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alpha,alpha-trehalose + H2O
2 D-glucopyranose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
alpha,alpha-trehalose + H2O
alpha-D-glucose + beta-D-glucose
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
alpha-alpha-trehalose + H2O
D-glucose
-
-
-
-
?
cellobiose + H2O
2 D-glucose
-
-
-
-
?
isomaltose + H2O
alpha-D-glucopyranose
-
-
-
-
?
maltose + H2O
2 D-glucose
maltose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
melibiose + H2O
D-glucose + D-galactose
-
-
-
-
?
melizitose + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
-
weak
-
-
?
raffinose + H2O
?
-
-
-
-
?
sucrose + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
trehalose + H2O
2 D-glucose
trehalose + H2O
D-glucose
additional information
?
-
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is involved in incorporation and utilization of trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is essential for growth on trehalose as carbon source, regulation by D-glucose repression
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
highly specific for alpha,alpha-trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
highly specific for alpha,alpha-trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
both isoforms are highly specific for trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
preferred substrate of acid trehalase
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the acid trehalase is involved in catabolism of trehalose by export of the disaccharide, extracellular hydrolysis, and subsequent uptake of released D-glucose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
trehalose is one of the major storage carbohydrates in the yeast Saccharomyces cerevisiae
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
spores contain neutral and acid trehalase. Lack of neutral trehalase severely reduces spore germination in fission yeast and sporulation-specific acid trehalase somehow participates in the degradation of endogenous trehalose in the ansence of neutral trehalase, thus playing an ancillary role during germination
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
Thermochaetoides thermophila
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
highly specific for
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
inverting-type enzyme
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
may play a role in the regulating the carbohydrate allocation in plants
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
neutral trehalase mobilizes trehalose accumulated by fungal cells as a protective and storage carbohydrate
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucose + beta-D-glucose
-
-
-
-
r
alpha,alpha-trehalose + H2O
alpha-D-glucose + beta-D-glucose
-
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
-
-
r
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of exogenous trehalose
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of exogenous trehalose
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
trehalase is an indispensable component of insect hemolymph that plays important role in energy metabolism and stress resistance
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
trehalase is an indispensable component of insect hemolymph that plays important role in energy metabolism and stress resistance
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of intracellular trehalose in response to physiological stimuli
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of intracellular trehalose in response to physiological stimuli
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
1.7% of the activity with trehalose
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
5.7% of the activity with trehalose
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
absolute specificity
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
pathway of trehalose utilization
-
?
trehalose + H2O
D-glucose
-
osmotically inducible enzyme
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
Lobosphaera sp.
-
-
-
?
trehalose + H2O
D-glucose
high specificity for trehalose
-
-
?
trehalose + H2O
D-glucose
highly specific for trehalose
-
-
?
trehalose + H2O
D-glucose
-
absolute specificity
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
absolute specificity
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
high specificity for trehalose
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
the trehalase is strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. The enzyme may be present in a constitutive form without the requirement for a specific inducer
-
?
trehalose + H2O
D-glucose
-
absolute specificity
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
absolute specificity
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
Thermochaetoides thermophila
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
?
trehalose + H2O
D-glucose
-
absolute specificity
-
?
trehalose + H2O
D-glucose
-
-
-
?
additional information
?
-
-
no activity with alpha,beta-trehalose and 6-beta-glucosyl-trehalose
-
-
?
additional information
?
-
no substrate: fructose, mannitol and sorbitol
-
-
?
additional information
?
-
-
no substrate: fructose, mannitol and sorbitol
-
-
?
additional information
?
-
-
no substrate: maltose, isomaltose, laminaribiose, cellobiose, sucrose, lactose
-
-
?
additional information
?
-
-
very poor substrates: lactose 0.1%, sucrose 0.08%, cellobiose 0.05%, maltose 0% and raffinose 0.9% of activity against trehalose, respectively
-
-
?
additional information
?
-
-
trehalose-invertase is specific for both sucrose and trehalose. The ratio between trehalase and invertase activity is 1:3.5
-
-
?
additional information
?
-
-
human trehalase Treh acts as a stress-response protein in the kidney rather than being involved in utilization of exogenous trehalose
-
-
?
additional information
?
-
does not hydrolyze cellobiose, maltose, sucrose, lactose, p-nitrophenyl galactopyranoside, p-nitrophenyl alpha-glucopyranoside, or p-nitrophenyl beta-glucopyranoside
-
-
?
additional information
?
-
-
does not hydrolyze cellobiose, maltose, sucrose, lactose, p-nitrophenyl galactopyranoside, p-nitrophenyl alpha-glucopyranoside, or p-nitrophenyl beta-glucopyranoside
-
-
?
additional information
?
-
-
both normal and glucocorticoid-induced maturation of the trehalase expression reflects transcriptional activation. The slow time course of the glucocorticoid effect suggests that trehalase may not be a primary response gene
-
-
?
additional information
?
-
-
does not hydrolyze alpha,beta-trehalose, beta,beta-trehalose, trehalose dimycolate, or any other alpha-glucoside or beta-glucoside
-
-
?
additional information
?
-
-
does not hydrolyze alpha,beta-trehalose, beta,beta-trehalose, trehalose dimycolate, or any other alpha-glucoside or beta-glucoside
-
-
?
additional information
?
-
enzyme is absolutely specific for trehalose
-
-
?
additional information
?
-
-
enzyme is absolutely specific for trehalose
-
-
?
additional information
?
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
-
no activity of acid trehalase with lactose and turanose
-
-
?
additional information
?
-
-
role of acid trehalase Ath1 in intracellular trehalose mobilization and in saline stress resistance
-
-
?
additional information
?
-
-
the 131 amino acid N-terminus of Ath1 are sufficient for invertase secretion, and the short transmembrane domain, located at the N-terminus, is indispensable for Ath1 function, overview
-
-
?
additional information
?
-
-
transcriptional and post-translational regulation of neutral trehalase in Schizosaccharomyces pombe during thermal stress
-
-
?
additional information
?
-
the enzyme does not hydrolyze any other trehalose analogs such as maltose, nigerose, and turanose
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze any other trehalose analogs such as maltose, nigerose, and turanose
-
-
?
additional information
?
-
-
no activity with sucrose, maltose, lactose or cellobiose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha,alpha-trehalose + H2O
2 D-glucose
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
alpha,alpha-trehalose + H2O
alpha-D-glucose + beta-D-glucose
-
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
-
-
r
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
trehalose + H2O
2 D-glucose
trehalose + H2O
D-glucose
additional information
?
-
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is involved in incorporation and utilization of trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is essential for growth on trehalose as carbon source, regulation by D-glucose repression
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the acid trehalase is involved in catabolism of trehalose by export of the disaccharide, extracellular hydrolysis, and subsequent uptake of released D-glucose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
trehalose is one of the major storage carbohydrates in the yeast Saccharomyces cerevisiae
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
spores contain neutral and acid trehalase. Lack of neutral trehalase severely reduces spore germination in fission yeast and sporulation-specific acid trehalase somehow participates in the degradation of endogenous trehalose in the ansence of neutral trehalase, thus playing an ancillary role during germination
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
the enzyme is important in insect metabolism with trehalose being the main circulating sugar in the organism with functions in storage, fuel for flight, and as a cryoprotector, in hemolymph trehalose is important for carbohydrate intake and nutritional homeostasis, enzyme deficiency leads to severe metabolic problems
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
Thermochaetoides thermophila
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
may play a role in the regulating the carbohydrate allocation in plants
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
-
neutral trehalase mobilizes trehalose accumulated by fungal cells as a protective and storage carbohydrate
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of exogenous trehalose
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of exogenous trehalose
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
trehalase is an indispensable component of insect hemolymph that plays important role in energy metabolism and stress resistance
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
trehalase is an indispensable component of insect hemolymph that plays important role in energy metabolism and stress resistance
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of intracellular trehalose in response to physiological stimuli
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
hydrolysis of intracellular trehalose in response to physiological stimuli
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
-
?
trehalose + H2O
2 D-glucose
-
-
-
-
?
trehalose + H2O
D-glucose
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
-
?
trehalose + H2O
D-glucose
-
pathway of trehalose utilization
-
?
trehalose + H2O
D-glucose
-
osmotically inducible enzyme
-
?
trehalose + H2O
D-glucose
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
-
the trehalase is strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. The enzyme may be present in a constitutive form without the requirement for a specific inducer
-
?
trehalose + H2O
D-glucose
-
-
-
?
additional information
?
-
-
trehalose-invertase is specific for both sucrose and trehalose. The ratio between trehalase and invertase activity is 1:3.5
-
-
?
additional information
?
-
-
human trehalase Treh acts as a stress-response protein in the kidney rather than being involved in utilization of exogenous trehalose
-
-
?
additional information
?
-
-
both normal and glucocorticoid-induced maturation of the trehalase expression reflects transcriptional activation. The slow time course of the glucocorticoid effect suggests that trehalase may not be a primary response gene
-
-
?
additional information
?
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
-
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
?
additional information
?
-
-
role of acid trehalase Ath1 in intracellular trehalose mobilization and in saline stress resistance
-
-
?
additional information
?
-
-
transcriptional and post-translational regulation of neutral trehalase in Schizosaccharomyces pombe during thermal stress
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
1,3-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)propane-1,3-dione
micromolar inhibitor
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
AlCl3
-
1 mM, complete inhibition
barium ion
Thermochaetoides thermophila
-
1 mM, complete inhibition
Borate
-
16% residual activity at 20 mM
CaCl2
over 90% inhibition at 10 mM
casuarine-6-O-alpha-D-glucoside
Citric acid
-
36.16% residual activity at 5 mM
CuCl2
20 mM, 20% residual activity
CuSO4
-
1 mM, 80% loss of activity
deoxynojirimycin
-
inhibition according to a ligand exclusion model
diethyldicarbonate
the compound modifies a His residue that results in a less active enzyme. After 40 min with 40 mM diethylpyrocarbonate at 30°C pH 6.0, trehalase activity decreases to about 50% of the initial activity
diphosphate
-
more than 50% inhibition at 8 mM and complete inhibition at 16 mM
EGTA
20 mM, 55% residual activity
FeCl3
-
10 mM, 35% inhibition
fructose
-
10 mM, 45% inhibition. Inhibitory effect is abolished by Ca2+
glucono-delta-lactone
linear competitive inhibitor
H2O2
-
inhibitory at 5-50 mM
Hg+
-
inhibits the acid trehalase by 95%
iodoacetamide
-
100 mM required for inhibition of more than 50%
KH2PO4
-
10.32% residual activity at 200 mM
lactose
-
10 mM, 68% inhibition. Inhibitory effect is abolished by Ca2+
Li+
-
12% residual activity at 20 mM
malate
-
37% residual activity at 20 mM
maltose
-
10 mM, 54% inhibition. Inhibitory effect is abolished by Ca2+
methyl beta-glucoside
-
-
methyl-alpha-D-mannoside
linear competitive inhibitor
methyl-alpha-mannoside
-
weak competitive inhibition
MnCl2
over 90% inhibition at 10 mM
NaCl
strong inhibition at 10 mM, treatment of cells leads to accumulation of trehalose
NEM
-
2 mM, 8.4% inhibition
NH4Cl
-
1 mM NH4Cl, 22% inhibition of extracellular enzyme, 27% inhibition of intracellular enzyme
p-aminophenyl-beta-D-glucoside
-
-
p-nitrophenyl-beta-D-glucoside
phenyl-beta-D-glucoside
-
-
potassium glutamate
-
0.5 M KCl, activity is 2fold lower
SDS
-
1.0%, 80% inhibition
sodium orthovanadate
-
80% inhibition at 10 mM
succinate
-
41% residual activity at 20 mM
Urea
-
10 mM, 6% inhibition
UTP
-
90% inhibition at 10 mM
validamycin
-
competitive
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
casuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
casuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
casuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
-
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
-
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
-
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
-
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-homocasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-homocasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-homocasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-deoxycasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-deoxycasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-deoxycasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
1,10-phenanthroline
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 5 mM trehalose
1,10-phenanthroline
-
inhibits the neutral trehalase in presence of 5 mM trehalose
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
micromolar inhibitor
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
-
micromolar inhibitor
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
micromolar inhibitor
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
-
micromolar inhibitor
1-deoxynojirimycin
-
7-deoxycasuarine
-
-
7-homocasuarine
-
-
acetate
-
strong inhibition by acetic acid/acetate buffer, V-trehalase
ADP
-
-
ADP
-
10 mM, 16% residual activity, extracellular isoform, 12% residual activity, intracellular isoform. In presence of CaCl2, 18% residual activity for extracellular isoform, 12% residual activity, intracellular isoform, respectively
ADP
Thermochaetoides thermophila
-
1 mM, 53% inhibition
ADP
-
Ca2+ abolishes inhibitory effect
ADP
-
10 mM, 51% inhibition
ADP
-
5 mM, 23% loss of activity
Al3+
-
1 mM AlCl3, complete inhibition
Al3+
-
1 mM, no residual activity, both isoforms
Al3+
Thermochaetoides thermophila
-
1 mM, complete inhibition
AMP
-
50% inhibition at 20 mM
AMP
-
Ca2+ abolishes inhibitory effect
AMP
-
10 mM, 5% inhibition
amygdalin
-
-
amygdalin
-
competitive inhibition
amygdalin
i.e. glucose-beta-1,6-glucose-beta-mandelonitrile, linear competitive inhibitor
ATP
-
strong
ATP
-
10% residual activity at 20 mM
ATP
-
trehalase of dormant spores is strongly inhibited by 0.5 mM ATP. Trehalase from germinating spores is not inhibited by ATP up to much higher ATP concentrations
ATP
-
90% inhibition at 20 mM
ATP
-
10 mM, 12% residual activity, extracellular isoform, 6% residual activity, intracellular isoform. In presence of CaCl2, 2% residual activity for extracellular isoform, 10% residual activity, intracellular isoform
ATP
-
at pH 4.5, the enzyme is neither activated by calcium nor inhibited by EDTA or ATP. At pH 6.5, the enzyme is activated by calcium and inhibited by ATP
ATP
Thermochaetoides thermophila
-
1 mM, 80% inhibition
ATP
Thermochaetoides thermophila
-
-
ATP
-
10 mM, 67% inhibition
ATP
-
at pH 4.5, the enzyme is neither activated by calcium nor inhibited by EDTA or ATP. At pH 6.5, the enzyme is activated by calcium and inhibited by ATP
ATP
-
5 mM, 21% loss of activity
Ca2+
-
67% residual activity at 20 mM
Ca2+
-
1.0 mM CaCl2, 9% loss of activity
castanospermine
-
-
castanospermine
-
potent, reversible, competitive
castanospermine
effective competitive inhibitor of trehalase, completely inhibited by 0.001 mM
castanospermine
-
effective competitive inhibitor of trehalase, completely inhibited by 0.001 mM
castanospermine
-
50% inhibition at 0.5 mg/ml
casuarine-6-O-alpha-D-glucoside
-
casuarine-6-O-alpha-D-glucoside
-
-
cellobiose
-
10 mM, 60% inhibition
cellobiose
-
10 mM, 54% inhibition. Inhibitory effect is abolished by Ca2+
Co2+
-
Co2+
71% inhibition at 5 mM
Co2+
-
5 mM, 58% loss of activity
Cu2+
-
14% residual activity at 20 mM
Cu2+
-
1.0 mM CuSO4, 13% loss of activity
Cu2+
Lobosphaera sp.
-
weak inhibition
Cu2+
-
1 mM CuSO4, complete inhibition of extracellular enzyme, 47% inhibition of intracellular enzyme
Cu2+
Thermochaetoides thermophila
-
1 mM, complete inhibition
Cu2+
-
5 mM, 96% loss of activity
D-glucose
-
isoform Atc1p is subject to glucose repression, but exhaustion of glucose itself does not increase the activity
D-glucose
competitive inhibitor
EDTA
-
10 mM, 28% inhibition
EDTA
20 mM, 50% residual activity
EDTA
-
16% residual activity at 20 mM
EDTA
-
18.18% residual activity at 5 mM
EDTA
-
1 mM, 30% inhibition of extracellular enzyme, 54% inhibition of intracellular enzyme
EDTA
-
1 mM, 70% residual activity for extracellular isoform, 46% residual activity, intracellular isoform
EDTA
-
at pH 4.5, the enzyme is neither activated by calcium nor inhibited by EDTA or ATP. At pH 6.5, the enzyme is activated by calcium and inhibited by ATP
EDTA
-
inhibits the acid trehalase by 70%
EDTA
moderate inhibitory level at 5 mM
EDTA
-
1 mM, C-trehalase, complete inhibition
EDTA
Thermochaetoides thermophila
-
1 mM, 55% inhibition
EDTA
Thermochaetoides thermophila
-
-
EDTA
-
at pH 4.5, the enzyme is neither activated by calcium nor inhibited by EDTA or ATP. At pH 6.5, the enzyme is activated by calcium and inhibited by ATP
EDTA
-
1 mM, 29% loss of activity
esculin
-
-
Fe3+
-
31% residual activity at 20 mM
Fe3+
-
inhibits the acid trehalase by 50%
Fe3+
-
5 mM, 34% loss of activity
gentiobiose
-
slight inhibition of acid trehalase
gentiobiose
-
slight inhibition of acid trehalase
glucose
the enzyme is regulated by glucose-induced catabolite repression
Hg2+
-
HgCl2
Hg2+
-
1 mM, 58% inhibition
Hg2+
-
1 mM HgCl2, complete inhibition
Hg2+
-
1 mM, no residual activity, both isoforms
Hg2+
-
the glycoprotein enzyme forms are more susceptible than the nonglycoprotein forms
Hg2+
-
2 mM HgCl2, 61.7% inhibition
Hg2+
-
0.1 mM, complete inhibition
Hg2+
-
10 mM HgCl2, 30% loss of activity
Hg2+
-
0.11 mM HgCl2. Cl- protects from inactivation by HgCl2
Hg2+
Thermochaetoides thermophila
-
1 mM, complete inhibition
K+
-
69% residual activity at 20 mM
K+
-
0.5 M KCl, activity is 2fold lower
K+
-
100 mM KCl, 65% inhibition of C-trehalase
K+
-
10 mM, % loss of activity
mandelonitrile
-
-
mandelonitrile
-
competitive inhibition
mandelonitrile
mixed-type non-competitive inhibitor
mannitol
-
competitive inhibitor, 8% residual activity at 20 mM
MDL 25 637
-
i.e. 7-O-beta-D-glucopyranosyl-alpha-homojirimycin; potent, reversible, competitive, slow-binding nature
MDL 25 637
-
i.e. 7-O-beta-D-glucopyranosyl-alpha-homojirimycin; potent, time-dependent
metal chelators
-
-
-
metal chelators
Thermochaetoides thermophila
-
-
-
methyl-alpha-glucoside
-
slight inhibition of acid trehalase
methyl-alpha-glucoside
-
weak competitive inhibition
methyl-alpha-glucoside
-
slight inhibition of acid trehalase
Mg2+
-
1.0 mM MgCl2, 13% loss of activity
Mg2+
-
1 mM MgCl2, 30% inhibition
Mg2+
moderate inhibitory level at 5 mM
MgCl2
20 mM, 60% residual activity
MgCl2
over 90% inhibition at 10 mM
MgCl2
-
50 mM, C-trehalase, complete inhibition
MgSO4
-
57.02% residual activity at 2 mM
MgSO4
over 90% inhibition at 20 mM
Mn2+
Lobosphaera sp.
-
weak
Mn2+
moderate inhibitory level at 5 mM
Na+
-
61% residual activity at 20 mM
Na+
-
0.5 M NaCl, activity is 2fold lower
p-nitrophenyl-beta-D-glucoside
-
-
p-nitrophenyl-beta-D-glucoside
-
-
PCMB
-
1 mM is required for inhibition of more than 50%
PCMB
-
2 mM, 30.1% inhibition
PCMB
-
1 mM, 30% inhibition
phloretin
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 20 mM trehalose
phloretin
linear competitive inhibitor
phloretin
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 20 mM trehalose
phlorizin
-
-
phlorizin
-
2 mM, 20% inhibition
phlorizin
-
hyperbolic uncompetitive, binds only to enzyme-substrate complex
phlorizin
i.e. glucose-phloretin, linear competitive inhibitor
phosphate
-
-
phosphate
-
Ca2+ abolishes inhibitory effect
prunasin
-
-
prunasin
-
competitive inhibition
prunasin
i.e glucose-beta-mandelonitrile, linear competitive inhibitor
Salicin
-
competitive inhibition
Salicin
linear competitive inhibitor
sucrose
-
competitive
sucrose
Lobosphaera sp.
-
25 mM, 33% inhibition; competitive
sucrose
-
10 mM, 60% inhibition
sucrose
-
10 mM, 54% inhibition. Inhibitory effect is abolished by Ca2+
trehazolin
-
trehazolin
specific inhibitor
Tris
-
-
Tris
-
100 mM, 28% inhibition
Tris
almost complete inhibition at 5 mM
Tris
-
100 mM, 92% inhibition
Tris
-
10 mM, complete inhibition
Tris
-
3.8 mM, competitive
validamycin A
-
-
validamycin A
-
competitive inhibitor, 49% residual activity at 5 nM
validamycin A
-
potent, reversible, competitive, slow-binding nature
validamycin A
validamycin A binds at the active site with multiple hydrogen bonds
validamycin A
-
inhibits the acid trehalase
validamycin A
-
potent, time-dependent
validamycin A
-
competitive
validoxylamine A
-
complete inhibition
validoxylamine A
-
competitive inhibition
validoxylamine A
-
potent, time-dependent
Zn2+
-
non-competitive inhibitor, 22% residual activity at 20 mM
Zn2+
-
1 mM, 50% residual activity for extracellular isoform, not inhibitory for intracellular isoform
Zn2+
95% inhibition at 5 mM
Zn2+
-
1 mM, 80% loss of activity
ZnCl2
20 mM, 40% residual activity
ZnCl2
-
0.1 mM, C-trehalase, complete inhibition
ZnCl2
-
1 mM, 10% loss of activity
ZnSO4
-
10 mM, 34% inhibition
ZnSO4
-
2.06% residual activity at 10 mM
additional information
-
reaction product D-glucose suppresses enzyme expression
-
additional information
-
insensitive to ATP, cyclic AMP or divalent cations
-
additional information
-
inhibitory potency of plant-derived inhibitors in different tissues on soluble and membranous enzymes, overview, mechanism of insect tocircumvent trehalase inhibition caused by glucosides, overview
-
additional information
-
inhibitory potency of plant-derived inhibitors in different tissues on soluble and membranous enzymes, overview, mechanism of insect tocircumvent trehalase inhibition caused by glucosides, overview
-
additional information
-
40 mM sodium fluoride and trehazolin have no inhibitory effect
-
additional information
the enzyme activity is reduced under water-stress
-
additional information
-
the enzyme activity is reduced under water-stress
-
additional information
Ca2+ has no significant inhibitory effect at 5 mM
-
additional information
-
Ca2+ has no significant inhibitory effect at 5 mM
-
additional information
-
sodium arsenate (45 mM), carbonyl cyanide m-chlorophenylhydrazone (0.14 mM), and sodium fluoride (28 mM) do not inhibit the activity
-
additional information
-
not inhibited by ATP, acetate and EDTA
-
additional information
-
inhibitory potency of plant-derived inhibitors in different tissues on soluble and membranous enzymes, overview, mechanism of insect tocircumvent trehalase inhibition caused by glucosides, overview
-
additional information
-
no inhibition by 1,10-phenanthroline at 2 mM, and by gentiobiose
-
additional information
-
not inhibited by 1,3-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)propane-1,3-dione
-
additional information
-
inhibitory potency of plant-derived inhibitors in different tissues on soluble and membranous enzymes, overview, mechanism of insect tocircumvent trehalase inhibition caused by glucosides, overview
-
additional information
EDTA, polyaminopropyl biguanide, tetranitromethane, N-bromosuccinamide, gentiobiose (glucose-beta-1,6-glucose), methyl alpha-D-glucoside, 1,10-phenanthroline, and Tris (pH 6.0) do not inhibit the trehalase
-
additional information
-
EDTA, polyaminopropyl biguanide, tetranitromethane, N-bromosuccinamide, gentiobiose (glucose-beta-1,6-glucose), methyl alpha-D-glucoside, 1,10-phenanthroline, and Tris (pH 6.0) do not inhibit the trehalase
-
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0.00000066 - 0.000012
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
0.0053 - 0.0093
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
0.0256 - 0.0554
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
0.000157 - 0.01
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
0.000022 - 0.000138
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
0.000009
1-thiatrehazolin
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
0.00059 - 0.0117
7-deoxycasuarine
0.033 - 0.107
7-homocasuarine
0.00486 - 0.0067
castanospermine
0.00012
casuarine
-
pH 6.5, 30°C
7
D-glucose
at 65°C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
0.00139
deoxynojirimycin
-
pH 6.5, 30°C
1.4
glucono-delta-lactone
at pH 6.0 and 30°C
1.14
mandelonitrile
-
pH 6.0, 30°C
9
mannitol
-
at pH 5.5 and 55°C
0.043
methyl-alpha-D-mannoside
at pH 6.0 and 30°C
89
methyl-alpha-glucoside
-
pH 6.0, 30°C
6.2
methyl-alpha-mannoside
-
pH 6.0, 30°C
0.008
phloretin
at pH 6.0 and 30°C
0.000003 - 0.4
validamycin A
0.27
validamycin B
-
pH 3.3, 37°C, versus trehalose
0.0000019 - 0.0032
validoxylamine A
0.0103
validoxylamine B
-
pH 3.3, 37°C, versus trehalose
7
Zn2+
-
at pH 5.5 and 55°C
additional information
additional information
-
inhibition kinetics
-
0.00000066
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000011
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000012
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
pH not specified in the publication, temperature not specified in the publication
0.0053
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
pH 6.5, 30°C
0.0093
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
pH 6.5, 30°C
0.0256
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
pH 6.5, 30°C
0.0554
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
pH 6.5, 30°C
0.000157
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
pH not specified in the publication, temperature not specified in the publication
0.0028
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
pH not specified in the publication, temperature not specified in the publication
0.01
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000022
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000086
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000138
(2S,3R,4S,5S,6R)-2-[[(2R,5R,6R,7R,7aR)-6,7-dihydroxy-5-(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
pH not specified in the publication, temperature not specified in the publication
0.00059
7-deoxycasuarine
-
pH 6.5, 30°C
0.0117
7-deoxycasuarine
-
pH 6.5, 30°C
0.033
7-homocasuarine
-
pH 6.5, 30°C
0.107
7-homocasuarine
-
pH 6.5, 30°C
0.21
amygdalin
-
pH 6.0, 30°C
0.22
amygdalin
at pH 6.0 and 30°C
0.00486
castanospermine
-
pH 6.5, 30°C
0.0067
castanospermine
55°C, pH 7.4
0.0067
castanospermine
-
55°C, pH 7.4
0.09
phlorizin
-
pH 6.0, 30°C
0.5
phlorizin
at pH 6.0 and 30°C
0.43
prunasin
at pH 6.0 and 30°C
0.92
prunasin
-
pH 6.0, 30°C
19
Salicin
-
pH 6.0, 30°C
190
Salicin
at pH 6.0 and 30°C
0.000003
validamycin A
pH and temperature not specified in the publication
0.000004
validamycin A
-
at pH 5.5 and 55°C
0.4
validamycin A
-
pH 3.3, 37°C, versus trehalose
0.0000019
validoxylamine A
-
55°C, pH 5.0
0.00001
validoxylamine A
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
0.0032
validoxylamine A
-
pH 3.3, 37°C, versus trehalose
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0.226
supernatant, at pH 6.0 and 30°C
0.227
-
cell extract, at 37°C
0.405
-
after 40fold purification, at pH 7.0 and 30°C
1.03
-
soluble trehalase P I after 86.9fold purification, in acetate buffer, pH 5.5, at 30°C
1.224
culture filtrate, in 20 mM MES buffer, pH 5.5, at 30°C
10.8
-
40°C, pH 4.5, intracellular isoform, activity sensitive to EDTA inhibition
100
-
40°C, pH 6.5, intracellular isoform, activity resistant to EDTA inhibition
101.3
recombinant enzyme, after purification, at 30°C
106.7
-
pH 5.5, 60°C, substrate: alpha,alpha-trehalose
11.2
-
40°C, pH 6.5, intracellular isoform, activity resistant to EDTA inhibition
11.5
-
40°C, pH 4.5, extracellular isoform, activity resistant to EDTA inhibition
113.4
-
40°C, pH 6.5, extracellular isoform, activity resistant to EDTA inhibition
117
-
after 232fold purification, at pH 5.5 and 55°C
12.2
membrane-bound isozyme
12.3
-
40°C, pH 4.5, intracellular isoform, activity sensitive to EDTA inhibition
12.4
-
60°C, pH 4.5, extracellular isoform, activity sensitive to EDTA inhibition
144.7
-
pH 5.4, 37°C, recombinant protein with N-terminal His-tag
154
-
60°C, pH 6.5, extracellular isoform, activity sensitive to EDTA inhibition
16.5
-
40°C, pH 4.5, intracellular isoform, activity resistant to EDTA inhibition
16.67
after 74fold purification, at pH 6.0 and 30°C
1700
-
extracellular isoform, pH 6.0, 60°C
175.7
-
purified acid trehalase
1775
-
extracellular enzyme
18.4
-
40°C, pH 6.5, intracellular isoform, activity sensitive to EDTA inhibition
184
-
40°C, pH 6.5, extracellular isoform, activity resistant to EDTA inhibition
19.5
-
40°C, pH 6.5, intracellular isoform, activity sensitive to EDTA inhibition
195.5
-
40°C, pH 6.5, extracellular isoform, activity sensitive to EDTA inhibition
2.9
-
soluble trehalase P II after 245.7fold purification, in acetate buffer, pH 5.5, at 30°C
25.6
-
40°C, pH 4.5, intracellular isoform, activity resistant to EDTA inhibition
26.2
-
60°C, pH 4.5, intracellular isoform, activity sensitive to EDTA inhibition
27
-
40°C, pH 6.5, intracellular isoform, activity resistant to EDTA inhibition
274.8
-
60°C, pH 6.5, extracellular isoform, activity sensitive to EDTA inhibition
3.2
-
40°C, pH 4.5, extracellular isoform, activity resistant to EDTA inhibition
36.99
-
after 162fold purification, at 37°C
3700
-
intracellular isoform, pH 6.0, 65°C
389
-
40°C, pH 6.5, extracellular isoform, activity resistant to EDTA inhibition
4.8
-
40°C, pH 4.5, intracellular isoform, activity resistant to EDTA inhibition
42.2
-
40°C, pH 6.5, extracellular isoform, activity resistant to EDTA inhibition
46
-
40°C, pH 4.5, intracellular isoform, activity resistant to EDTA inhibition
48.6
-
40°C, pH 6.5, intracellular isoform, activity resistant to EDTA inhibition
49.6
-
60°C, pH 4.5, intracellular isoform, activity sensitive to EDTA inhibition
5.2
-
40°C, pH 4.5, extracellular isoform, activity sensitive to EDTA inhibition
53.4
-
solubilized enzyme
6.2
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
76.5
-
60°C, pH 6.5, intracellular isoform, activity sensitive to EDTA inhibition
76.8
-
60°C, pH 6.5, intracellular isoform, activity sensitive to EDTA inhibition
95.5
-
40°C, pH 6.5, extracellular isoform, activity sensitive to EDTA inhibition
0.01
-
soluble trehalase P I from supernatant, in acetate buffer, pH 5.5, at 30°C
0.01
-
soluble trehalase P II from supernatant, in acetate buffer, pH 5.5, at 30°C
0.01
-
supernatant, at pH 7.0 and 30°C
0.5
-
crude extract, at pH 5.5 and 55°C
0.5
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
120
after 98.04fold purification, in 20 mM MES buffer, pH 5.5, at 30°C
120
native enzyme, after purification, at 30°C
120
Thermochaetoides thermophila
-
-
31.5
-
40°C, pH 4.5, extracellular isoform, activity resistant to EDTA inhibition
31.5
-
60°C, pH 4.5, extracellular isoform, activity sensitive to EDTA inhibition
7.7
-
40°C, pH 4.5, extracellular isoform, activity resistant to EDTA inhibition
7.7
-
40°C, pH 4.5, extracellular isoform, activity sensitive to EDTA inhibition
75
-
pH 6.5, 30°C
additional information
-
-
additional information
-
-
additional information
Lobosphaera sp.
-
-
additional information
-
activities of neutral and acid trehalase at different pH values and temperatures
additional information
determination of trehalose contents in differently treated cells, overview
additional information
-
determination of trehalose contents in differently treated cells, overview
additional information
-
-
additional information
-
-
additional information
-
activities of neutral and acid trehalase at different pH values and temperatures
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malfunction
-
knockdown of trehalase leads to a loss of the lamina and a smaller medulla in optic lobe
malfunction
-
spores deficient in trehalase are less sensitive to heat stress in a very early stage of germination
malfunction
-
loss of treA significantly reduces its cell invasion capacity and colonization of the bladder in a murine model of urinary tract infection
malfunction
trehalase deletion mutant (treA) has increased tolerance to thermal stress and produces less biofilm than the wild type B. pseudomallei K96243 strain. The DELTAtreA mutant has reduced ability to survive in macrophages
malfunction
-
trehalase deletion mutant (treA) has increased tolerance to thermal stress and produces less biofilm than the wild type B. pseudomallei K96243 strain. The DELTAtreA mutant has reduced ability to survive in macrophages
-
malfunction
-
loss of treA significantly reduces its cell invasion capacity and colonization of the bladder in a murine model of urinary tract infection
-
metabolism
-
different functions of the insect soluble and membrane-bound trehalase genes in chitin biosynthesis, overview
metabolism
the enzyme catalyzes the last step in the trehalose metabolism and is the key enzyme controlling the pathway in response to water conditions
metabolism
-
the enzyme catalyzes the last step in the trehalose metabolism and is the key enzyme controlling the pathway in response to water conditions
-
physiological function
-
role for Nth2p in the mobilization of intracellular trehalose during salt-stress recovery, overview
physiological function
the enzyme trehalase is involved in energy metabolism and controlling trehalose, the main blood sugar of insects, levels in cells
physiological function
diapause hormone stimulates expression of both soluble trehalase and integral membrane trehalase. The amount of treh-2 mRNA is approximately 1000fold higher than that of treh-1 mRNA. Trehalase activity enhanced by diapause hormone in developing ovaries is mostly induced by treh-2 protein depending on the transcriptional level
physiological function
-
intracellular trehalase activity is required for development, germination and heat-stress resistance of Aspergillus niger conidia
physiological function
-
the enzyme takes part in the insect carbohydrate metabolism associated with the reproductive process
physiological function
-
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
A4WBE4
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
-
trehalase plays a role in neuroepithelial stem cell maintenance and differentiation during Drosophila optic lobe development. Trehalase is essential for lamina and medulla development and suppresses the differentiation of neuroepithelial cells
physiological function
-
treA gene is needed for optimal production of type 1 fimbriae in ExPEC strain MT78
physiological function
trehalase is an indispensable component of insect hemolymph that plays important role in energy metabolism and stress resistance
physiological function
-
trehalase is an indispensable component of insect hemolymph that plays important role in energy metabolism and stress resistance
physiological function
trehalase plays a role in macrophage colonization and virulence of Burkholderia pseudomallei in insect and mammalian hosts
physiological function
-
role for Nth2p in the mobilization of intracellular trehalose during salt-stress recovery, overview
-
physiological function
-
trehalase function is central in carbon partitioning and energy homeostasis regulation
-
physiological function
-
trehalase plays a role in macrophage colonization and virulence of Burkholderia pseudomallei in insect and mammalian hosts
-
physiological function
-
trehalase function is central in carbon partitioning and energy homeostasis regulation
-
physiological function
-
treA gene is needed for optimal production of type 1 fimbriae in ExPEC strain MT78
-
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