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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
-
brush
- disaccharidase
- trehalose-6-phosphate
- larvae
- glycogen
- midgut
-
camp-dependent
- glucoamylase
- hemolymph
- validamycin
- isomaltase
- bombyx
- silkworm
- alpha-glucosidase
-
instar
- gamma-glutamyltransferase
- sucrase-isomaltase
-
brush-border
- molitor
-
carbohydrases
-
entomopathogenic
- cellobiase
- microvillar
- metarhizium
- tenebrio
- planthopper
-
diapause
- ascospores
- synthesis
- medicine
- diagnostics
- biotechnology
- analysis
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acid (non regulatory) trehalase, acid non-regulatory trehalase, acid trehalase, alkaline trehalase, alpha,alpha glucoside 1-glucohydrolase, alpha,alpha trehalase, alpha,alpha trehalose glucohydrolase, alpha,alpha'-trehalose 1-D-glucohydrolase, Alpha,alpha-trehalase, Alpha,alpha-trehalose glucohydrolase, 
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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 beta-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
-
both isoforms are highly specific for trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
-
trehalose is one of the major storage carbohydrates in the yeast Saccharomyces cerevisiae
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
highly specific for
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
inverting-type enzyme
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
may play a role in the regulating the carbohydrate allocation in plants
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
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
A0A156C5X3
-
-
-
?
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
-
-
-
?
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
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
A0A2E0NWL6
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
-
the enzyme is involved in incorporation and utilization of trehalose
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
-
the enzyme is essential for growth on trehalose as carbon source, regulation by D-glucose repression
-
-
?
alpha,alpha-trehalose + H2O
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
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
D-glucose
-
highly specific for alpha,alpha-trehalose
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
-
highly specific for alpha,alpha-trehalose
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
-
preferred substrate of acid trehalase
-
-
?
alpha,alpha-trehalose + H2O
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
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
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
-
-
?
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
?
-
A0A2E0NWL6
no activity with sucrose, maltose, lactose or cellobiose
-
-
?
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
2 beta-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
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
-
trehalose is one of the major storage carbohydrates in the yeast Saccharomyces cerevisiae
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
may play a role in the regulating the carbohydrate allocation in plants
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
-
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
A0A156C5X3
-
-
-
?
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
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
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
-
the enzyme is involved in incorporation and utilization of trehalose
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
-
the enzyme is essential for growth on trehalose as carbon source, regulation by D-glucose repression
-
-
?
alpha,alpha-trehalose + H2O
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
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
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
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
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
-
-
?
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
-
-
?
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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
A0A2E0NWL6
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 neutral trehalase in presence of 5 mM trehalose
1,10-phenanthroline
-
inhibits the acid trehalase, 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
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
0.3793
alpha,alpha-trehalose
A0A2E0NWL6
mutant enzyme Y227H/R442G, 50°C, pH 6.0
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
-
433.69
alpha,alpha-trehalose
A0A2E0NWL6
mutant enzyme Y227H/R442G, 50°C, pH 6.0
662
trehalose
recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.6, with 0.01% Triton X-100, at 35°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1143.4
alpha,alpha-trehalose
A0A2E0NWL6
mutant enzyme Y227H/R442G, 50°C, pH 6.0
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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