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Information on EC 3.2.1.28 - alpha,alpha-trehalase
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3.2.1.28 alpha,alpha-trehalaseIUBMB Comments
The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha-trehalose, releasing initially equimolar amounts of alpha- and beta-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
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Word Map
- 3.2.1.28
- sucrase
- lactase
- border
- larvae
- disaccharidase
-
brush
- trehalose-6-phosphate
- glycogen
- midgut
- glucoamylase
- hemolymph
-
camp-dependent
- validamycin
- chitin
- isomaltase
- silkworm
- alpha-glucosidase
-
instar
- bombyx
-
brush-border
- gamma-glutamyltransferase
- sucrase-isomaltase
- microvillar
- lepidoptera
-
carbohydrases
- molitor
- tenebrio
- 20-hydroxyecdysone
-
diapause
- metarhizium
- cellobiase
- planthopper
- ascospores
- analysis
- diagnostics
- synthesis
- agriculture
- medicine
- biotechnology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
trehalase, neutral trehalase, acid trehalase, soluble trehalase, tre-2, nth1p, alpha,alpha-trehalase, setre-2, atc1p, ntp1p, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid (non regulatory) trehalase
acid trehalase
alpha,alpha'-trehalose 1-D-glucohydrolase
-
-
-
-
Alpha,alpha-trehalase
-
-
-
-
Alpha,alpha-trehalose glucohydrolase
alpha-glucoside-1-glucohydrolase
ATC1
Atc1p
Ath1
glucose alpha-1,1-glucose hydrolase
MSMEG 4528
neutral trehalase
Ntc1p
NTH1
Tre-2
TRE1
TreA
trehalase
Alpha,alpha-trehalose glucohydrolase
-
-
-
-
trehalase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
-
-
-
-
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
role of carboxyl, guanidine and imidazole groups in catalysis
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose glucohydrolase
The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha-trehalose, releasing initially equimolar amounts of alpha- and beta-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
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CAS REGISTRY NUMBER
COMMENTARY
9025-52-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
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
-
both isoforms are highly specific for trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
preferred substrate of acid trehalase
-
-
?
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
-
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
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
-
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
-
neutral trehalase mobilizes trehalose accumulated by fungal cells as a protective and storage carbohydrate
-
-
?
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
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
-
-
-
?
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
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
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
-
-
-
?
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
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
-
-
-
?
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
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
maltose + H2O
2 D-glucose
1.7% of the activity with trehalose
-
-
?
sucrose + H2O
D-glucose + D-fructose
5.7% of the activity with trehalose
-
-
?
trehalose + H2O
D-glucose
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
-
?
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
-
?
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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
-
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
-
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
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
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
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
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
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
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
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
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
trehalose + H2O
D-glucose
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
-
?
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
-
?
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
Co2+
gentiobiose
K+
Mg2+
MgCl2
Mn2+
Na+
NaCl
phloretin
additional information
Ca2+
-
C-trehalase is absolutely dependent on Ca2+ or Mn2+. 4fold activation of C-trehalase at 2.5 mM CaCl2
Ca2+
-
D97 and D108 in the conserved putative Ca2+-binding motif of Ntp1p appear to be responsible for this interaction. Strains expressing Ntp1p variants that are unable to bind Ca2+ partially resemble those devoid of the ntp1+ gene in terms of trehalose hyperaccumulation
Mg2+
-
absolutely required for activity, optimum activity occurring at concentrations of 3.5-4 mM
Mn2+
-
30% activation by 20-300 mM neutral salts such as KCl, NaNO3 and MnCl2, V-trehalase. C-trehalase is absolutely dependent on Ca2+ or Mn2+. 2fold activation of C-trehalase by MnCl2
Na+
-
the glycoprotein enzyme forms show lower activation than the nonglycoprotein forms
Na+
-
30% activation by 20-300 mM neutral salts such as KCl, NaNO3 and MnCl2, V-trehalase
NaCl
-
activity is increased by the presence of NaCl, showing the highest activity (136 %) at 1 M NaCl
phloretin
-
activates the neutral trehalase in presence of 5 mM trehalose
phloretin
-
activates the neutral trehalase in presence of 5 mM trehalose
additional information
-
Zn2+, Ca2+, Mg2+, Fe3+, EDTA, and 4-chloromercuribenzoate have different effects on alkaline trehalase and acid trehalases
additional information
the activity is independent of divalent cations
additional information
-
Mg2+ can not be replaced by Ca2+, Mn2+ or Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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,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
1,3-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)propane-1,3-dione
micromolar inhibitor
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
fructose
-
10 mM, 45% inhibition. Inhibitory effect is abolished by Ca2+
lactose
-
10 mM, 68% inhibition. Inhibitory effect is abolished by Ca2+
maltose
-
10 mM, 54% inhibition. Inhibitory effect is abolished by Ca2+
NaCl
strong inhibition at 10 mM, treatment of cells leads to accumulation of trehalose
NH4Cl
-
1 mM NH4Cl, 22% inhibition of extracellular enzyme, 27% inhibition of intracellular enzyme
(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,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
acetate
-
strong inhibition by acetic acid/acetate buffer, V-trehalase
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
amygdalin
i.e. glucose-beta-1,6-glucose-beta-mandelonitrile, linear competitive inhibitor
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
-
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
-
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
castanospermine
effective competitive inhibitor of trehalase, completely inhibited by 0.001 mM
castanospermine
-
effective competitive inhibitor of trehalase, completely inhibited by 0.001 mM
cellobiose
-
10 mM, 54% inhibition. Inhibitory effect is abolished by Ca2+
Cu2+
-
1 mM CuSO4, complete inhibition of extracellular enzyme, 47% inhibition of intracellular enzyme
D-glucose
-
isoform Atc1p is subject to glucose repression, but exhaustion of glucose itself does not increase the activity
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
-
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
glucose
the enzyme is regulated by glucose-induced catabolite repression
Hg2+
-
the glycoprotein enzyme forms are more susceptible than the nonglycoprotein forms
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
methyl-alpha-glucoside
-
slight inhibition of acid trehalase
phloretin
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 20 mM trehalose
phloretin
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 20 mM trehalose
phlorizin
-
hyperbolic uncompetitive, binds only to enzyme-substrate complex
prunasin
i.e glucose-beta-mandelonitrile, linear competitive inhibitor
sucrose
-
10 mM, 54% inhibition. Inhibitory effect is abolished by Ca2+
validamycin A
-
potent, reversible, competitive, slow-binding nature
validamycin A
validamycin A binds at the active site with multiple hydrogen bonds
Zn2+
-
1 mM, 50% residual activity for extracellular isoform, not inhibitory for intracellular isoform
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
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3',5'-cAMP
-
activation is dependent on presence of ATP and a divalent cation such as Mg2+, Mn2+ or Co2+
alpha,alpha-trehalose
-
the enzymatic activity increases with increasing concentrations of alpha,alpha-trehalose in the incubations up to about 50 mM
AMP
-
10 mM, in presence of CaCl2, 18% residual activity for extracellular isoform, 12% residual activity, intracellular isoform. No activation in absence of Ca2+
amygdalin
-
induces the enzyme in different organs, e.g. Malphigian tubules, midgut, fat body, hemolymph, and body wall, when feeded to larvae
esculin
-
induces the enzyme in different organs, e.g. Malphigian tubules, midgut, fat body, hemolymph, and body wall, when feeded to larvae
MgATP2-
-
C-trehalase can be activated by MgATP2- in presence of cAMP
Ca2+
-
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
Ca2+
-
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
additional information
-
activation by cAMP-dependent protein kinase
-
additional information
-
the cryptic enzyme form is completely activated at protein concentrations higher than 60 mg/ml
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
alpha,alpha-trehalose
-
pH 5.4, 37°C, recombinant protein with N-terminal His-tag
1.34
alpha,alpha-trehalose
pH and temperature not specified in the publication
3.09
alpha,alpha-trehalose
-
presence of Mn2+, intracellular isoform, pH 6.0, 65°C
6.43
alpha,alpha-trehalose
-
presence of Ca2+, intracellular isoform, pH 6.0, 65°C
7.63
alpha,alpha-trehalose
-
presence of Mn2+, extracellular isoform, pH 6.0, 60°C
9.51
alpha,alpha-trehalose
-
presence of Ca2+, extracellular isoform, pH 6.0, 60°C
0.16
trehalose
at 65°C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
0.27
trehalose
at 88°C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
0.52
trehalose
recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.6, with 0.01% Triton X-100, at 35°C
2.3
trehalose
native enzyme, in 20 mM MES, pH 6.0 for 10 min at 30°C
2.6
trehalose
recombinant enzyme, in 20 mM MES, pH 6.0 for 10 min at 30°C
additional information
additional information
-
trehalase from dormant spores shows a deviation from the Michaelis-Menten equation
-
additional information
additional information
-
Km of neutral and acid trehalase at different temperatures and pH values
-
additional information
additional information
-
Km of neutral and acid trehalase at different temperatures and pH values
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the molecular activity is 86.2 per s
-
662
trehalose
recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.6, with 0.01% Triton X-100, at 35°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000157 - 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)
7
D-glucose
at 65°C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
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
0.0093
(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
0.000003
validamycin A
pH and temperature not specified in the publication
0.00001
validoxylamine A
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0061 - 0.024
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
0.223
1,3-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)propane-1,3-dione
Chironomus riparius
at pH 6.9 and 30°C
0.011 - 0.076
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
additional information
additional information
Termitoidae
-
the concentrations of validoxylamine A, validoxylamine B, validamycin A and validamycin B required for 50% inhibition IC50 of termites trehalase are 14.73 mg/l, 20.80 mg/l, 3.17 x 103 mg/l, and 2.24 x 103 mg/l, respectively
-
0.019
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
Chironomus riparius
-
pH 6.5, 30°C
0.0524
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
Chironomus riparius
-
pH 6.5, 30°C
0.1108
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
Sus scrofa
-
pH 6.5, 30°C
0.0061
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
Chironomus riparius
at pH 6.9 and 30°C
0.024
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
Sus scrofa
-
at pH 6.9 and 30°C
0.011
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
Chironomus riparius
at pH 6.9 and 30°C
0.076
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
Sus scrofa
-
at pH 6.9 and 30°C
0.000013
trehazolin
Metarhizium anisopliae
native enzyme, in 20 mM MES, pH 6.0, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.5
1.03
-
soluble trehalase P I after 86.9fold purification, in acetate 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
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
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
120
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
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
31.5
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
6.2
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
7.7
75
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
additional information
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
0.5
-
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
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
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
-
activities of neutral and acid trehalase at different pH values and temperatures
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
a minor activity maximum at pH 3.5 and a major activity maximum at pH 6.5
4.5
4.5 - 5
5 - 5.5
5.5
5.6
5.8 - 6
6.5
6.7
7.1
7.4
6.5
-
a minor activity maximum at pH 3.5 and a major activity maximum at pH 6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.6 - 7.9
-
pH 3.2: about 45% of maximal activity, pH 6.9: about 40% of maximal activity
3 - 5
pH 3.0: about 50% of maximal activity, pH 5.0: about 40% of maximal activity, recombinant enzyme
3 - 7
-
pH 3.0: about 70% of maximal activity, pH 7.0: about 85% of maximal activity
3.2 - 7
-
pH 3.2: about 50% of maximal activity, pH 7.0: about 60% of maximal activity
3.5 - 6
-
pH 3.5: about 75% of maximal activity, pH 6.0: about 80% of maximal activity
4 - 7
4 - 7.5
-
pH 4.0: about 35% of maximal activity, pH 7.5: about 30% of maximal activity
4 - 8.5
-
90% of maximal activity at pH 6.0, maximal activity at pH 7.0
4.5
4.5 - 7
4.8 - 8.5
-
pH 4.9: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
5 - 8
-
retains more than 60% of the original activity in a pH range of 5.0-8.0, wild type enzyme, mutant enzyme Y227H/R442G, mutant enzyme Y227H, mutant enzyme R442G
6.5
4 - 7
pH 4.0: about 90% of maximal activity, pH 7.0: about 30% of maximal activity
4 - 7
-
pH 4.0: about 90% of maximal activity, pH 7.0: about 30% of maximal activity
4.5
-
at pH 4.5, enzyme is neither activated by calcium nor inhibited by EDTA or ATP.
4.5
-
at pH 4.5, enzyme is neither activated by calcium nor inhibited by EDTA or ATP.
6.5
-
at p-h 6.5, enzyme is activated by calcium and inhibited by ATP
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
40 - 45
45
45 - 55
50
55
60
65
additional information
Thermochaetoides thermophila
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
50
-
wild type enzyme, mutant enzyme Y227H/R442G, mutant enzyme Y227H, mutant enzyme R442G
60
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
60
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
-
30°C: 80% of maximal activity, 50°C: 50% of maximal activity
30 - 65
-
30°C: about 65% of maximal activity, 65°C: about 40% of maximal activity
37 - 60
37 - 65
37°C: about 40% of maximal activity, 65°C: about 70% of maximal activity
40 - 60
-
more than 50% of their original activities in the temperature range of 40 to 60 °C, wild type enzyme, mutant enzyme Y227H/R442G, mutant enzyme Y227H, mutant enzyme R442G
40 - 75
50 - 60
Thermochaetoides thermophila
-
50°C: 39% of maximal activity, 60°C: 44% of maximal activity
37 - 60
37°C: about 60% of maximal activity, 60°C: about 90% of maximal activity
37 - 60
-
37°C: about 60% of maximal activity, 60°C: about 90% of maximal activity
40 - 75
40°C: about 75% of maximal activity, 75°C: about 35% of maximal activity, recombinant enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
4.7
4.9
5.02
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
neutral trehalase and acid trehalase isozymes encoded by the NTH1 and ATH1 genes
-
-
brenda
Thermochaetoides thermophila
fragment; subspecies Metarhizium anisopliae acridum, strain CQMa102
UniProt
brenda
NlTre-1; brown planthopper, gene NlTre-1 encoding the soluble isozyme
UniProt
brenda
NlTre-2; brown planthopper, gene NlTre-2 encoding the membrane-bound isozyme
UniProt
brenda
2 nonglycoprotein enzyme forms: A1 and B1 and 2 glycoprotein enzyme form A2 and B2
-
-
brenda
-
-
-
brenda
neutral Nth1 and Nth2 and acid Ath1, encoded by gene ath1
-
-
brenda
neutral trehalase and acid trehalase isozymes encoded by the NTH1 and ATH1 genes
-
-
brenda
membrane-bound trehalase SfTre2; membrane-bound isozyme SfTre2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
early in gestation amniotic fluid enzyme activity originates exclusively from the fetal kidney, but more and more intestinal enzyme is released into the amniotic cavity as the fetus develops
brenda
Purkinje cells of the cerebellum show higher immunoreactivity than neurons in the hippocampus and cerebral cortex
brenda
strong trehalase activity in the perikarya and dendrites of neurons located in the hippocampus
brenda
strong trehalase activity in the perikarya and dendrites of neurons located in the hippocampus
brenda
-
activity is low in the healthy infants and elevated in patients with asphyxia. Markedly high activity is observed in patients with Lowe syndrome. Increase of urinary trehalase reflects the extent of renal tubular damage
brenda
additional information
-
sudden 10fold increase in trehalase activity within the first min of spore germination. After reaching a maximum between 5 and 10 min, the activity declines back to low values during the next hours
brenda
-
sudden 10fold increase in trehalase activity within the first min of spore germination. After reaching a maximum between 5 and 10 min, the activity declines back to low values during the next hours
-
brenda
-
activity in nitrogen-fixing pure culture is about 4times greater than in non-fixing cultures
brenda
-
activity in nitrogen-fixing pure culture is about 4times greater than in non-fixing cultures
-
brenda
midgut, isozyme SfTre1 is localized at the secretory vesicles and at the glycocalyx of columnar cells
brenda
in embryonic and larval stages, the transcript levels of Hl-Tre decreases during embryonic development and increases after the pentactula stage
brenda
high level of activity. Positive Hl-Tre signals are observed in the brush borders of the intestinal mucosa
brenda
in embryonic and larval stages, the transcript levels of Hl-Tre decreases during embryonic development and increases after the pentactula stage
brenda
-
under normal conditions, expression in root nodule is induced compared with leaf and root
brenda
-
under normal conditions, expression in root nodule is induced compared with leaf and root
brenda
columnar cells, distribution of membrane-bound trehalase, isozyme SfTre2, along Spodoptera frugiperda midgut cells, overview
brenda
columnar cells, distribution of soluble trehalase, isozyme SfTre1, along Spodoptera frugiperda midgut cells, overview
brenda
-
vesicle clusters isolated from Alnus rubra nitrogen-fixing nodules infected with ArI3. Activity is 6-7 times greater than in nitrogen-fixing cultures and 26-33 times greater than in non-fixing cultures
brenda
-
vesicle clusters isolated from Alnus rubra nitrogen-fixing nodules infected with ArI3. Activity is 6-7 times greater than in nitrogen-fixing cultures and 26-33 times greater than in non-fixing cultures
-
brenda
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
brenda
-
under normal conditions, expression in root nodule is induced compared with leaf and root
brenda
-
under normal conditions, expression in root nodule is induced compared with leaf and root
brenda
-
downregulation under salt stress. Under normal conditions, expression in root nodule is induced compared with leaf and root
brenda
-
under normal conditions, expression in root nodule is induced compared with leaf and root. In senescent nodules, the activity decreases
brenda
-
contains 2 different forms which are convertible in vivo: a form with low activity found in dormant spores and an active form after breaking the dormancy
brenda
additional information
-
expression pattern in presence or absence of D-glucose
brenda
additional information
-
no activity in the fat body, distribution in the soluble and membrane fractions of the tissues, overview
brenda
additional information
-
distribution in the soluble and membrane fractions of the tissues, overview
brenda
additional information
activity and gene mRNA level at different developmental stages, expression pattern, overview
brenda
additional information
activity and gene mRNA level at different developmental stages, expression pattern, overview
brenda
additional information
-
activity and gene mRNA level at different developmental stages, expression pattern, overview
brenda
additional information
-
growth on trehalose leads to the Kluyver effect, in contrast to other yeasts
brenda
additional information
-
tissue distribution of soluble trehalase SeTre-1, developmental expression pattern of the two trehalase genes SeTre-1 and SeTre-2, overview
brenda
additional information
-
distribution in the soluble and membrane fractions of the tissues, overview
brenda
additional information
isoform Treh1 is not detected in the brain and Malpighian tubules
brenda
additional information
isoform Treh1 is not detected in the brain and Malpighian tubules
brenda
additional information
-
isoform Treh1 is not detected in the brain and Malpighian tubules
brenda
additional information
-
distribution in the soluble and membrane fractions of the tissues, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
trehalase accounts for 0.1% and 0.3% of total brush-border membrane protein of intestine and kidney, respectively
brenda
-
apical, anchored by a glycosylphosphatidylinositol-anchor, isozyme type 2
brenda
-
elevated activity in resting cells or in cultures growing on trehalose or glycerol
brenda
-
TreF. TreF can be exported to the periplasm where it is present in a misfolded and inactive form
brenda
-
high activity in exponential growth phase, regardless of the carbon source
brenda
-
the internal trehalase can be separated into a cell wall-bound and a soluble intracellular fraction
brenda
-
the internal trehalase can be separated into a cell wall-bound and a soluble intracellular fraction
-
brenda
-
cell surface, the isozyme type 2 contains one transmembrane segment and lacks the omega site
brenda
NlTre2, contains a putative transmembrane domain
brenda
-
the acid trehalase contains either a transmembrane segment or a signal sequence at the N-terminus
brenda
-
TreA. TrA can fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence
-
brenda
NlTre1, the soluble trehalase isozyme accounts for the majority of total trehalase activity
-
brenda
additional information
NlTre-1 contains trehalase signature motifs
-
brenda
additional information
NlTre-1 contains trehalase signature motifs
-
brenda
additional information
-
NlTre-1 contains trehalase signature motifs
-
brenda
additional information
NlTre-2 contains trehalase signature motifs
-
brenda
additional information
NlTre-2 contains trehalase signature motifs
-
brenda
additional information
-
NlTre-2 contains trehalase signature motifs
-
brenda
additional information
-
Ath1 possesses a transmembrane domain. Existence of a secretion sequence in Ath1
-
brenda
additional information
immunohistochemic localization study of isozyme SfTre1
-
brenda
additional information
immunohistochemic localization study of isozyme SfTre1
-
brenda
additional information
-
immunohistochemic localization study of isozyme SfTre1
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
Escherichia coli MT78
-
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
Escherichia coli MT78
-
treA gene is needed for optimal production of type 1 fimbriae in ExPEC strain MT78
-
Show AA Sequence and Transmembrane Helices (11453 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
120000
170000
175000
210000
30000
370000
38000
48500
-
enzyme form amniotic fluid, protein part of the enzyme, radiation inactivation
49000
-
enzyme form kidney and intestine, protein part of the enzyme, radiation inactivation
51500
-
2 * 60000, SDS-PAGE, 2 * 51500, deglycosylated enzyme, SDS-PAGE
58000
60000
65000
65610
66300 - 72000
-
depending on the amount of sugar bound to the enzyme, enzyme from amniotic fluid, calculation from hydrodynamic parameters
67000
67070
x * 67070, isoform Treh1, calculated from amino acid sequence
68000
69000
71000
73620
x * 73620, isoform Treh2, calculated from amino acid sequence
74000
75000
76000
77000
80000
84000
85000
170000
-
enzyme from kidney and intestine, gel filtration in presence of 1% Triton
210000
-
enzyme from activated spores and from dormant spores, gel filtration
30000
-
x * 30000, about, recombinant GFP-tagged Ath1 N-terminal domain
60000
-
2 * 60000, SDS-PAGE, 2 * 51500, deglycosylated enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
multimer
pentamer
additional information
?
x * 67070, isoform Treh1, calculated from amino acid sequence
?
x * 73620, isoform Treh2, calculated from amino acid sequence
dimer
-
2 * 60000, SDS-PAGE, 2 * 51500, deglycosylated enzyme, SDS-PAGE
pentamer
-
5 * 82000, extracellular isoform, 5 * 85000, intracellular isoform, SDS-PAGE
additional information
-
a major protein species of 42000 Da and two minor protein species of 45000 Da and 49000 Da are detected by SDS-PAGE
additional information
-
TrA can fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence
additional information
-
polypeptide bands of 84000 Da, 98000 Da and 105000 Da are detected on SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
side-chain modification
glycoprotein
-
five potential N-glycosylation sites are detected by sequence analysis
glycoprotein
-
recombinant protein with N-terminal His-tag contains O-linked oligosaccharide chains having Galbeta1-3GalNAc-structure without terminal sialic acids
glycoprotein
-
extracellular enzyme contains 81% carbohydrate, intracellular enzyme contains 51% carbohydrate
glycoprotein
-
carbohydrate content 81%, extracellular isoform, and 51%, intracellular isoform, respectively
glycoprotein
-
2 nonglycoprotein enzyme forms: A1 and B1, and 2 glycoprotein enzyme forms: A2 and B2
glycoprotein
-
the maturation of trehalase is a stepwise process beginning with a carbohydrate-free 41000 Da protein. This form is core-glycosylated in the endoplasmic reticulum yielding a 76000 Da form observed in sec18 mutant cells. A higher glycosylated 180000 Da enzyme form accumulates in sec7 mutant cells indicating localization in the Golgi body. The apparent molecular mass of the mature enzyme form observed in wild-type cells is 220000 Da
glycoprotein
membrane-bound trehalase.SfTre2 contains potential N-glycosylation sites
glycoprotein
soluble trehalase.SfTre1 contains potential N-glycosylation sites
phosphoprotein
enzyme is phosphorylated by cAMP-dependent protein kinase, but not significantly activated
phosphoprotein
the enzyme is regulated by reversible phosphorylation mediated by the cAMP-PKA pathway
phosphoprotein
-
the enzyme is regulated by reversible phosphorylation mediated by the cAMP-PKA pathway
-
side-chain modification
-
multiple forms of cryptic totally inactive trehalase-c of 32000 Da, 160000 Da and 80000 Da are activated by protein kinase. A single active enzyme form, trehalase-a of 16000 Da is formed
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures are determined in the ligand-free form and bound to the inhibitor validoxylamine A. Multiple salt bridges are identified that potentially facilitate closure of a hood over the substrate-binding site
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D108K
-
mutant enzyme fails to bind Ca2+ or to undergo enzyme activation
D97L
-
mutant enzyme fails to bind Ca2+ or to undergo enzyme activation
D322A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
E520A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis. In presence of azide, activity increases three fold
R169A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R222A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R222A/R287A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R287A
at least four orders of magnitude less active than wild type trehalase, with no structural difference between mutant and wild type enzyme discernible by circular dichroism. Mutation causes an increase in the activation energy for trehalose hydrolysis
R442G
-
the mutant enzyme displays a 56% decrease in Km, a 22% increase in kcat, and a 1.78fold increase in kcat/Km compared with the wild type enzyme. The mutation reduces the size of the side chain and decreases the steric hindrance, which contributes to channel the substrate into the active cavity easier and promote the release of the product
Y227H
-
the mutant enzyme displays a 27% decrease in Km, a 14% increase in kcat, and a 0.57fold increase in kcat/Km compared with the wild type enzyme. The mutation enlarges the shape of the binding pocket, to improve the binding of the substrate and the release of the products
Y227H/R442G
-
the mutant enzyme displays a 61% decrease in Km, a 65% increase in kcat and a 3.3 fold increase in catalytic efficiency compared with the wild type enzyme (265.91 mmol-1 s-1)
additional information
additional information
-
construction of enzyme-deficient mutants by gene disruption at two ATC chromosomal alleles
additional information
-
expression in Saccharomyces cerevisiae mutant lacking the endogenous trehalase nth1 does not rescue its dysfunction or enable the mutant to grow on trehalose. Expression in Saccharomyces cerevisiae trehalase mutants nth1 or ath1 does not rescue their sensitivity to heat, osmotic stress, or oxidative stress
additional information
-
complementation of the Saccharomyces cerevisiae suc2D mutant SEY6210 strain with different Ath1-invertase chimera, where the Suc2 signal peptide is replaced by full-length ATH1 sequence, overview. Hybrid Ath1 truncated mutants fused at their C-terminus with the yeast internal invertase reveal that a 131 amino acid N-terminal fragment of Ath1 is sufficient to target the fusion protein to the cell surface, enabling growth of the suc2DELTA mutant on sucrose. Removal of the N-terminus of Ath1 causes a strict vacuolar localization. Fusion of the signal peptide of invertase to N-terminally truncated Ath1 allows the ath1D mutant to grow on trehalose, whereas the signal sequence of the vacuolar-targeted Pep4 constrained Ath1 in the vacuole and prevents growth of this mutant on trehalose
additional information
-
construction of mutants defective in neutral trehalase and/or acid trehalase isozymes, metabolism phenotypes and viability, overview. The mutants show altered recovery from salt stress compared to the wild-type enzyme
additional information
-
construction of mutants defective in neutral trehalase and/or acid trehalase isozymes, metabolism phenotypes and viability, overview. The mutants show altered recovery from salt stress compared to the wild-type enzyme
-
additional information
-
Ntp1p elutes mainly in an inactive conformation instead of the dimeric or trimeric active form of the enzyme. Activation of the enzyme under different conditions depends upon binding through the Ca2+-binding motif as a prerequiste for correct enzyme oligomerization to its active form
additional information
-
knockout by RNAi of genes SeTre-1 and SeTre-2 leads to significant higher mortality rates during the larva-pupa stage and pupa-adult stage, lethal phenotypes, overview. Knockdown of SeTre-1 gene largely inhibited the expression of chitin synthase gene A and reduced the chitin content in the cuticle to two-thirds relative to the control insects
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 8
after incubation at pH values of 3.5-8.0 and 30°C for 1 h, all residual activities of reATM1 are over 80%
682673
4 - 9
Lobosphaera sp.
-
5°C, 15 h, stable
136179
6.5 - 8
-
the trehalase activity drops sharply at pH values of 6.5 and below, as well as at pH values of 8.0 and above
679765
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36
-
90 min, 93.3% loss of activity of the enzyme from activated spores, 67% loss of activity of the enzyme from dormant spores
40
45 - 50
50
55
60
62
65
70
70 - 90
the enzyme exhibits approximately a half-life of 6 h at 70°C, and of 2.5 h at 80°C, incubation of 10 min at 87°C results in 70% loss of the enzyme activity, and after 10 min at 90°C no residual activity is detected
80
the recombinant trehalase with a histidine tag at the N-terminus loses 50% of the activity after 10 min incubation at 80°C in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
90
half-life of native enzyme: 53 min, half-life of revcombinant enzyme: 41 min
additional information
40
recombinant enzyme, stable under incubation at 40°C or lower for 15 min
50
the enzyme is stable below 50°C, but it loses activity rapidly above 50°C
50
-
the enzyme remains practically unaffected by 10 min treatment at 50°C
60
-
extracellular enzyme has a half-life of 3 min. Intracellular enzyme loses 20% of activity after 40 min when incubated without Ca2+, and is fully stable in presence of Ca2+
62
solubilized membrane-bound isozyme SfTre2, half-life is 10 min
65
-
intracellular enzyme has a half-life of 4.5 min when incubated without Ca2+
additional information
-
the acid trehalase is more thermostable than the neutral trehalase
additional information
thermostability of recombinant enzyme is slightly reduced compared to native enzyme
additional information
-
thermostability of recombinant enzyme is slightly reduced compared to native enzyme
additional information
Thermochaetoides thermophila
-
addition of Ca2+ decreases stability, half-life at 65°C is diminished about 2fold
additional information
Thermochaetoides thermophila
-
the acid trehalase is more thermostable than the neutral trehalase
additional information
-
bovine serum albumin and casein protects from heat-inactivation
additional information
-
the acid trehalase is more thermostable than the neutral trehalase
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme form A1 becomes labile on addition of glycerol, activity in presence of 20% or 40% glycerol is about 30-40% lower than in absence of glycerol. Enzyme form B2 becomes more stable on addition of glycerol, activity in presence of 20% or 40% glycerol is about 30 higher than in absence of glycerol
-
rapid inactivation during butanol treatment at temperatures above 4°C for periods of more than 3 min at 4°C
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60°C, intestinal, renal and amniotic fluid enzyme retain full activity for at least 6 months
-
-80°C, 9 days, 15% loss of activity of enzyme form A1, 5% loss of activity of enzyme form A2, 35% loss of activity of enzyme form B1, 65% loss of activity of enzyme form B2
-
4°C, 0.02 M phosphate buffer, pH 6.2, the cryptic trehalase-c is completely stable in dilute aqueous solution and can be activated even after 6 months
-
4°C, pH 7.5, 20% glycerol, 20% loss of activity of trehalase-a after 5 months
-
immobilized crude recombinant enzyme on chitin shows no significant loss of activity being reused 10times and stored at 10°C, in 50 mM sodium maleate, pH 6.0, for 55 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2896fold from midgut of larvae, by ammonium sulfate precipitation, 2 steps of hydrophobic interaction and ion exchange chromatography
-
acid trehalase 425fold from root nodules, by ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and native PAGE
-
ammonium sulfate fractionation, phenyl-Sepharose DE-52 column chromatography and Sephacryl S-300 gel filtration
-
ammonium sulfate precipitation, Biosuite DEAE column chromatography, and gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, CM Sepharose column chromatography, and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, DEAE-Sephadex-A50 column chromatography, and HPLC gel filtration on Protein Pak 300 SW
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Q Sepharose column chromatography
DEAE Sepharose Fast Flow column chromatography and Sephacryl S-100 gel filtration
Econo-Pac methyl hydrophobic interaction column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
High Q Sepharose column chromatography, 25Q Sepharose column chromatography, and Sephacryl-200s HR gel filtration
nickel exchange chromatography
partial
recombinant His-tagged enzyme by His affinity chromatography to homogeneity
Sephacryl S-300 gel filtration, DEAE-cellulofine column chromatography, and Con A-Sepharose column chromatography
-
stem enzyme 800fold by ion exchange chromatography, gel filtration, and other steps
-
with PEG 3350 (25% w/v) and bis(2-hydroxyethyl)aminotris(hydroxymethyl)methane (Bis-Tris)/HCl buffer (0.1 m, pH 6.5)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, analysis, and comparisons
expressed in Escherichia coli
expressed in Escherichia coli strain BL21
expression in Escherichia coli
expression in Saccharomyces cerevisiae lacking the activites of endogenous trehalases Nth1, Nth2, or Ath1
-
gene ATC1, DNA and amino acid sequence determination and analysis, expression pattern, subcloning in Escherichia coli, in vitro transcription and translation of HA-tagged enzyme using an Escherichia coli-derived system
-
gene treH is organized in a gene cluster with the other two genes of the trehalose metabolism pathway, treZ and treY encoding malto-oligosyltrehalose trehalohydrolase and maltooligosyltrehalose synthase, DNA and amino acid sequence determination and analysis, overview. Expression of the N-terminally His-tagged active enzyme in Escherichia coli
isozyme SfTre1, cDNA library preparation, DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, expression in Escherichia coli strain BL21(DE3)
isozyme SfTre2, cDNA library preparation, DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, expression in Escherichia coli strain BL21(DE3)
soluble trehalase gene SeTre-1, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, developmental expression pattern of the two trehalase genes SeTre-1 and SeTre-2, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
20-hydroxyecdysone induces the soluble trehalase isozyme encoded by gene NlTre1
after a challenge of starvation, the intestinal Hl-Tre mRNA levels are observed to be first decreased and partially recovered thereafter
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
in embryonic and larval stages, the transcript levels of Hl-Tre decreases during embryonic development and increases after the pentactula stage
no induction by 20-hydroxyecdysone of the membrane-bound trehalase isozyme encoded by gene NlTre2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
trehalase inhibition is a potential insecticidal strategy. Validamycin A is recommended as a prospective value-added ingredient to commercial bio-pesticide formulations
biotechnology
diagnostics
a trehalase-based biosensor platform offers a versatile and convenient method for point-of-care applications as it does not require sample preparation or handling and can be integrated with existing glucometers or sensors
medicine
synthesis
-
expression as a fusion protein with an N-terminal or C-terminal hexahistidine tag in a baculovirus-silkworm expression system. Only N-terminally tagged trehalase shows a high activity
biotechnology
-
immobilization of the crude enzyme on chitin resulting in stable, specific, and reusable reactors for application in other biotechnological processes, the immobilized enzyme shows no significant loss of activity being reused 10times and stored at 10°C, in 50 mM sodium maleate, pH 6.0, for 55 days
biotechnology
-
immobilization of the crude enzyme on chitin resulting in stable, specific, and reusable reactors for application in other biotechnological processes, the immobilized enzyme shows no significant loss of activity being reused 10times and stored at 10°C, in 50 mM sodium maleate, pH 6.0, for 55 days
-
medicine
-
analysis of enzyme activities in intestinal mucosal samples. Of 200 patients, most of whom complained of abdominal symptoms and diarrhoea, 18 had total alpha,alpha-trehalase deficiency and 39 had partial deficiency
medicine
-
treatment of weaning rats with lyophilized Saccharomyces boulardii results in significant increase in alpha,alpha-trehalase activity in the endoluminal fluid and the intestinal mucosa. Discussion of oral administration of Saccharomyces boulardii to patients with digestive symptoms caused by trehalose intolerance
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