha-D-glucose + beta-D-glucose
-
 r

Synonyms

Synonyms Comment Organism
trehalase
-
 Apis mellifera

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 assay at Apis mellifera

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 assay at Apis mellifera