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Information on EC 3.2.1.28 - alpha,alpha-trehalase and Organism(s) Escherichia coli and UniProt Accession P13482

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IUBMB Comments
The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the alpha-glucosidic O-linkage of alpha,alpha-trehalose, releasing initially equimolar amounts of alpha- and beta-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
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Escherichia coli
UNIPROT: P13482
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
trehalase, neutral trehalase, acid trehalase, soluble trehalase, tre-2, nth1p, alpha,alpha-trehalase, setre-2, atc1p, ntp1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GH37 trehalase
-
alpha,alpha'-trehalose 1-D-glucohydrolase
-
-
-
-
Alpha,alpha-trehalase
-
-
-
-
Alpha,alpha-trehalose glucohydrolase
-
-
-
-
trehalase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-52-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
trehalose + H2O
D-glucose
show the reaction diagram
-
-
-
?
alpha,alpha-trehalose + H2O
alpha-D-glucopyranose + D-glucose
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
cytoplasmic enzyme has no metal dependency
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-thiatrehazolin
-
validoxylamine A
-
(1R,2R,3R,6S,7S,7aS)-3-(hydroxymethyl)-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy]hexahydro-1H-pyrrolizine-1,2,7-triol
-
casuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(2R,3R,4S,5R,6R)-2-[[(1R,2R,5R,6R,7R,7aR)-6,7-dihydroxy-1,5-bis(hydroxymethyl)hexahydro-1H-pyrrolizin-2-yl]oxy]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
-
7-homocasuarine-6-O-alpha-D-glucoside, active against trehalases derived from insects, bacteria and eukaryotes
(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
K+
-
0.5 M KCl, activity is 2fold lower
Na+
-
0.5 M NaCl, activity is 2fold lower
potassium glutamate
-
0.5 M KCl, activity is 2fold lower
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
trehalose
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
0.16 - 1.5
alpha,alpha-trehalose
1.9
trehalose
-
cytoplasmic enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
199
trehalose
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000009
1-thiatrehazolin
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
0.00001
validoxylamine A
at 37°C in sodium maleate buffer (75 mM, pH 5.5)
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
0.0028
(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
0.000086
(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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
6.2
-
enzyme in periplasmic fraction, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
immobilized enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
immobilized enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
malfunction
-
loss of treA significantly reduces its cell invasion capacity and colonization of the bladder in a murine model of urinary tract infection
physiological function
-
treA gene is needed for optimal production of type 1 fimbriae in ExPEC strain MT78
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
-
x * 58000, recombinant enzyme
61000
-
x * 61000, SDS-PAGE
64000
-
1 * 64000, cytoplasmic enzyme, SDS-PAGE
74000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 64000, cytoplasmic enzyme, SDS-PAGE
additional information
-
TrA can fold into the active conformation in its nonnative cellular compartment, the cytoplasm, after removal of its signal sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzymatic activity of TreA/TreF hybrids
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized crude recombinant enzyme on chitin shows no significant loss of activity being reused 10times and stored at 10°C, in 50 mM sodium maleate, pH 6.0, for 55 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
with PEG 3350 (25% w/v) and bis(2-hydroxyethyl)aminotris(hydroxymethyl)methane (Bis-Tris)/HCl buffer (0.1 m, pH 6.5)
from an overexpressing strain, cytoplasmic enzyme
-
preparation of periplasmic fraction of recombinant Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expressed in Gluconobacter oxydans
-
overexpression of the enzyme in strain Mph2 from plasmid pTRE11
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
a trehalase-based biosensor platform offers a versatile and convenient method for point-of-care applications as it does not require sample preparation or handling and can be integrated with existing glucometers or sensors
biotechnology
-
immobilization of the crude enzyme on chitin resulting in stable, specific, and reusable reactors for application in other biotechnological processes, the immobilized enzyme shows no significant loss of activity being reused 10times and stored at 10°C, in 50 mM sodium maleate, pH 6.0, for 55 days
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Repoila, F.; Gutierrez, C.
Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter
Mol. Microbiol.
5
747-755
1991
Escherichia coli
Manually annotated by BRENDA team
Horlacher, R.; Uhland, K.; Klein, W.; Ehrmann, M.; Boos, W.
Characterization of a cytoplasmic trehalase of Escherichia coli
J. Bacteriol.
178
6250-6257
1996
Escherichia coli
Manually annotated by BRENDA team
Uhland, K.; Mondigler, M.; Spiess, C.; Prinz, W.; Ehrmann, M.
Determinants of translocation and folding of TreF, a trehalase of Escherichia coli
J. Biol. Chem.
275
23439-23445
2000
Escherichia coli
Manually annotated by BRENDA team
Martins, A.S.; Peixoto, D.; Paiva, L.M.C.; Panek, A.D.; Paiva, C.L.A.
A simple method for obtaining reusable reactors containing immobilized trehalase: characterization of a crude trehalase preparation immobilized on chitin particles
Enzyme Microb. Technol.
38
486-492
2006
Escherichia coli, Escherichia coli Mph2
-
Manually annotated by BRENDA team
Gibson, R.P.; Gloster, T.M.; Roberts, S.; Warren, R.A.; Storch de Gracia, I.; Garcia, A.; Chiara, J.L.; Davies, G.J.
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors
Angew. Chem.
46
4115-4119
2007
Escherichia coli (P13482)
Manually annotated by BRENDA team
Cardona, F.; Goti, A.; Parmeggiani, C.; Parenti, P.; Forcella, M.; Fusi, P.; Cipolla, L.; Roberts, S.M.; Davies, G.J.; Gloster, T.M.
Casuarine-6-O-alpha-D-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases
Chem. Commun. (Camb. )
46
2629-2631
2010
Escherichia coli, Sus scrofa, Chironomus riparius
Manually annotated by BRENDA team
Kosciow, K.; Zahid, N.; Schweiger, P.; Deppenmeier, U.
Production of a periplasmic trehalase in Gluconobacter oxydans and growth on trehalose
J. Biotechnol.
189C
27-35
2014
Escherichia coli, Escherichia coli K12 DH5alpha
Manually annotated by BRENDA team
Barraza, A.; Sanchez, F.
Trehalases: a neglected carbon metabolism regulator?
Plant Signal. Behav.
8
e24778
2013
Apis mellifera (A8J4S9), Arabidopsis thaliana (Q9SU50), Aspergillus nidulans (O42777), Caenorhabditis elegans (Q9GYK9), Candida albicans (P52494), Drosophila melanogaster (Q9W2M2), Enterobacter sp. (A4WBE4), Enterobacter sp. 638 (A4WBE4), Erwinia amylovora (D4I261), Escherichia coli (P13482), Glycine max (Q9XEY7), Homo sapiens (O43280), Laccaria bicolor (B0CV22), Laccaria bicolor (B0DA99), Medicago truncatula (Q9XGH9), Metarhizium acridum (Q6Q5X7), Metarhizium anisopliae (A9XE63), Mus musculus (Q9JLT2), Neurospora crassa (O42783), Neurospora crassa DSM 1257 (O42783), Neurospora tetrasperma (F8MBS5), Nicotiana tabacum (D2KWM9), Physcomitrium patens (A6MIZ4), Ralstonia solanacearum, Rattus norvegicus (O70282), Saccharomyces cerevisiae (P48016), Spodoptera exigua (B0M0J3), Spodoptera frugiperda (B5ATV4), Xanthomonas campestris (Q3BXX2)
Manually annotated by BRENDA team
Drikic, M.; De Buck, J.
Split trehalase as a versatile reporter for a wide range of biological analytes
Biotechnol. Bioeng.
115
1128-1136
2018
Escherichia coli (P13482), Escherichia coli
Manually annotated by BRENDA team
Pavanelo, D.B.; Houle, S.; Matter, L.B.; Dozois, C.M.; Horn, F.
The periplasmic trehalase affects type 1 fimbria production and virulence of extraintestinal pathogenic Escherichia coli strain MT78
Infect. Immun.
86
e00241-18
2018
Escherichia coli, Escherichia coli MT78
Manually annotated by BRENDA team