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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
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 ACCESSION NO.
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
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
-
-
Atc1p
-
isoform
Atc1p
Candida albicans CAI4
-
-
-
ATM1
Q307Q4
mature enzyme
GH37 trehalase
-
-
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
trehalase
-
-
-
-
trehalase
-
-
trehalase
-
-
trehalase
-
-
trehalase
Escherichia coli Mph2
-
-
-
trehalase
-
-
trehalase
-
-
trehalase
-
-
trehalase
-
-
trehalase
Mycobacterium smegmatis b11
-
-
-
trehalase
C0LZJ6, C0LZJ7
-
trehalase
B6ZIV1
-
trehalase
Nostoc punctiforme IAM M-15
B6ZIV1
-
-
trehalase
A1XBT9
-
trehalase
Scytalidium thermophilum 77.7.8
-
-
-
trehalase
-
-
trehalase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-52-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
strain Mph2
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
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
-
different functions of the insect soluble and membrane-bound trehalase genes in chitin biosynthesis, overview
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
C0LZJ6, C0LZJ7, -
the enzyme trehalase is involved in energy metabolism and controlling trehalose, the main blood sugar of insects, levels in cells; the enzyme trehalase is involved in energy metabolism and controlling trehalose, the main blood sugar of insects, levels in cells
physiological function
-
role for Nth2p in the mobilization of intracellular trehalose during salt-stress recovery, overview
physiological function
P32358, Q3MV18
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; 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
Saccharomyces cerevisiae MCY1264
-
role for Nth2p in the mobilization of intracellular trehalose during salt-stress recovery, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
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
?
-
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 ACCESSION NO.
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
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
?
-
Nostoc punctiforme IAM M-15
B6ZIV1
mechanism of trehalose accumulation in response to desiccation and salt stress, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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
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
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%
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
phloretin
-
activates the neutral trehalase in presence of 5 mM trehalose
Zn2+
-
2.5-5.0 mM ZnCl2, slight stimulation
Mn2+
-
weak stimulation
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 ACCESSION NO.
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-thiatrehazolin
P13482
-
acetate
-
strong inhibition by acetic acid/acetate buffer, V-trehalase
ADP
-
Ca2+ abolishes inhibitory effect
ADP
-
1 mM, 53% inhibition
Al3+
-
1 mM AlCl3, complete inhibition
Al3+
-
1 mM, complete inhibition
AMP
-
Ca2+ abolishes inhibitory effect
AMP
-
50% inhibition at 20 mM
amygdalin
-
competitive inhibition
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
Ba+
-
1 mM, complete inhibition
-
Ca2+
-
1.0 mM CaCl2, 9% loss of activity
CaCl2
B6ZIV1, -
over 90% inhibition at 10 mM
castanospermine
-
potent, reversible, competitive
castanospermine
-
50% inhibition at 0.5 mg/ml
castanospermine
-
-
casuarine
-
-
-
cellobiose
-
10 mM, 60% inhibition
Co2+
A1XBT9, -
71% inhibition at 5 mM
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
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
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
EGTA
A1YQE2, -
20 mM, 55% residual activity
Fe3+
Lobosphaera sp.
-
-
-
Fe3+
-
inhibits the acid trehalase by 50%
-
FeCl3
-
10 mM, 35% inhibition
Gentiobiose
-
slight inhibition of acid trehalase
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
Mandelonitrile
-
competitive inhibition
mannitol
-
partial
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-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
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
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
phlorizin
-
2.4 mM
phlorizin
-
2 mM, 20% inhibition
phlorizin
-
hyperbolic uncompetitive, binds only to enzyme-substrate complex
phosphate
-
Ca2+ abolishes inhibitory effect
potassium glutamate
-
0.5 M KCl, activity is 2fold lower
prunasin
-
competitive inhibition
Salicin
-
competitive inhibition
SDS
-
1.0%, 80% inhibition
sodium orthovanadate
-
80% inhibition at 10 mM
Sucrose
-
competitive
Sucrose
-
competitive
Sucrose
-
10 mM, 60% inhibition
Sucrose
Lobosphaera sp.
-
25 mM, 33% inhibition; competitive
Sucrose
-
competitive
trehazolin
-, Q307Q4
-
trehazolin
Q307Q4
specific inhibitor
Tris
-
3.8 mM, competitive
Tris
-
100 mM, 28% inhibition
Tris
-
100 mM, 92% inhibition
Tris
-
10 mM, complete inhibition
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 B
-
-
Validoxylamine A
-
potent, time-dependent
Validoxylamine A
P13482
-
Validoxylamine A
-
-
Validoxylamine A
-
complete inhibition
validoxylamine B
-
-
Zn2+
A1XBT9, -
95% inhibition at 5 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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
esculin
-
induces the enzyme in different organs, e.g. Malphigian tubules, midgut, fat body, hemolymph, and body wall, when feeded to larvae
MgATP2-
-
C-trehalase can be activated by MgATP2- in presence of cAMP
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
0.44
-
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
-
1.5
-
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
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)
0.41
-
trehalose
P13482
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
0.52
-
trehalose
-
-
0.52
-
trehalose
A8J4S9, -
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
1.4
-
trehalose
-
V-trehalase
1.56
-
trehalose
-
soluble trehalase P I, in acetate buffer, pH 5.5, at 30C
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
-
-
4.79
-
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
P13482
at 37C in sodium maleate buffer (75 mM, pH 5.5)
662
-
trehalose
A8J4S9, -
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]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.008
-
alpha,alpha-trehalose
Q0ZIF5, -
mutant R222A/R287A, pH 7.0, 30C
6709
0.009
-
alpha,alpha-trehalose
Q0ZIF5, -
mutant R222A, pH 7.0, 30C
6709
0.027
-
alpha,alpha-trehalose
Q0ZIF5, -
mutant E520A, pH 7.0, 30C
6709
0.045
-
alpha,alpha-trehalose
Q0ZIF5, -
mutant R287A, pH 7.0, 30C
6709
0.18
-
alpha,alpha-trehalose
Q0ZIF5, -
mutant D322A, pH 7.0, 30C
6709
0.27
-
alpha,alpha-trehalose
Q0ZIF5, -
mutant R169A, pH 7.0, 30C
6709
2400
-
alpha,alpha-trehalose
Q0ZIF5, -
wild-type, pH 7.0, 30C
6709
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
P13482
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
0.00486
-
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
1.14
-
Mandelonitrile
-
pH 6.0, 30C
89
-
methyl-alpha-glucoside
-
pH 6.0, 30C
0.09
-
phlorizin
-
pH 6.0, 30C
0.92
-
prunasin
-
pH 6.0, 30C
19
-
Salicin
-
pH 6.0, 30C
15
-
Sucrose
-
-
0.55
-
Tris
-
pH 6.0, 30C
0.000045
-
validamycin
-
-
0.4
-
validamycin A
-
pH 3.3, 37C, versus trehalose
0.27
-
validamycin B
-
pH 3.3, 37C, versus trehalose
0.00001
-
Validoxylamine A
P13482
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
6.2
-
methyl-alpha-mannoside
-
pH 6.0, 30C
additional information
-
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
0.0012
-
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
0.227
-
-
cell extract, at 37C
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
12.2
-
C0LZJ6, C0LZJ7, -
membrane-bound isozyme
36.99
-
-
after 162fold purification, at 37C
39.4
-
C0LZJ6, C0LZJ7, -
soluble isozyme
50
-
-
free enzyme
53.4
-
-
solubilized enzyme
73.9
-
-
-
80
150
O42783
pH 7.0, 30C
101.3
-
Q307Q4
recombinant enzyme, after purification, at 30C
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
-
-
-
312
-
-
kidney
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
4.9
-
-
-
5
-
-
muscle acid trehalase
5.5
-
-
-
5.5
-
Lobosphaera sp.
-
-
5.5
-
-
immobilized enzyme
5.5
-
-, Q307Q4
-
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
-
-
a minor activity maximum at pH 3.5 and a major activity maximum at pH 6.5
6.5
-
A1XBT9, -
-
6.5
-
-
soluble trehalase P I
6.7
-
-
at 40 mM trehalose, C-trehalase
6.7
-
-
assay at
7
-
O42783
-
7
-
A1YQE2, -
-
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
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
4.8
8.5
-
pH 4.9: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
A8J4S9, -
recombinant enzyme
30
-
-
assay at
30
-
-
assay at
30
-
-, Q307Q4
-
30
-
Q307Q4
recombinant enzyme
30
-
O42783
-
35
-
-
assay at
37
-
-
assay at
37
-
B6ZIV1, -
assay at
37
-
C0LZJ6, C0LZJ7, -
assay at; assay at
37
-
-
-
40
45
-
soluble trehalase P I
40
-
-
-
45
-
-
muscle acid trehalase
50
-
-
immobilized enzyme
50
-
-
above 50C, soluble trehalase P I
55
-
-
intestinal acid trehalase and reproductive system alkaline trehalase
55
-
A1YQE2, -
-
60
-
-
extracellular enzyme
60
-
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
65
-
-
intracellular enzyme
65
-
Lobosphaera sp.
-
-
88
-
A1XBT9, -
-
additional information
-
-
the acid trehalase shows a higher temperature optimum than the neutral trehalase
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
6
-
A7XZC0, -
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
-
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; 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
-
microvillus membrane
Manually annotated by BRENDA team
-
mucosa of small intestine; small intestine
Manually annotated by BRENDA team
-
acid trehalase
Manually annotated by BRENDA team
-
brush-border membrane of cortex
Manually annotated by BRENDA team
-
brush border membrane
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
-
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
P32358, Q3MV18
;
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 membrane-bound trehalase, isozyme SfTre2, along Spodoptera frugiperda midgut cells, overview; columnar cells, distribution of soluble trehalase, isozyme SfTre1, along Spodoptera frugiperda midgut cells, overview
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
-
distribution in the soluble and membrane fractions of the tissues, overview
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
-
expression pattern in presence or absence of D-glucose
Manually annotated by BRENDA team
additional information
C0LZJ6, C0LZJ7, -
activity and gene mRNA level at different developmental stages, expression pattern, overview; 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
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
Lobosphaera sp.
-
-
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
-
the acid trehalase contains either a transmembrane segment or a signal sequence at the N-terminus
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
B5ATV4, Q0ZIF5
bound, isozyme SfTre2
Manually annotated by BRENDA team
C0LZJ6, C0LZJ7, -
NlTre2, contains a putative transmembrane domain
Manually annotated by BRENDA team
-
membrane-bound isozyme SeTre-2
Manually annotated by BRENDA team
P32358, Q3MV18
-
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 K12, Escherichia coli Mph2
-
-
-
-
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
P32358, Q3MV18
-
-
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; 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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48500
-
-
enzyme form amniotic fluid, protein part of the enzyme, radiation inactivation
49000
-
-
enzyme form kidney and intestine, protein part of the enzyme, radiation inactivation
59000
-
A1XBT9, -
SDS-PAGE
59270
-
A1XBT9, -
calculated from amino acid sequence
60000
-
-
extracellular trehalase, SDS-PAGE
62000
69000
-
gel filtration
65000
-
-
gel filtration
66300
72000
-
depending on the amount of sugar bound to the enzyme, enzyme from amniotic fluid, calculation from hydrodynamic parameters
67000
-
-
gel filtration, PAGE
69000
-
A8J4S9, -
wild type enzyme, SDS-PAGE
69180
-
A8J4S9, -
calculated from amino acid sequence
71000
-
-
SDS-PAGE
73000
-
-
soluble trehalase P I, SDS-PAGE
74000
-
-
gel filtration
76000
-
-
nondenaturing-PAGE
76000
-
A8J4S9, -
recombinant enzyme, SDS-PAGE
77000
-
A1XBT9, -
gel filtration
80000
-
-
SDS-PAGE
81000
-
O42783
gel filtration
85000
-
-
enzyme from kidney and intestine, gel filtration
91000
-
-
enzyme from amniotic fluid, gel filtration
96000
-
-
gel filtration
100000
-
-
disc gel electrophoresis
105000
-
-
gel filtration
114300
-
-, Q307Q4
calculated from amino acid sequence
120000
-
-
gel filtration, stem enzyme
120000
-
-
intracellular trehalase, SDS-PAGE
122000
-
-
non-denaturing PAGE
130000
-
-, Q307Q4
SDS-PAGE, deglycosylated enzyme
140000
-
-
soluble trehalase P II, SDS-PAGE
145000
-
-
gel filtration
158000
-
-
gel filtration
160000
-
-
gel filtration
165000
-
-
gel filtration
170000
-
-
enzyme from kidney and intestine, gel filtration in presence of 1% Triton
170000
-
-
C-trehalase, gel filtration
170000
-
-
gel filtration
170000
-
-, Q307Q4
SDS-PAGE
170000
-
Q307Q4
SDS-PAGE, recombinant enzyme
175000
-
-
gel filtration
200000
-
-
gel filtration
210000
-
-
enzyme from activated spores and from dormant spores, gel filtration
210000
-
-
gel filtration
215000
-
-
V-trehalase, gel filtration
218000
-
-
gel filtration
240000
-
-
gel filtration
250000
-
-
gel filtration
370000
-
-
extracellular enzyme, gel filtration
398000
-
-
intracellular enzyme, gel filtration
400000
-
Lobosphaera sp.
-
gel filtration
437000
-
-
gel filtration
480000
-
-
gel filtration
580000
-
-
gel filtration
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 41000, endoglycosidase H digestion before SDS-PAGE
?
-
x * 80000, SDS-PAGE
?
-
x * 88000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 36000, SDS-PAGE
?
-
x * 85000, deglycosylated species, SDS-PAGE
?
-
x * 135000, SDS-PAGE
?
-
x * 58000, recombinant enzyme
?
-
x * 67000, SDS-PAGE
?
-
x * 42000 + x * 45000, SDS-PAGE
?
A7XZC0, -
x * 74000, SDS-PAGE
?
B6ZIV1, -
x * 52000, recombinant His-tagged active enzyme, SDS-PAGE
?
-
x * 30000, about, recombinant GFP-tagged Ath1 N-terminal domain
?
B5ATV4, Q0ZIF5
x * 67000, isozyme SfTre1, SDS-PAGE
?
-
x * 66480, SeTre-1, sequence calculation
?
-
x * 68000, recombinant enzyme with His-tag
?
P32358, Q3MV18
x * 68000, SDS-PAGE; x * 74000, SDS-PAGE
?
A1YQE2, -
x * 84400, calculated, x * 84000, SDS-PAGE
?
Escherichia coli Mph2
-
x * 58000, recombinant enzyme
-
?
Nostoc punctiforme IAM M-15
-
x * 52000, recombinant His-tagged active enzyme, SDS-PAGE
-
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 98000, SDS-PAGE
dimer
Lobosphaera sp.
-
2 * 180000-220000, SDS-PAGE
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 * 79000-91000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE, 2 * 51500, deglycosylated enzyme, SDS-PAGE
monomer
-
1 * 75000, enzyme from kidney and intestine, SDS-PAGE
monomer
-
1 * 95000, SDS-PAGE
monomer
-
1 * 90000, SDS-PAGE
monomer
-
1 * 77000, SDS-PAGE
monomer
-
1 * 64000, cytoplasmic enzyme, SDS-PAGE
monomer
-
1 * 69000
monomer
A1XBT9, -
1 * 59000, SDS-PAGE
monomer
O42783
1 * 84000, SDS-PAGE and calculated
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
-
1 * 67000, 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
-
polypeptide bands of 84000 Da, 98000 Da and 105000 Da are detected on 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 ACCESSION NO.
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
-
2 nonglycoprotein enzyme forms: A1 and B1, and 2 glycoprotein enzyme forms: A2 and B2
glycoprotein
-
-
glycoprotein
-
carbohydrate content is 72%
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
glycoprotein
-
highly glycosylated
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; soluble trehalase.SfTre1 contains potential N-glycosylation sites
glycoprotein
-
contains 2 mol of glucosamine per mol of trehalase
glycoprotein
-
20% carbohydrate content
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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%
3.5
-
-
15 min, around 40% loss of activity
4
10
-
30C, stable in the range
4
9
Lobosphaera sp.
-
5C, 15 h, stable
4.5
12
-
4C, 24 h, stable
4.5
7
-
37C, 2 h, stable
5
10.5
A8J4S9, -
recombinant enzyme
5
-
-
more stable at pH 5.0 than at pH 4.0
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
7
-
-
15 min, around 40% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
36
-
-
90 min, 93.3% loss of activity of the enzyme from activated spores, 67% loss of activity of the enzyme from dormant spores
40
-
-
15 min, stable up to
40
-
-
stable up to
40
-
-
30 min, stable up to
40
-
A8J4S9, -
recombinant enzyme, stable under incubation at 40C or lower for 15 min
40
-
O42783
half-life 2.5 min
45
50
-
5 min, stable
45
50
-
loss of 40% activity, purified acid trehalase
45
-
-
muscle acid trehalase, inactivation
50
-
-
stable up to
50
-
-
stable for at least 6 h
50
-
-
half-life is 34 h
50
-
-
rapid inactivation above
50
-
-
30 min, stable up to
50
-
-
15 min, about 35% of maximal activity
50
-
-
15 min, stable
50
-
-
1 h, stable, purified enzyme
50
-
-
the enzyme remains practically unaffected by 10 min treatment at 50C
50
-
Q307Q4
the enzyme is stable below 50C, but it loses activity rapidly above 50C
55
-
-
1 h, stable
55
-
-
5 min, 19% loss of activity
55
-
-
activity is drastically reduced above
55
-
-
15 min, about 25% of maximal activity
55
-
-
intestinal acid trehalase, inactivation
55
-
-, Q307Q4
activity decreases rapidly at 55C or above
60
-
-
t1/2: 30 min, in presence of 1% v/v Triton t1/2 is 12 min
60
-
-
5 min, 72% loss of activity
60
-
-
half-life: 1.8 min
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+
60
-
-
15 min, complete inactivation
60
-
-
15 min, 50% loss of activity
60
-
-
half-life of purified enzyme is 1.3 min
60
-
-
nearly complete inactivation of purified acid trehalase
62
-
B5ATV4, Q0ZIF5
solubilized membrane-bound isozyme SfTre2, half-life is 10 min; soluble isozyme SfTre1, completely stable
65
-
-
intracellular enzyme has a half-life of 4.5 min when incubated without Ca2+
65
-
Lobosphaera sp.
-
10 min, pH 5.5, stable below
65
-
-
15 min, almost complete inactivation
65
-
-
reproductive system alkaline trehalase is stable for at least 15 min
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
70
-
-
3 min, 90% loss of activity
70
-
-
half-life: 0.35 min
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)
additional information
-
-
bovine serum albumin and casein protects from heat-inactivation
additional information
-
-
addition of Ca2+ decreases stability, half-life at 65C is diminished about 2fold
additional information
-
-
the acid trehalase is more thermostable than the neutral trehalase
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
-
4C, stable for 3 months
-
-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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE Sepharose Fast Flow column chromatography and Sephacryl S-100 gel filtration
A8J4S9, -
extracellular and intracellular enzyme
-
recombinant protein
-
Sephacryl S-300 gel filtration, DEAE-cellulofine column chromatography, and Con A-Sepharose column chromatography
-
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)
P13482
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, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Pichia pastoris strain GS115
A8J4S9, -
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
P13482
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 ACCESSION NO.
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; 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
P32358, Q3MV18
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, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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