Information on EC 3.2.1.28 - alpha,alpha-trehalase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.28
-
RECOMMENDED NAME
GeneOntology No.
alpha,alpha-trehalase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
show the reaction diagram
role of carboxyl, guanidine and imidazole groups in catalysis
-
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
show the reaction diagram
nucleophilic double, not single, displacement catalytic forward reaction mechanism via oxocarbenium ion intermediate, detailed overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
metabolism of disaccharids
-
-
Starch and sucrose metabolism
-
-
trehalose degradation II (trehalase)
-
-
trehalose degradation VI (periplasmic)
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acid (non regulatory) trehalase
-
-
acid (non regulatory) trehalase
Schizosaccharomyces pombe 968
-
-
-
acid non-regulatory trehalase
-
-
acid trehalase
A8J4S9
-
acid trehalase
-
-
acid trehalase
-
-
acid trehalase
-
-
acid trehalase
Candida albicans CAI4
-
-
-
acid trehalase
Q307Q4
-
acid trehalase
-
-
acid trehalase
P48016
-
acid trehalase
Saccharomyces cerevisiae MCY1264
-
-
-
acid trehalase
-
-
acid trehalase
Scytalidium thermophilum 77.7.8
-
-
-
alkaline trehalase
-
-
alpha,alpha glucoside 1-glucohydrolase
-
-
alpha,alpha trehalase
A8J4S9
-
alpha,alpha trehalose glucohydrolase
A8J4S9
-
alpha,alpha'-trehalose 1-D-glucohydrolase
-
-
-
-
Alpha,alpha-trehalase
-
-
-
-
Alpha,alpha-trehalose glucohydrolase
-
-
-
-
Alpha,alpha-trehalose glucohydrolase
A1XBT9
-
Alpha,alpha-trehalose glucohydrolase
B5ATV4, Q0ZIF5
-
alpha-glucoside-1-glucohydrolase
J7EJ73
-
alpha-glucoside-1-glucohydrolase
-
-
alpha-glucoside-1-glucohydrolase
-
-
alpha-glucoside-1-glucohydrolase
-
-
Atc1p
-
isoform
Atc1p
Candida albicans CAI4
-
-
-
ATM1
Q307Q4
mature enzyme
GH37 trehalase
-
-
glucose alpha-1,1-glucose hydrolase
P32359
-
membrane-bound SfTre2
B5ATV4
-
MSMEG 4528
Mycobacterium smegmatis b11
-
-
-
neutral regulatory trehalase
-
-
neutral trehalase
-
-
neutral trehalase
Candida albicans CAI4
-
-
-
neutral trehalase
A4QMP6
-
neutral trehalase
Saccharomyces cerevisiae MCY1264
-
-
-
neutral trehalase
-
-
neutral trehalase
Scytalidium thermophilum 77.7.8
-
-
-
Ntc1p
-
isoform
Ntc1p
Candida albicans CAI4
-
-
-
NTH1
A1YQE2
-
SfTre1
Q0ZIF5
-
soluble P I type trehalase
-
-
soluble P II type trehalase
-
-
soluble trehalase
Q0ZIF5
-
Tre-2
A7XZC0
isoform
TRE1
P32359
-
TreA
Escherichia coli K12 DH5alpha
-
-
-
treB
-
gene name
Treh1
D2KHJ0
isoform
Treh2
D2KHI9
isoform
trehalase
-
-
-
-
trehalase
-
-
trehalase
A8J4S9
-
trehalase
Q9SU50
-
trehalase
O42777
-
trehalase
-
-
trehalase
-
-
trehalase
Q9GYK9
-
trehalase
P52494
-
trehalase
J7EJ73
-
trehalase
-
-
trehalase
Q9W2M2
-
trehalase
A4WBE4
-
trehalase
A4WBE4
-
-
trehalase
D4I261
-
trehalase
P13482
-
trehalase
Escherichia coli K12 DH5alpha, Escherichia coli Mph2
-
-
-
trehalase
-
-
trehalase
Q9XEY7
-
trehalase
O43280
-
trehalase
-
-
trehalase
B0CV22, B0DA99
-
trehalase
-
-
trehalase
Q9XGH9
-
trehalase
Q6Q5X7
-
trehalase
A9XE63
-
trehalase
Q9JLT2
-
trehalase
-
-
trehalase
Mycobacterium smegmatis b11
-
-
-
trehalase
O42783
-
trehalase
Neurospora crassa DSM 1257
O42783
-
-
trehalase
F8MBS5
-
trehalase
D2KWM9
-
trehalase
C0LZJ6, C0LZJ7
-
trehalase
B6ZIV1
-
trehalase
Nostoc punctiforme IAM M-15
B6ZIV1
-
-
trehalase
A6MIZ4
-
trehalase
D8MZ26
-
trehalase
O70282
-
trehalase
-
-
trehalase
A1XBT9
-
trehalase
Scytalidium thermophilum 77.7.8
-
-
-
trehalase
-
-
trehalase
B0M0J3
-
trehalase
B5ATV4
-
trehalase
D2KHI9, D2KHJ0
-
trehalase
-
-
trehalase
-
-
trehalase
P32359
-
trehalase
Q3BXX2
-
trehalase-invertase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-52-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia-0
-
-
Manually annotated by BRENDA team
Blastobotrys adeninivorans SBUG 724
SBUG 724
-
-
Manually annotated by BRENDA team
isozymes trehalase type 1 and 2
-
-
Manually annotated by BRENDA team
treh-1, soluble trehalase
UniProt
Manually annotated by BRENDA team
treh-2, integral membrane trehalase
UniProt
Manually annotated by BRENDA team
gene ATC1
-
-
Manually annotated by BRENDA team
isoform Atc1p; isoform Ntc1p
-
-
Manually annotated by BRENDA team
strain CAI4
-
-
Manually annotated by BRENDA team
Candida albicans CAI4
strain CAI4
-
-
Manually annotated by BRENDA team
var. coprophilum
-
-
Manually annotated by BRENDA team
cultivar Giza 1
-
-
Manually annotated by BRENDA team
strain Mph2
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
Escherichia coli K12 DH5alpha
-
-
-
Manually annotated by BRENDA team
Escherichia coli Mph2
strain Mph2
-
-
Manually annotated by BRENDA team
strain ArI3
-
-
Manually annotated by BRENDA team
strain ArI3
-
-
Manually annotated by BRENDA team
var. thermoidea
-
-
Manually annotated by BRENDA team
isolated from brazilian soil
-
-
Manually annotated by BRENDA team
termites
-
-
Manually annotated by BRENDA team
strain Y55
-
-
Manually annotated by BRENDA team
Komagataella pastoris Y55
strain Y55
-
-
Manually annotated by BRENDA team
Lobosphaera sp.
-
-
-
Manually annotated by BRENDA team
fragment; subspecies Metarhizium anisopliae acridum, strain CQMa102
UniProt
Manually annotated by BRENDA team
strain Ma2575; strain Ma473; strain TIB2-1ii
Uniprot
Manually annotated by BRENDA team
strain SCB1-2i
SwissProt
Manually annotated by BRENDA team
strain SCB2-2i
SwissProt
Manually annotated by BRENDA team
Metarhizium anisopliae Ma2575
strain Ma2575
Uniprot
Manually annotated by BRENDA team
Metarhizium anisopliae Ma473
strain Ma473
Uniprot
Manually annotated by BRENDA team
Metarhizium anisopliae SCB1-2i
strain SCB1-2i
SwissProt
Manually annotated by BRENDA team
Metarhizium anisopliae SCB2-2i
strain SCB2-2i
SwissProt
Manually annotated by BRENDA team
Metarhizium anisopliae TIB2-1ii
strain TIB2-1ii
Uniprot
Manually annotated by BRENDA team
strain SCB1-2i
-
-
Manually annotated by BRENDA team
Metarhizium flavoviride SCB1-2i
strain SCB1-2i
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis b11
strain B11
-
-
Manually annotated by BRENDA team
neutral trehalase
Uniprot
Manually annotated by BRENDA team
Neurospora crassa DSM 1257
-
Uniprot
Manually annotated by BRENDA team
NlTre-1; brown planthopper, gene NlTre-1 encoding the soluble isozyme
UniProt
Manually annotated by BRENDA team
NlTre-2; brown planthopper, gene NlTre-2 encoding the membrane-bound isozyme
UniProt
Manually annotated by BRENDA team
strain IAM M-15, gene treH
UniProt
Manually annotated by BRENDA team
Nostoc punctiforme IAM M-15
strain IAM M-15, gene treH
UniProt
Manually annotated by BRENDA team
2 nonglycoprotein enzyme forms: A1 and B1 and 2 glycoprotein enzyme form A2 and B2
-
-
Manually annotated by BRENDA team
strain DSM 4252T
-
-
Manually annotated by BRENDA team
isoform Ath1
-
-
Manually annotated by BRENDA team
neutral Nth1 and Nth2 and acid Ath1, encoded by gene ath1
-
-
Manually annotated by BRENDA team
strain MCY1264, neutral trehalase and acid trehalase isozymes encoded by the NTH1 and ATH1 genes
-
-
Manually annotated by BRENDA team
strain S288c
-
-
Manually annotated by BRENDA team
two enzyme activities, C-trehalase and V-trehalase
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae MCY1264
strain MCY1264, neutral trehalase and acid trehalase isozymes encoded by the NTH1 and ATH1 genes
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe 968
strain 968
-
-
Manually annotated by BRENDA team
intracellular and extracellular threhalase
-
-
Manually annotated by BRENDA team
strain 77.7.8, isolated from indian soil
-
-
Manually annotated by BRENDA team
Scytalidium thermophilum 77.7.8
strain 77.7.8, isolated from indian soil
-
-
Manually annotated by BRENDA team
genes SeTre-1 and SeTre-2
-
-
Manually annotated by BRENDA team
isoform Tre-2
UniProt
Manually annotated by BRENDA team
membrane-bound trehalase SfTre2; membrane-bound isozyme SfTre2
UniProt
Manually annotated by BRENDA team
soluble trehalase SfTre1; soluble isozyme SfTre1
UniProt
Manually annotated by BRENDA team
Thermomyces lanuginosus RM-B
RM-B
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
-
different functions of the insect soluble and membrane-bound trehalase genes in chitin biosynthesis, overview
metabolism
B6ZIV1
the enzyme catalyzes the last step in the trehalose metabolism and is the key enzyme controlling the pathway in response to water conditions
metabolism
Nostoc punctiforme IAM M-15
-
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
B5ATV4
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
O42783
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q3BXX2
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
Q9W2M2
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
D4I261
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
O43280
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
D8MZ26
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
D2KWM9
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q9XGH9
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
A6MIZ4
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q9GYK9
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
F8MBS5
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
O42777
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q6Q5X7
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q9XEY7
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
P52494
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q9SU50
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
A9XE63
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
B0M0J3
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
O70282
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
Q9JLT2
trehalase function is central in carbon partitioning and energy homeostasis regulation
physiological function
P48016
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
Saccharomyces cerevisiae MCY1264
-
role for Nth2p in the mobilization of intracellular trehalose during salt-stress recovery, overview
-
physiological function
Enterobacter sp. 638, Neurospora crassa DSM 1257
-
trehalase function is central in carbon partitioning and energy homeostasis regulation
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
Q6UDD9, Q6UDE0, Q9HDE9
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
highly specific for
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
may play a role in the regulating the carbohydrate allocation in plants
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
neutral trehalase mobilizes trehalose accumulated by fungal cells as a protective and storage carbohydrate
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
inverting-type enzyme
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
Metarhizium flavoviride SCB1-2i
-
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
Metarhizium anisopliae SCB2-2i
Q6UDD9
-
-
-
?
alpha,alpha-trehalose + H2O
2 beta-D-glucose
show the reaction diagram
-
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
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is essential for growth on trehalose as carbon source, regulation by D-glucose repression
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in incorporation and utilization of trehalose
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
preferred substrate of acid trehalase
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
Mycobacterium smegmatis, Mycobacterium smegmatis b11
-
highly specific for alpha,alpha-trehalose
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
Scytalidium thermophilum 77.7.8
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucopyranose
show the reaction diagram
O42783
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
B5ATV4, Q0ZIF5
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
Q0ZIF5
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
A1YQE2
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
trehalose is one of the major storage carbohydrates in the yeast Saccharomyces cerevisiae
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucose + beta-D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
J7EJ73
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D2KHI9, D2KHJ0
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
P32359
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
B5ATV4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O42783
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q3BXX2
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9W2M2
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D4I261
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O43280
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D8MZ26
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D2KWM9
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9XGH9
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A6MIZ4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9GYK9
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
B0CV22, B0DA99
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
F8MBS5
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O42777
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q6Q5X7
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9XEY7
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
P52494
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9SU50
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A9XE63
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
B0M0J3
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O70282
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9JLT2
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
P48016
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Neurospora crassa DSM 1257
O42783
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Escherichia coli K12 DH5alpha
-
-
-
-
?
alpha-alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
cellobiose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
A1YQE2
1.7% of the activity with trehalose
-
-
?
maltose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
melibiose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
raffinose + H2O
?
show the reaction diagram
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
A1YQE2
5.7% of the activity with trehalose
-
-
?
sucrose + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
P13482
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Lobosphaera sp.
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
A4QMP6
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
A8J4S9
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
absolute specificity
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
absolute specificity
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
absolute specificity
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
absolute specificity
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
absolute specificity
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
absolute specificity
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
pathway of trehalose utilization
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
osmotically inducible enzyme
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
the trehalase is strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. The enzyme may be present in a constitutive form without the requirement for a specific inducer
-
-
trehalose + H2O
D-glucose
show the reaction diagram
Q307Q4
high specificity for trehalose
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
A1XBT9
high specificity for trehalose
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Q307Q4
highly specific for trehalose
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Thermomyces lanuginosus RM-B
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Candida albicans CAI4
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Komagataella pastoris Y55
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Escherichia coli K12
-
osmotically inducible enzyme
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Blastobotrys adeninivorans SBUG 724
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Schizosaccharomyces pombe 968
-
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
B6ZIV1
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
C0LZJ6, C0LZJ7
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
Nostoc punctiforme IAM M-15
B6ZIV1
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
Saccharomyces cerevisiae MCY1264
-
-
-
-
?
melizitose + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
show the reaction diagram
-
weak
-
-
?
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
?
-
-
transcriptional and post-translational regulation of neutral trehalase in Schizosaccharomyces pombe during thermal stress
-
-
-
additional information
?
-
-
no activity with alpha,beta-trehalose and 6-beta-glucosyl-trehalose
-
-
-
additional information
?
-
-
no activity of acid trehalase with lactose and turanose
-
-
-
additional information
?
-
-
does not hydrolyze alpha,beta-trehalose, beta,beta-trehalose, trehalose dimycolate, or any other alpha-glucoside or beta-glucoside
-
-
-
additional information
?
-
Q307Q4
does not hydrolyze cellobiose, maltose, sucrose, lactose, p-nitrophenyl galactopyranoside, p-nitrophenyl alpha-glucopyranoside, or p-nitrophenyl beta-glucopyranoside
-
-
-
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
?
-
-
role of acid trehalase Ath1 in intracellular trehalose mobilization and in saline stress resistance
-
-
-
additional information
?
-
O42783
enzyme is absolutely specific for trehalose
-
-
-
additional information
?
-
B6ZIV1
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
-
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
?
-
A1YQE2
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
?
-
Mycobacterium smegmatis b11
-
does not hydrolyze alpha,beta-trehalose, beta,beta-trehalose, trehalose dimycolate, or any other alpha-glucoside or beta-glucoside
-
-
-
additional information
?
-
Nostoc punctiforme IAM M-15
B6ZIV1
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
may play a role in the regulating the carbohydrate allocation in plants
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose
show the reaction diagram
-
neutral trehalase mobilizes trehalose accumulated by fungal cells as a protective and storage carbohydrate
-
-
?
alpha,alpha-trehalose + H2O
2 beta-D-glucose
show the reaction diagram
-
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
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is essential for growth on trehalose as carbon source, regulation by D-glucose repression
-
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in incorporation and utilization of trehalose
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
B5ATV4, Q0ZIF5
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
trehalose is one of the major storage carbohydrates in the yeast Saccharomyces cerevisiae
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucose + beta-D-glucose
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
J7EJ73
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D2KHI9, D2KHJ0
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
P32359
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
B5ATV4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O42783
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q3BXX2
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9W2M2
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D4I261
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O43280
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D8MZ26
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
D2KWM9
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9XGH9
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A6MIZ4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9GYK9
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
B0CV22, B0DA99
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
F8MBS5
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O42777
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q6Q5X7
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9XEY7
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
P52494
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9SU50
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A9XE63
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
B0M0J3
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
O70282
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Q9JLT2
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
P48016
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
A4WBE4
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Neurospora crassa DSM 1257
O42783
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
Escherichia coli K12 DH5alpha
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
pathway of trehalose utilization
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
osmotically inducible enzyme
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
the trehalase is strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. The enzyme may be present in a constitutive form without the requirement for a specific inducer
-
-
trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
B6ZIV1
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
C0LZJ6, C0LZJ7
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
Nostoc punctiforme IAM M-15
B6ZIV1
-
-
-
?
trehalose + H2O
2 D-glucose
show the reaction diagram
Saccharomyces cerevisiae MCY1264
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
-
trehalase activity in crude extracts increases over time when cells are induced to fix nitrogen
-
?
trehalose + H2O
D-glucose
show the reaction diagram
Escherichia coli K12
-
osmotically inducible enzyme
-
?
alpha,alpha-trehalose + H2O
D-glucose
show the reaction diagram
Scytalidium thermophilum 77.7.8
-
-
-
-
?
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
?
-
-
transcriptional and post-translational regulation of neutral trehalase in Schizosaccharomyces pombe during thermal stress
-
-
-
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
?
-
-
role of acid trehalase Ath1 in intracellular trehalose mobilization and in saline stress resistance
-
-
-
additional information
?
-
B6ZIV1
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
-
additional information
?
-
-
trehalose-invertase is specific for both sucrose and trehalose. The ratio between trehalase and invertase activity is 1:3.5
-
-
-
additional information
?
-
Nostoc punctiforme IAM M-15
B6ZIV1
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
C-trehalase is absolutely dependent on Ca2+ or Mn2+. 4fold activation of C-trehalase at 2.5 mM CaCl2
Ca2+
-
2.5-5.0 mM CaCl2, slight stimulation
Ca2+
-
activates
Ca2+
-
stimulates
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
Ca2+
-
stimulates
Ca2+
-
activates
Ca2+
-
activates, dependent on pH
Ca2+
-
weak stimulation
Ca2+
O42783
absolutely required
CaCl2
-
10 mM, activates 1.2fold
Co2+
-
slight stimulation
Co2+
-
activates
Co2+
-
stimulates
Co2+
-
activates the acid trehalase
Co2+
-
122% activity at 20 mM
Gentiobiose
-
activates the neutral trehalase
iodoacetate
-
10 mM, activates 1.3fold
K+
-
30% activation by 100 mM KCl, V-trehalase
K+
-
optimal stimulation from 100-200 mM
K+
-
activates the acid trehalase
KNO3
-
10 mM, activates 2.2fold
Li+
-
activates the acid trehalase
Mg2+
-
2.5-5.0 mM MgCl2, slight stimulation
Mg2+
-
activates the acid trehalase by about 30%
Mg2+
-
absolutely required for activity, optimum activity occurring at concentrations of 3.5-4 mM
Mg2+
-
133% activity at 20 mM
MgCl2
-
10 mM, activates 2.4fold
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
Mn2+
-
activates
Mn2+
-
stimulates
Mn2+
-
activates, required
Mn2+
-
activates the acid trehalase by about 30%
Mn2+
-
weak stimulation
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
Na+
-
optimal stimulation from 100-200 mM
Na+
-
activates the acid trehalase by about 30%
NaCl
-
10 mM, activates 1.4fold
NaCl
-
activating at 0.5 mM
NH4+
-
optimal stimulation from 100-200 mM
Ni2+
-
122% activity at 20 mM
phloretin
-
activates the neutral trehalase in presence of 5 mM trehalose
Zn2+
-
2.5-5.0 mM ZnCl2, slight stimulation
Mn2+
-
210% activity at 20 mM
additional information
-
cytoplasmic enzyme has no metal dependency
additional information
-
Zn2+, Ca2+, Mg2+, Fe3+, EDTA, and 4-chloromercuribenzoate have different effects on alkaline trehalase and acid trehalases
additional information
-
Mg2+ can not be replaced by Ca2+, Mn2+ or Zn2+
additional information
-
not activated by Ca2+
INHIBITORS
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
-
casuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
-
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
-
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-homocasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(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
J7EJ73
micromolar inhibitor
-
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
-
micromolar inhibitor
-
1,3-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)propane-1,3-dione
J7EJ73
micromolar inhibitor
-
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
J7EJ73
micromolar inhibitor
-
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
-
micromolar inhibitor
-
1-deoxynojirimycin
J7EJ73
-
1-deoxynojirimycin
-
-
1-thiatrehazolin
-
-
7-deoxycasuarine
-
-
7-homocasuarine
-
-
acetate
-
strong inhibition by acetic acid/acetate buffer, V-trehalase
ADP
-
Ca2+ abolishes inhibitory effect
ADP
-
1 mM, 53% inhibition
Ag+
O42783
-
Al3+
-
1 mM AlCl3, complete inhibition
Al3+
-
1 mM, complete inhibition
Al3+
O42783
-
AMP
-
Ca2+ abolishes inhibitory effect
AMP
-
50% inhibition at 20 mM
amygdalin
-
competitive inhibition
amygdalin
P32359
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
-
1 mM, 80% inhibition
ATP
-
90% inhibition at 20 mM
ATP
-
strong
ATP
O42783
-
ATP
-
10% residual activity at 20 mM
Ba+
-
1 mM, complete inhibition
-
Borate
-
16% residual activity at 20 mM
Ca2+
-
1.0 mM CaCl2, 9% loss of activity
Ca2+
-
67% residual activity at 20 mM
CaCl2
B6ZIV1
over 90% inhibition at 10 mM
castanospermine
-
potent, reversible, competitive
castanospermine
-
50% inhibition at 0.5 mg/ml
castanospermine
-
-
casuarine
-
-
casuarine-6-O-alpha-D-glucoside
J7EJ73
-
-
casuarine-6-O-alpha-D-glucoside
-
-
-
cellobiose
-
10 mM, 60% inhibition
Citric acid
-
36.16% residual activity at 5 mM
Co2+
A1XBT9
71% inhibition at 5 mM
Co2+
O42783
-
Cu2+
-
1.0 mM CuSO4, 13% loss of activity
Cu2+
-
1 mM CuSO4, complete inhibition of extracellular enzyme, 47% inhibition of intracellular enzyme
Cu2+
-
1 mM, complete inhibition
Cu2+
Lobosphaera sp.
-
weak inhibition
Cu2+
O42783
-
Cu2+
-
14% residual activity at 20 mM
CuCl2
A1YQE2
20 mM, 20% residual activity
D-glucose
A1XBT9
competitive inhibitor
D-glucose
-
isoform Atc1p is subject to glucose repression, but exhaustion of glucose itself does not increase the activity
deoxynojirimycin
-
inhibition according to a ligand exclusion model
diethyldicarbonate
P32359
the compound modifies a His residue that results in a less active enzyme. After 40 min with 40 mM diethylpyrocarbonate at 30C 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
EDTA
-
1 mM, C-trehalase, complete inhibition
EDTA
-
1 mM, 30% inhibition of extracellular enzyme, 54% inhibition of intracellular enzyme
EDTA
-
1 mM, 55% inhibition
EDTA
-
10 mM, 28% inhibition
EDTA
-
inhibits the acid trehalase by 70%
EDTA
A1XBT9
moderate inhibitory level at 5 mM
EDTA
A1YQE2
20 mM, 50% residual activity
EDTA
-
18.18% residual activity at 5 mM
EDTA
-
16% residual activity at 20 mM
EGTA
A1YQE2
20 mM, 55% residual activity
Fe3+
Lobosphaera sp.
-
-
Fe3+
-
inhibits the acid trehalase by 50%
Fe3+
-
31% residual activity at 20 mM
FeCl3
-
10 mM, 35% inhibition
Gentiobiose
-
slight inhibition of acid trehalase
glucono-delta-lactone
P32359
linear competitive inhibitor
glucose
-
-
H2O2
-
inhibitory at 5-50 mM
Hg+
-
inhibits the acid trehalase by 95%
Hg2+
-
10 mM HgCl2, 30% loss of activity
Hg2+
-
0.11 mM HgCl2. Cl- protects from inactivation by HgCl2
Hg2+
-
the glycoprotein enzyme forms are more susceptible than the nonglycoprotein forms
Hg2+
-
1 mM, 58% inhibition
Hg2+
-
2 mM HgCl2, 61.7% inhibition
Hg2+
-
0.1 mM, complete inhibition
Hg2+
-
1 mM HgCl2, complete inhibition
Hg2+
-
1 mM, complete inhibition
iodoacetamide
-
100 mM required for inhibition of more than 50%
K+
-
100 mM KCl, 65% inhibition of C-trehalase
K+
-
0.5 M KCl, activity is 2fold lower
K+
-
69% residual activity at 20 mM
KH2PO4
-
10.32% residual activity at 200 mM
Li+
-
12% residual activity at 20 mM
malate
-
37% residual activity at 20 mM
Mandelonitrile
-
competitive inhibition
Mandelonitrile
P32359
mixed-type non-competitive inhibitor
mannitol
-
partial
mannitol
-
competitive inhibitor, 8% residual activity at 20 mM
Mannose
-
-
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 beta-glucoside
-
-
methyl-alpha-D-mannoside
P32359
linear competitive inhibitor
methyl-alpha-glucoside
-
slight inhibition of acid trehalase
methyl-alpha-glucoside
-
weak competitive inhibition
methyl-alpha-mannoside
-
weak competitive inhibition
Mg2+
-
1.0 mM MgCl2, 13% loss of activity
Mg2+
-
1 mM MgCl2, 30% inhibition
Mg2+
A1XBT9
moderate inhibitory level at 5 mM
Mg2SO4
-
57.02% residual activity at 2 mM
-
MgCl2
-
50 mM, C-trehalase, complete inhibition
MgCl2
B6ZIV1
over 90% inhibition at 10 mM
MgCl2
A1YQE2
20 mM, 60% residual activity
MgSO4
B6ZIV1
over 90% inhibition at 20 mM
Mn2+
Lobosphaera sp.
-
weak
Mn2+
A1XBT9
moderate inhibitory level at 5 mM
Na+
-
0.5 M NaCl, activity is 2fold lower
Na+
-
61% residual activity at 20 mM
NaCl
B6ZIV1
strong inhibition at 10 mM, treatment of cells leads to accumulation of trehalose
NEM
-
2 mM, 8.4% inhibition
NH4Cl
-
1 mM NH4Cl, 22% inhibition of extracellular enzyme, 27% inhibition of intracellular enzyme
p-Aminophenyl-beta-D-glucoside
-
-
p-nitrophenyl-beta-D-glucoside
-
-
p-nitrophenyl-beta-D-glucoside
-
-
PCMB
-
2 mM, 30.1% inhibition
PCMB
-
1 mM is required for inhibition of more than 50%
PCMB
-
1 mM, 30% inhibition
phenyl-beta-D-glucoside
-
-
phloretin
-
inhibits the acid trehalase, inhibits the neutral trehalase in presence of 20 mM trehalose
phloretin
P32359
linear competitive inhibitor
phlorizin
-
2.4 mM
phlorizin
-
2 mM, 20% inhibition
phlorizin
-
hyperbolic uncompetitive, binds only to enzyme-substrate complex
phlorizin
P32359
i.e. glucose-phloretin, linear competitive inhibitor
phosphate
-
Ca2+ abolishes inhibitory effect
Polyphosphate
-
-
potassium glutamate
-
0.5 M KCl, activity is 2fold lower
prunasin
-
competitive inhibition
prunasin
P32359
i.e glucose-beta-mandelonitrile, linear competitive inhibitor
Salicin
-
competitive inhibition
Salicin
P32359
linear competitive inhibitor
SDS
-
1.0%, 80% inhibition
sodium orthovanadate
-
80% inhibition at 10 mM
succinate
-
41% residual activity at 20 mM
Sucrose
-
-
Sucrose
-
competitive
Sucrose
-
competitive
Sucrose
-
-
Sucrose
-
10 mM, 60% inhibition
Sucrose
Lobosphaera sp.
-
25 mM, 33% inhibition; competitive
Sucrose
-
competitive
trehazolin
Q307Q4
-
trehazolin
Q307Q4
specific inhibitor
trehazolin
J7EJ73
-
trehazolin
-
-
Tris
-
3.8 mM, competitive
Tris
-
competitive
Tris
-
100 mM, 28% inhibition
Tris
-
competitive
Tris
-
100 mM, 92% inhibition
Tris
-
10 mM, complete inhibition
Tris
-
competitive
Tris
B6ZIV1
almost complete inhibition at 5 mM
Urea
-
10 mM, 6% inhibition
UTP
-
90% inhibition at 10 mM
validamycin
-
competitive
validamycin A
-
potent, reversible, competitive, slow-binding nature
validamycin A
-
potent, time-dependent
validamycin A
-
-
validamycin A
-
inhibits the acid trehalase
validamycin A
-
competitive
validamycin A
-
competitive inhibitor, 49% residual activity at 5 nM
validamycin B
-
-
Validoxylamine A
-
potent, time-dependent
Validoxylamine A
-
-
Validoxylamine A
-
-
Validoxylamine A
-
complete inhibition
Validoxylamine A
J7EJ73
-
Validoxylamine A
-
-
validoxylamine B
-
-
Zn2+
A1XBT9
95% inhibition at 5 mM
Zn2+
-
non-competitive inhibitor, 22% residual activity at 20 mM
Zn2SO4
-
2.06% residual activity at 10 mM
-
ZnCl2
-
0.1 mM, C-trehalase, complete inhibition
ZnCl2
A1YQE2
20 mM, 40% residual activity
ZnSO4
-
10 mM, 34% inhibition
MnCl2
B6ZIV1
over 90% inhibition at 10 mM
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
-
reaction product D-glucose suppresses enzyme expression
-
additional information
A1XBT9
Ca2+ has no significant inhibitory effect at 5 mM
-
additional information
-
40 mM sodium fluoride and trehazolin have no inhibitory effect
-
additional information
-
sodium arsenate (45 mM), carbonyl cyanide m-chlorophenylhydrazone (0.14 mM), and sodium fluoride (28 mM) do not inhibit the activity
-
additional information
-
not inhibited by ATP, acetate and EDTA
-
additional information
-
insensitive to ATP, cyclic AMP or divalent cations
-
additional information
B6ZIV1
the enzyme activity is reduced under water-stress
-
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
P32359
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
-
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
amygdalin
-
induces the enzyme in different organs, e.g. Malphigian tubules, midgut, fat body, hemolymph, and body wall, when feeded to larvae
betaine
-
activates
esculin
-
induces the enzyme in different organs, e.g. Malphigian tubules, midgut, fat body, hemolymph, and body wall, when feeded to larvae
phosphate
-
activates
MgATP2-
-
C-trehalase can be activated by MgATP2- in presence of cAMP
additional information
-
the cryptic enzyme form is completely activated at protein concentrations higher than 60 mg/ml
-
additional information
-
activation by cAMP-dependent protein kinase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
alpha,alpha-trehalose
Q0ZIF5
mutant R222A/R287A, pH 7.0, 30C
0.109
alpha,alpha-trehalose
-
pH 6.3, 37C
0.16
alpha,alpha-trehalose
-
signal sequenceless TreA
0.2
alpha,alpha-trehalose
-
pH 4.5, 45C
0.22
alpha,alpha-trehalose
Q0ZIF5
mutant E520A, pH 7.0, 30C; mutant R287A, pH 7.0, 30C
0.3
alpha,alpha-trehalose
Q0ZIF5
wild-type, pH 7.0, 30C
0.31
alpha,alpha-trehalose
-
periplasmic TreA
0.35
alpha,alpha-trehalose
-
pH 5.4, 37C, recombinant protein with N-terminal His-tag
0.38
alpha,alpha-trehalose
-
-
0.43
alpha,alpha-trehalose
P32359
at pH 6.0 and 30C
0.44
alpha,alpha-trehalose
-
pH 5.5, 30C
0.45
alpha,alpha-trehalose
Q0ZIF5
mutant R169A, pH 7.0, 30C
0.47
alpha,alpha-trehalose
-
pH 6.0, 30C
0.47
alpha,alpha-trehalose
B5ATV4, Q0ZIF5
isozyme SfTre1
0.48
alpha,alpha-trehalose
-
pH 6.5, 30C
0.5
alpha,alpha-trehalose
-
pH 5.5, 30C, immobilized enzyme
0.52
alpha,alpha-trehalose
-
pH 7.5, 30C
0.66
alpha,alpha-trehalose
-
-
1
alpha,alpha-trehalose
Q0ZIF5
mutant D322A, pH 7.0, 30C
1.11
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
1.32
alpha,alpha-trehalose
-
pH 5.5, 30C, soluble enzyme
1.34
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
1.37
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
1.42
alpha,alpha-trehalose
-
in 50 mM phosphate buffer, at pH 5.5 and 37C
1.5
alpha,alpha-trehalose
-
cytoplsmic wild-type treF
1.54
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
1.6
alpha,alpha-trehalose
B5ATV4, Q0ZIF5
isozyme SfTre2
1.74
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
1.77
alpha,alpha-trehalose
-
-
3.33
alpha,alpha-trehalose
Q0ZIF5
mutant R222A, pH 7.0, 30C
3.64
alpha,alpha-trehalose
-
at pH 5.5 and 55C
6.6
alpha,alpha-trehalose
-
-
11.78
alpha,alpha-trehalose
-
-
20
alpha,alpha-trehalose
-
at 37C
0.0109
trehalose
-
in 50 mM acetate buffer, pH 4.6, at 30C
0.031
trehalose
-
pH 3.3, 37C
0.13
trehalose
-
-
0.156
trehalose
-
-
0.16
trehalose
A1XBT9
at 65C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
0.22
trehalose
-
-
0.27
trehalose
A1XBT9
at 88C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
0.4
trehalose
-
-
0.41
trehalose
-
at 37C in sodium maleate buffer (75 mM, pH 5.5)
0.44
trehalose
-
soluble trehalase P II, inacetate buffer, pH 5.5, at 30C
0.5
trehalose
-
-
0.52
trehalose
-
-
0.52
trehalose
-
recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.6, with 0.01% Triton X-100, at 35C
0.57
trehalose
-
-
0.6
trehalose
Lobosphaera sp.
-
-
0.63
trehalose
-
presence of Ca2+
0.666
trehalose
-
-
0.67
trehalose
-
-
0.8
trehalose
-
extracellular enzyme
0.89
trehalose
-
-
0.9
trehalose
-
cell wall-bound enzyme
1
trehalose
-
intracellular enzyme
1.2
trehalose
-
-
1.4
trehalose
-
V-trehalase
1.56
trehalose
-
soluble trehalase P I, in acetate buffer, pH 5.5, at 30C
1.8
trehalose
-
-
1.9
trehalose
-
cytoplasmic enzyme
2.1
trehalose
-
-
2.24
trehalose
-
intracellular enzyme
2.3
trehalose
-
-
2.3
trehalose
Q307Q4
in 20 mM MES buffer, pH 5.5, at 30C
2.3
trehalose
Q307Q4
native enzyme, in 20 mM MES, pH 6.0 for 10 min at 30C
2.6
trehalose
Q307Q4
recombinant enzyme, in 20 mM MES, pH 6.0 for 10 min at 30C
3.1
trehalose
-
-
3.15
trehalose
-
enzyme form kidney, intestine and amniotic fluid
3.3
trehalose
-
detergent-solubilized trehalase
3.5
trehalose
-
pH 6.0
3.58
trehalose
-
extracellular enzyme
3.6
trehalose
-
proteinase-treated trehalase
4.2
trehalose
-
-
4.7
trehalose
-
-
4.7
trehalose
-
-
4.79
trehalose
-
in absence of trehalose-c
5.28
trehalose
-
in presence of trehalose-c
5.4
trehalose
-
-
5.5
trehalose
-
phosphate buffer, pH 5.7
5.7
trehalose
-
C-trehalase
8
trehalose
-
actetate buffer, pH 5.0
10
trehalose
-
apparent value, at pH 7.1
11
trehalose
-
actetate buffer, pH 5.7
18
trehalose
B6ZIV1
pH 7.5, 37C, recombinant enzyme
55
trehalose
-
trehalase from activated spores
42
alpha,alpha-trehalose
O42783
pH 7.0, 30C
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
-
kinetics
-
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00045
alpha,alpha-trehalose
Q0ZIF5
mutant R222A/R287A, pH 7.0, 30C
0.0005
alpha,alpha-trehalose
Q0ZIF5
mutant E520A, pH 7.0, 30C
0.0009
alpha,alpha-trehalose
Q0ZIF5
mutant R287A, pH 7.0, 30C
0.12
alpha,alpha-trehalose
Q0ZIF5
mutant R169A, pH 7.0, 30C
0.18
alpha,alpha-trehalose
Q0ZIF5
mutant D322A, pH 7.0, 30C
0.3
alpha,alpha-trehalose
Q0ZIF5
mutant R222A, pH 7.0, 30C
0.67
alpha,alpha-trehalose
-
-
0.91
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
0.94
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
0.99
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
1.02
alpha,alpha-trehalose
Q6UDD9, Q6UDE0, Q9HDE9
-
167
trehalose
-
-
199
trehalose
-
at 37C in sodium maleate buffer (75 mM, pH 5.5)
662
trehalose
-
recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.6, with 0.01% Triton X-100, at 35C
730
alpha,alpha-trehalose
Q0ZIF5
wild-type, pH 7.0, 30C
additional information
additional information
-
the molecular activity is 86.2 per s
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
alpha,alpha-trehalose
Q0ZIF5
mutant R222A/R287A, pH 7.0, 30C
589
0.009
alpha,alpha-trehalose
Q0ZIF5
mutant R222A, pH 7.0, 30C
589
0.027
alpha,alpha-trehalose
Q0ZIF5
mutant E520A, pH 7.0, 30C
589
0.045
alpha,alpha-trehalose
Q0ZIF5
mutant R287A, pH 7.0, 30C
589
0.18
alpha,alpha-trehalose
Q0ZIF5
mutant D322A, pH 7.0, 30C
589
0.27
alpha,alpha-trehalose
Q0ZIF5
mutant R169A, pH 7.0, 30C
589
2400
alpha,alpha-trehalose
Q0ZIF5
wild-type, pH 7.0, 30C
589
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000066
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000011
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
pH not specified in the publication, temperature not specified in the publication
0.000012
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
pH not specified in the publication, temperature not specified in the publication
0.0053
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
pH 6.5, 30C
0.0093
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
pH 6.5, 30C
0.0256
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
pH 6.5, 30C
0.0554
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
pH 6.5, 30C
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
0.000009
1-thiatrehazolin
-
at 37C in sodium maleate buffer (75 mM, pH 5.5)
0.00059
7-deoxycasuarine
-
pH 6.5, 30C
0.0117
7-deoxycasuarine
-
pH 6.5, 30C
0.033
7-homocasuarine
-
pH 6.5, 30C
0.107
7-homocasuarine
-
pH 6.5, 30C
0.21
amygdalin
-
pH 6.0, 30C
0.22
amygdalin
P32359
at pH 6.0 and 30C
0.00486
castanospermine
-
pH 6.5, 30C
0.00012
casuarine
-
pH 6.5, 30C
7
D-glucose
A1XBT9
at 65C, in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
0.00139
deoxynojirimycin
-
pH 6.5, 30C
1.4
glucono-delta-lactone
P32359
at pH 6.0 and 30C
1.14
Mandelonitrile
-
pH 6.0, 30C
9
mannitol
-
at pH 5.5 and 55C
0.043
methyl-alpha-D-mannoside
P32359
at pH 6.0 and 30C
89
methyl-alpha-glucoside
-
pH 6.0, 30C
0.008
phloretin
P32359
at pH 6.0 and 30C
0.09
phlorizin
-
pH 6.0, 30C
0.5
phlorizin
P32359
at pH 6.0 and 30C
0.43
prunasin
P32359
at pH 6.0 and 30C
0.92
prunasin
-
pH 6.0, 30C
19
Salicin
-
pH 6.0, 30C
190
Salicin
P32359
at pH 6.0 and 30C
15
Sucrose
-
-
0.55
Tris
-
pH 6.0, 30C
0.000045
validamycin
-
-
0.000004
validamycin A
-
at pH 5.5 and 55C
0.4
validamycin A
-
pH 3.3, 37C, versus trehalose
0.27
validamycin B
-
pH 3.3, 37C, versus trehalose
0.00001
Validoxylamine A
-
at 37C in sodium maleate buffer (75 mM, pH 5.5)
0.0032
Validoxylamine A
-
pH 3.3, 37C, versus trehalose
0.0103
validoxylamine B
-
pH 3.3, 37C, versus trehalose
7
Zn2+
-
at pH 5.5 and 55C
6.2
methyl-alpha-mannoside
-
pH 6.0, 30C
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0106
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
pH 6.5, 30C
0.019
(2R,3R,4R)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidine
-
pH 6.5, 30C
0.0524
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
pH 6.5, 30C
0.1108
(2R,3R,4R,5R)-3,4-dihydroxy-2-(hydroxymethyl)-5-methylpyrrolidine
-
pH 6.5, 30C
0.0061
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
J7EJ73
at pH 6.9 and 30C
-
0.024
1,2-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)ethane-1,2-dione
-
at pH 6.9 and 30C
-
0.223
1,3-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)propane-1,3-dione
J7EJ73
at pH 6.9 and 30C
-
0.011
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
J7EJ73
at pH 6.9 and 30C
-
0.076
1,4-bis((2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl)butane-1,4-dione
-
at pH 6.9 and 30C
-
0.00283
1-deoxynojirimycin
J7EJ73
at pH 6.9 and 30C
0.00596
1-deoxynojirimycin
-
at pH 6.9 and 30C
0.0012
7-deoxycasuarine
-
pH 6.5, 30C
0.0215
7-deoxycasuarine
-
pH 6.5, 30C
0.0655
7-homocasuarine
-
pH 6.5, 30C
0.214
7-homocasuarine
-
pH 6.5, 30C
0.00993
castanospermine
-
pH 6.5, 30C
0.00025
casuarine
-
pH 6.5, 30C
0.000013
trehazolin
Q307Q4
in 20 mM MES buffer, pH 5.5, at 30C
0.000013
trehazolin
Q307Q4
native enzyme, in 20 mM MES, pH 6.0, at 30C
0.000019
trehazolin
Q307Q4
recombinant enzyme, in 20 mM MES, pH 6.0, at 30C
0.00283
deoxynojirimycin
-
pH 6.5, 30C
additional information
additional information
-
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
-
soluble trehalase P I from supernatant, in acetate buffer, pH 5.5, at 30C; soluble trehalase P II from supernatant, in acetate buffer, pH 5.5, at 30C
0.01
-
supernatant, at pH 7.0 and 30C
0.226
P32359
supernatant, at pH 6.0 and 30C
0.227
-
cell extract, at 37C
0.405
-
after 40fold purification, at pH 7.0 and 30C
0.5
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
0.5
-
crude extract, at pH 5.5 and 55C
0.531
-
-
1.03
-
soluble trehalase P I after 86.9fold purification, in acetate buffer, pH 5.5, at 30C
1.224
Q307Q4
culture filtrate, in 20 mM MES buffer, pH 5.5, at 30C
2.9
-
soluble trehalase P II after 245.7fold purification, in acetate buffer, pH 5.5, at 30C
6.2
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
12.2
C0LZJ6, C0LZJ7
membrane-bound isozyme
16.67
P32359
after 74fold purification, at pH 6.0 and 30C
36.99
-
after 162fold purification, at 37C
39.4
C0LZJ6, C0LZJ7
soluble isozyme
50
-
free enzyme
53.4
-
solubilized enzyme
80 - 150
O42783
pH 7.0, 30C
101.3
Q307Q4
recombinant enzyme, after purification, at 30C
117
-
after 232fold purification, at pH 5.5 and 55C
120
Q307Q4
after 98.04fold purification, in 20 mM MES buffer, pH 5.5, at 30C
120
Q307Q4
native enzyme, after purification, at 30C
144.7
-
pH 5.4, 37C, recombinant protein with N-terminal His-tag
168
-
purified enzyme
175.7
-
purified acid trehalase
278
-
-
343
-
intestine
1775
-
extracellular enzyme
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Lobosphaera sp.
-
-
additional information
-
activities of neutral and acid trehalase at different pH values and temperatures
additional information
B6ZIV1
determination of trehalose contents in differently treated cells, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.3
-
-
3.5
-
a minor activity maximum at pH 3.5 and a major activity maximum at pH 6.5
3.9
-
acid trehalase
4 - 5
-
V-trehalase, at 40 mM trehalose
4.3
-
intestinal acid trehalase
4.5 - 5.3
-
-
4.7
-
acetate buffer
5 - 5.5
-
-
5
-
muscle acid trehalase
5.3
P32359
-
5.5 - 5.7
-
-
5.5
Lobosphaera sp.
-
-
5.5
-
immobilized enzyme
5.5
-
soluble trehalase P II
5.5
-
recombinant protein with N-terminal His-tag
5.6
-
sodium acetate buffer
5.7
-
phosphate buffer or histidine buffer
5.8 - 6
-
-
5.8 - 6
-
phosphate buffer
6
-
extracellular and intracellular enzyme
6
-
assay at
6
Q307Q4
recombinant enzyme
6.5 - 7
-
-
6.5
-
a minor activity maximum at pH 3.5 and a major activity maximum at pH 6.5
6.5
-
soluble trehalase P I
6.7
-
at 40 mM trehalose, C-trehalase
6.7
-
assay at
7.4
-
reproductive system alkaline trehalase
7.4
C0LZJ6, C0LZJ7
assay at; assay at
7.5
B6ZIV1
assay at
additional information
-
acid pH optimum
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 - 4.5
-
activity range
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
3.6 - 6.6
-
-
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 - 7
Q307Q4
-
4.5 - 7.5
Q307Q4
recombinant enzyme
4.5 - 9
-
no activity at pH values less than 4.5 or more than 9.0
4.8 - 8.5
-
pH 4.9: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
recombinant enzyme
30
-
assay at
30
Q307Q4
recombinant enzyme
35
-
assay at
37
-
assay at
37
B6ZIV1
assay at
37
C0LZJ6, C0LZJ7
assay at; assay at
37
-
-
40 - 45
-
soluble trehalase P I
45 - 55
-
-
45
-
muscle acid trehalase
50
-
immobilized enzyme
50
-
above 50C, soluble trehalase P I
55
-
intestinal acid trehalase and reproductive system alkaline trehalase
60
-
extracellular enzyme
60
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
65
-
intracellular enzyme
65
Lobosphaera sp.
-
-
additional information
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
Q307Q4
recombinant enzyme
20 - 45
Q307Q4
-
25 - 60
-
40% of maximal activity at 25C and 60C
30 - 50
-
30C: 80% of maximal activity, 50C: 50% of maximal activity
30 - 65
-
30C: about 65% of maximal activity, 65C: about 40% of maximal activity
35 - 65
-
more than 50% activity between 35 and 65C
40 - 75
-
about 35% of maximal activity at 40C and at 75C
50 - 60
-
50C: 39% of maximal activity, 60C: 44% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
Q307Q4
isoelectric focusing
4.7
Q307Q4
native enzyme, isoelectric focusing
4.75
-
SeTre-1, sequence calculation
4.9
Q307Q4
recombinant enzyme, isoelectric focusing
4.9
D2KHI9, D2KHJ0
isoform Treh1, calculated from amino acid sequence
5.9
D2KHI9, D2KHJ0
isoform Treh2, calculated from amino acid sequence
6
A7XZC0
calculated
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
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Komagataella pastoris Y55
-
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
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe 968
-
-
-
Manually annotated by BRENDA team
D2KHI9, D2KHJ0
-
Manually annotated by BRENDA team
-
activity in nitrogen-fixing pure culture is about 4times greater than in non-fixing cultures
Manually annotated by BRENDA team
-
activity in nitrogen-fixing pure culture is about 4times greater than in non-fixing cultures
-
Manually annotated by BRENDA team
B5ATV4, Q0ZIF5
midgut, isozyme SfTre1 is localized at the secretory vesicles and at the glycocalyx of columnar cells
Manually annotated by BRENDA team
Blastobotrys adeninivorans SBUG 724
-
-
-
Manually annotated by BRENDA team
-
high expression level of isozyme SeTre-1
Manually annotated by BRENDA team
A7XZC0
of fifth instar larvae and pupae
Manually annotated by BRENDA team
-
high expression level of isozyme SeTre-2
Manually annotated by BRENDA team
-
cavity, isozyme type 1
Manually annotated by BRENDA team
-
larval, only soluble
Manually annotated by BRENDA team
-
brush-border membrane
Manually annotated by BRENDA team
-
mucosa of small intestine, small intestine
Manually annotated by BRENDA team
-
microvillus membrane
Manually annotated by BRENDA team
-
acid trehalase
Manually annotated by BRENDA team
-
brush border membrane
Manually annotated by BRENDA team
-
brush-border membrane of cortex
Manually annotated by BRENDA team
-
proximal tubular cells
Manually annotated by BRENDA team
-
fifth instar larvae
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
under normal conditions, expression in root nodule is induced compared with leaf and root
Manually annotated by BRENDA team
-
high expression level of isozyme SeTre-1
Manually annotated by BRENDA team
-
over 60% of total enzyme activity, larval
Manually annotated by BRENDA team
A7XZC0
of feeding-stage larvae, but not in pupae
Manually annotated by BRENDA team
B5ATV4, Q0ZIF5
columnar cells, distribution of membrane-bound trehalase, isozyme SfTre2, along Spodoptera frugiperda midgut cells, overview
Manually annotated by BRENDA team
-
acid trehalase
Manually annotated by BRENDA team
Thermomyces lanuginosus RM-B
-
-
-
Manually annotated by BRENDA team
-
activity is strongly decreased in ectomycorrhizas
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
-
diapause hormone stimulates transcription of the trehalase gene in developing ovaries
Manually annotated by BRENDA team
-
alkaline trehalase
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
under normal conditions, expression in root nodule is induced compared with leaf and root
Manually annotated by BRENDA team
-
downregulation under salt stress. Under normal conditions, expression in root nodule is induced compared with leaf and root
Manually annotated by BRENDA team
-
under normal conditions, expression in root nodule is induced compared with leaf and root. In senescent nodules, the activity decreases
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
free and bound enzyme form
Manually annotated by BRENDA team
-
high expression level of isozyme SeTre-2
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
B5ATV4, Q0ZIF5
columnar cells, distribution of soluble trehalase, isozyme SfTre1, along Spodoptera frugiperda midgut cells, overview
Manually annotated by BRENDA team
additional information
-
distribution in the soluble and membrane fractions of the tissues, overview
Manually annotated by BRENDA team
additional information
-
expression pattern in presence or absence of D-glucose
Manually annotated by BRENDA team
additional information
-
growth on trehalose leads to the Kluyver effect, in contrast to other yeasts
Manually annotated by BRENDA team
additional information
-
no activity in the fat body, distribution in the soluble and membrane fractions of the tissues, overview
Manually annotated by BRENDA team
additional information
-
activity and gene mRNA level at different developmental stages, expression pattern, overview
Manually annotated by BRENDA team
additional information
-
tissue distribution of soluble trehalase SeTre-1, developmental expression pattern of the two trehalase genes SeTre-1 and SeTre-2, overview
Manually annotated by BRENDA team
additional information
D2KHI9, D2KHJ0
isoform Treh1 is not detected in the brain and Malpighian tubules
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
trehalase accounts for 0.1% and 0.3% of total brush-border membrane protein of intestine and kidney, respectively
Manually annotated by BRENDA team
-
apical, anchored by a glycosylphosphatidylinositol-anchor, isozyme type 2
Manually annotated by BRENDA team
-
elevated activity in resting cells or in cultures growing on trehalose or glycerol
Manually annotated by BRENDA team
Candida albicans CAI4, Schizosaccharomyces pombe 968
-
-
-
Manually annotated by BRENDA team
-
TreF. TreF can be exported to the periplasm where it is present in a misfolded and inactive form
Manually annotated by BRENDA team
-
isozyme type 1
Manually annotated by BRENDA team
-
high activity in exponential growth phase, regardless of the carbon source
Manually annotated by BRENDA team
-
soluble-bound isozyme SeTre-2
Manually annotated by BRENDA team
Mycobacterium smegmatis b11
-
-
-
Manually annotated by BRENDA team
-
intracellular and extracellular enzyme
-
Manually annotated by BRENDA team
Blastobotrys adeninivorans SBUG 724
-
-
-
-
Manually annotated by BRENDA team
Scytalidium thermophilum 77.7.8
-
acid trehalase
-
-
Manually annotated by BRENDA team
Lobosphaera sp.
-
-
Manually annotated by BRENDA team
-
intracellular and extracellular enzyme
Manually annotated by BRENDA team
-
the internal trehalase can be separated into a cell wall-bound and a soluble intracellular fraction
Manually annotated by BRENDA team
Blastobotrys adeninivorans SBUG 724
-
the internal trehalase can be separated into a cell wall-bound and a soluble intracellular fraction
-
Manually annotated by BRENDA team
Scytalidium thermophilum 77.7.8
-
neutral trehalase
-
Manually annotated by BRENDA team
-
intestinal and muscle acid acid trehalases
Manually annotated by BRENDA team
P32358, Q3MV18
-
Manually annotated by BRENDA team
-
cell surface, the isozyme type 2 contains one transmembrane segment and lacks the omega site
Manually annotated by BRENDA team
-
the acid trehalase contains either a transmembrane segment or a signal sequence at the N-terminus
Manually annotated by BRENDA team
B5ATV4, Q0ZIF5
bound, isozyme SfTre2
Manually annotated by BRENDA team
-
membrane-bound isozyme SeTre-2
Manually annotated by BRENDA team
C0LZJ6, C0LZJ7
NlTre2, contains a putative transmembrane domain
Manually annotated by BRENDA team
D2KHI9, D2KHJ0
isoform Treh2
Manually annotated by BRENDA team
-
at high osmolarity a periplasmic trehalase is induced
-
Manually annotated by BRENDA team
-
TreA. TrA can fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence
-
Manually annotated by BRENDA team
Escherichia coli Mph2, Enterobacter sp. 638, Escherichia coli K12, Escherichia coli K12 DH5alpha
-
-
-
-
Manually annotated by BRENDA team
P32358, Q3MV18
-
-
Manually annotated by BRENDA team
D2KHI9, D2KHJ0
-
-
Manually annotated by BRENDA team
B5ATV4, Q0ZIF5
isozyme SfTre1
-
Manually annotated by BRENDA team
C0LZJ6, C0LZJ7
NlTre1, the soluble trehalase isozyme accounts for the majority of total trehalase activity
-
Manually annotated by BRENDA team
-
alkaline trehalase
Manually annotated by BRENDA team
additional information
-
bound to particulate fraction
-
Manually annotated by BRENDA team
additional information
-
Ath1 possesses a transmembrane domain. Existence of a secretion sequence in Ath1
-
Manually annotated by BRENDA team
additional information
B5ATV4, Q0ZIF5
immunohistochemic localization study of isozyme SfTre1
-
Manually annotated by BRENDA team
additional information
C0LZJ6, C0LZJ7
NlTre-1 contains trehalase signature motifs
-
Manually annotated by BRENDA team
additional information
C0LZJ6, C0LZJ7
NlTre-2 contains trehalase signature motifs
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48500
-
enzyme form amniotic fluid, protein part of the enzyme, radiation inactivation
136143
49000
-
enzyme form kidney and intestine, protein part of the enzyme, radiation inactivation
136143
59000
A1XBT9
SDS-PAGE
679712
59270
A1XBT9
calculated from amino acid sequence
679712
60000
-
extracellular trehalase, SDS-PAGE
682056
62000 - 69000
-
gel filtration
655006
65000
-
gel filtration
136159
66300 - 72000
-
depending on the amount of sugar bound to the enzyme, enzyme from amniotic fluid, calculation from hydrodynamic parameters
136143
67000
-
gel filtration, PAGE
715128
69000
-
wild type enzyme, SDS-PAGE
678800
69180
-
calculated from amino acid sequence
678800
71000
-
SDS-PAGE
679765
73000
-
soluble trehalase P I, SDS-PAGE
681232
74000
-
gel filtration
136178
76000
-
nondenaturing-PAGE
655271
76000
-
recombinant enzyme, SDS-PAGE
678800
77000
A1XBT9
gel filtration
679712
80000
-
SDS-PAGE
679865
81000
O42783
gel filtration
701068
85000
-
enzyme from kidney and intestine, gel filtration
136148
91000
-
enzyme from amniotic fluid, gel filtration
136143
96000
-
gel filtration
136160
100000
-
disc gel electrophoresis
136151
105000
-
gel filtration
136151
105000
-
gel filtration
664996
114300
Q307Q4
calculated from amino acid sequence
680542
120000
-
gel filtration, stem enzyme
663561
120000
-
intracellular trehalase, SDS-PAGE
682056
122000
-
non-denaturing PAGE
136156
130000
Q307Q4
SDS-PAGE, deglycosylated enzyme
680542
140000
-
soluble trehalase P II, SDS-PAGE
681232
145000
-
gel filtration
136149
158000
-
gel filtration
656848
160000
-
gel filtration
136144
165000
-
gel filtration
656876
170000
-
enzyme from kidney and intestine, gel filtration in presence of 1% Triton
136143
170000
-
C-trehalase, gel filtration
136150
170000
-
gel filtration
136155
170000
Q307Q4
SDS-PAGE
680542
170000
Q307Q4
SDS-PAGE, recombinant enzyme
682673
175000
-
gel filtration
136147
175000
-
gel filtration
729103
200000
-
gel filtration
136177
210000
-
enzyme from activated spores and from dormant spores, gel filtration
136161
210000
-
gel filtration
136175
215000
-
V-trehalase, gel filtration
136150
218000
-
gel filtration
136141
223000
-
gel filtration
731011
240000
-
gel filtration
136157
250000
-
gel filtration
136170
370000
-
extracellular enzyme, gel filtration
136164
398000
-
intracellular enzyme, gel filtration
136164
400000
Lobosphaera sp.
-
gel filtration
136179
437000
-
gel filtration
136149
480000
-
gel filtration
136180
580000
-
gel filtration
136176
additional information
-
-
136145
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 80000, SDS-PAGE
?
P32359
x * 58000, SDS-PAGE
?
-
x * 67000, SDS-PAGE
?
A7XZC0
x * 74000, SDS-PAGE
?
P32358, Q3MV18
x * 74000, SDS-PAGE
?
-
x * 61000, SDS-PAGE
?
-
x * 135000, SDS-PAGE
?
-
x * 36000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 88000, SDS-PAGE
?
-
x * 41000, endoglycosidase H digestion before SDS-PAGE
?
-
x * 85000, deglycosylated species, SDS-PAGE
?
P32358, Q3MV18
x * 68000, SDS-PAGE
?
-
x * 42000 + x * 45000, SDS-PAGE
?
-
x * 58000, recombinant enzyme
?
-
x * 30000, about, recombinant GFP-tagged Ath1 N-terminal domain
?
B6ZIV1
x * 52000, recombinant His-tagged active enzyme, SDS-PAGE
?
-
x * 66480, SeTre-1, sequence calculation
?
B5ATV4, Q0ZIF5
x * 67000, isozyme SfTre1, SDS-PAGE
?
-
x * 68000, recombinant enzyme with His-tag
?
A1YQE2
x * 84400, calculated, x * 84000, SDS-PAGE
?
D2KHI9, D2KHJ0
x * 67070, isoform Treh1, calculated from amino acid sequence
?
D2KHI9, D2KHJ0
x * 73620, isoform Treh2, calculated from amino acid sequence
?
Nostoc punctiforme IAM M-15
-
x * 52000, recombinant His-tagged active enzyme, SDS-PAGE
-
?
Escherichia coli Mph2
-
x * 58000, recombinant enzyme
-
?
Escherichia coli K12 DH5alpha
-
x * 61000, SDS-PAGE
-
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 * 98000, SDS-PAGE
dimer
Lobosphaera sp.
-
2 * 180000-220000, SDS-PAGE
dimer
-
2 * 79000-91000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE, 2 * 51500, deglycosylated enzyme, SDS-PAGE
homohexamer
-
6 * 38000, SDS-PAGE
homotrimer
-
3 * 57000, SDS-PAGE
monomer
A1XBT9
1 * 59000, SDS-PAGE
monomer
-
1 * 90000, SDS-PAGE
monomer
-
1 * 95000, SDS-PAGE
monomer
-
1 * 67000, SDS-PAGE
monomer
-
1 * 64000, cytoplasmic enzyme, SDS-PAGE
monomer
-
1 * 75000, enzyme from kidney and intestine, SDS-PAGE
monomer
-
1 * 77000, SDS-PAGE
monomer
-
1 * 69000
multimer
-
20 or more subunits, gel filtration
multimer
Mycobacterium smegmatis b11
-
20 or more subunits, gel filtration
-
pentamer
-
5 * 82000, extracellular enzyme, SDS-PAGE, 5 * 85000, intracellular enzyme, SDS-PAGE
tetramer
-
4 * 92000, SDS-PAGE
monomer
O42783
1 * 84000, SDS-PAGE and calculated
additional information
-
polypeptide bands of 84000 Da, 98000 Da and 105000 Da are detected on 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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
contains 3.1% carbohydrate
side-chain modification
-
enzyme contains some type of bound lipid
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
-
Atc1p contains 20 potential N-glycosylation sites
glycoprotein
-
acid trehalase
no glycoprotein
-
no carbohydrate detected
glycoprotein
-
-
glycoprotein
-
contains 56% carbohydrate
glycoprotein
-
acid trehalase
glycoprotein
-
-
glycoprotein
Lobosphaera sp.
-
-
glycoprotein
Q307Q4
23.5% carbohydrate content
glycoprotein
-
contains 43% carbohydrate
phosphoprotein
O42783
enzyme is phosphorylated by cAMP-dependent protein kinase, but not significantly activated
glycoprotein
-
-
glycoprotein
-
2 nonglycoprotein enzyme forms: A1 and B1, and 2 glycoprotein enzyme forms: A2 and B2
glycoprotein
-
carbohydrate content is 72%
glycoprotein
-
highly glycosylated
glycoprotein
-
86% carbohydrate
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
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
glycoprotein
Schizosaccharomyces pombe 968
-
-
-
glycoprotein
-
extracellular enzyme contains 81% carbohydrate, intracellular enzyme contains 51% carbohydrate
glycoprotein
-
acid trehalase
glycoprotein
Scytalidium thermophilum 77.7.8
-
acid trehalase
-
glycoprotein
B5ATV4, Q0ZIF5
membrane-bound trehalase.SfTre2 contains potential N-glycosylation sites
glycoprotein
B5ATV4, Q0ZIF5
soluble trehalase.SfTre1 contains potential N-glycosylation sites
glycoprotein
-
contains 2 mol of glucosamine per mol of trehalase
glycoprotein
-
20% carbohydrate content
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 8
Q307Q4
after incubation at pH values of 3.5-8.0 and 30C for 1 h, all residual activities of reATM1 are over 80%
682673
3.5
-
15 min, around 40% loss of activity
136165
4 - 10
-
30C, stable in the range
656848
4 - 9
Lobosphaera sp.
-
5C, 15 h, stable
136179
4.5 - 12
-
4C, 24 h, stable
655006
4.5 - 7
-
37C, 2 h, stable
136148
5 - 10.5
-
recombinant enzyme
678800
5
-
more stable at pH 5.0 than at pH 4.0
136170
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
7
-
15 min, around 40% loss of activity
136165
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
136161
40
-
15 min, stable up to
655006
40
-
stable up to
656848
40
-
30 min, stable up to
666654
40
-
recombinant enzyme, stable under incubation at 40C or lower for 15 min
678800
40
O42783
half-life 2.5 min
701068
45 - 50
-
5 min, stable
136151
45 - 50
-
loss of 40% activity, purified acid trehalase
666654
45
-
muscle acid trehalase, inactivation
665118
50
-
stable up to
136148
50
-
stable for at least 6 h
136149
50
-
half-life is 34 h
136154
50
-
rapid inactivation above
136171
50
-
30 min, stable up to
136177
50
-
15 min, about 35% of maximal activity
655006
50
-
15 min, stable
655271
50
-
1 h, stable, purified enzyme
664996
50
-
the enzyme remains practically unaffected by 10 min treatment at 50C
681784
50
Q307Q4
the enzyme is stable below 50C, but it loses activity rapidly above 50C
682673
55
-
1 h, stable
136143
55
-
5 min, 19% loss of activity
136151
55
-
activity is drastically reduced above
136170
55
-
15 min, about 25% of maximal activity
655006
55
-
intestinal acid trehalase, inactivation
665118
55
Q307Q4
activity decreases rapidly at 55C or above
680542
60
-
t1/2: 30 min, in presence of 1% v/v Triton t1/2 is 12 min
136143
60
-
5 min, 72% loss of activity
136151
60
-
half-life: 1.8 min
136154
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+
136164
60
-
15 min, complete inactivation
655006
60
-
15 min, 50% loss of activity
655271
60
-
half-life of purified enzyme is 1.3 min
664996
60
-
nearly complete inactivation of purified acid trehalase
666654
62
B5ATV4, Q0ZIF5
solubilized membrane-bound isozyme SfTre2, half-life is 10 min; soluble isozyme SfTre1, completely stable
708733
65
-
intracellular enzyme has a half-life of 4.5 min when incubated without Ca2+
136164
65
Lobosphaera sp.
-
10 min, pH 5.5, stable below
136179
65
-
15 min, almost complete inactivation
655271
65
-
reproductive system alkaline trehalase is stable for at least 15 min
665118
70 - 90
A1XBT9
the enzyme exhibits approximately a half-life of 6 h at 70C, and of 2.5 h at 80C, incubation of 10 min at 87C results in 70% loss of the enzyme activity, and after 10 min at 90C no residual activity is detected
679712
70
-
3 min, 90% loss of activity
136148
70
-
half-life: 0.35 min
136154
70
-
no activity after 15 min at 70C
729103
80
A1XBT9
the recombinant trehalase with a histidine tag at the N-terminus loses 50% of the activity after 10 min incubation at 80C in 50 mM Bis/Tris/propane-HCl buffer (pH 6.5)
679712
additional information
-
bovine serum albumin and casein protects from heat-inactivation
136155
additional information
-
addition of Ca2+ decreases stability, half-life at 65C is diminished about 2fold
136177
additional information
-
the acid trehalase is more thermostable than the neutral trehalase
664188
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
8 M urea, 30C, 10 min, 25% loss of activity
-
stable for at least 4 successive freeze-thaw cycles
-
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 4C for periods of more than 3 min at 4C
-
trehalase is stabilized by aggregation with sucrase
-
Ca2+ and Mn2+ protect from thermoinactivation
-
Mn2+ stabilizes the enzyme during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-12C, stable for at least 2 months
-
4-10C, stable for at least 2-4 days
-
immobilized crude recombinant enzyme on chitin shows no significant loss of activity being reused 10times and stored at 10C, in 50 mM sodium maleate, pH 6.0, for 55 days
-
0C, 0.05 M maleate buffer, pH 6.5, stable for 1 month
-
-60C, intestinal, renal and amniotic fluid enzyme retain full activity for at least 6 months
-
-80C, 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
-
-15C, loses ca. 18% of activity after 3 months
-
0-4C, pH 4.5, 50% loss of activity after 1 month
-
4C, 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
-
4C, pH 7.5, 20% glycerol, 20% loss of activity of trehalase-a after 5 months
-
4C, stable for 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose Fast Flow column chromatography and Sephacryl S-100 gel filtration
-
extracellular and intracellular enzyme
-
recombinant protein
-
Sephacryl S-300 gel filtration, DEAE-cellulofine column chromatography, and Con A-Sepharose column chromatography
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, CM Sepharose column chromatography, and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, Biosuite DEAE column chromatography, and gel filtration
-
from an overexpressing strain, cytoplasmic enzyme
-
preparation of periplasmic fraction of recombinant Escherichia coli
-
with PEG 3350 (25% w/v) and bis(2-hydroxyethyl)aminotris(hydroxymethyl)methane (Bis-Tris)/HCl buffer (0.1 m, pH 6.5)
-
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
-
Lobosphaera sp.
-
stem enzyme 800fold by ion exchange chromatography, gel filtration, and other steps
-
High Q Sepharose column chromatography, 25Q Sepharose column chromatography, and Sephacryl-200s HR gel filtration
Q307Q4
Ni-NTA affinity column chromatography
Q307Q4
ammonium sulfate fractionation, phenyl-Sepharose DE-52 column chromatography and Sephacryl S-300 gel filtration
-
recombinant His-tagged enzyme by His affinity chromatography to homogeneity
B6ZIV1
4 enzyme form
-
acid trehalase 425fold from root nodules, by ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and native PAGE
-
native enzyme to homogeneity
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Q Sepharose column chromatography
A1XBT9
acid trehalase-sucrase aggregate
-
ammonium sulfate precipitation, DEAE-Sephadex-A50 column chromatography, and HPLC gel filtration on Protein Pak 300 SW
-
cryptic enzyme form; partial
-
IgG Sepharose column chromatography
-
2896fold from midgut of larvae, by ammonium sulfate precipitation, 2 steps of hydrophobic interaction and ion exchange chromatography
-
recombinant enzyme
Q0ZIF5
Econo-Pac methyl hydrophobic interaction column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
P32359
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris strain GS115
-
expression in yeast
-
expressed in yeast
-
expression in Escherichia coli
A1YQE2
isozyme type 2
-
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
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Gluconobacter oxydans
-
overexpression of the enzyme in strain Mph2 from plasmid pTRE11
-
expression in Saccharomyces cerevisiae lacking the activites of endogenous trehalases Nth1, Nth2, or Ath1
-
expressed in Pichia pastoris strain KM71
Q307Q4
expressed in Escherichia coli strain BL21
-
expression in Escherichia coli
O42783
DNA and amino acid sequence determination, analysis, and comparisons; DNA and amino acid sequence determination, analysis, and comparisons
C0LZJ6, C0LZJ7
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
B6ZIV1
expressed in Escherichia coli DH5alpha cells
A1XBT9
cloning of acid treahalase
-
expressed in Escherichia coli strain BL21
-
expression of GFP-tagged Ath1 N-terminal domain
-
genes NTH1 and ATH1
-
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
-
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)
B5ATV4, Q0ZIF5
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
no induction by 20-hydroxyecdysone of the membrane-bound trehalase isozyme encoded by gene NlTre2
C0LZJ6, C0LZJ7
20-hydroxyecdysone induces the soluble trehalase isozyme encoded by gene NlTre1
C0LZJ6, C0LZJ7
the enzyme expression is highest at day 7 after blood meal
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D108K
-
mutant enzyme fails to bind Ca2+ or to undergo enzyme activation
D322A
Q0ZIF5
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
Q0ZIF5
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
Q0ZIF5
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
Q0ZIF5
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
Q0ZIF5
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
Q0ZIF5
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
additional information
-
construction of enzyme-deficient mutants by gene disruption at two ATC chromosomal alleles
additional information
-
enzymatic activity of TreA/TreF hybrids
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
Saccharomyces cerevisiae MCY1264
-
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
-
D97L
-
mutant enzyme fails to bind Ca2+ or to undergo enzyme activation
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 10C, in 50 mM sodium maleate, pH 6.0, for 55 days
biotechnology
Escherichia coli Mph2
-
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 10C, in 50 mM sodium maleate, pH 6.0, for 55 days
-
analysis
-
highly specific tool for the assay of trehalose
medicine
-
urinary trehalase is a specific marker of renal tubular damage
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