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Information on EC 3.2.1.28 - alpha,alpha-trehalase and Organism(s) Metarhizium anisopliae and UniProt Accession Q6UDD9

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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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This record set is specific for:
Metarhizium anisopliae
UNIPROT: Q6UDD9
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The taxonomic range for the selected organisms is: Metarhizium anisopliae
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
alpha,alpha'-trehalose 1-D-glucohydrolase
-
-
-
-
Alpha,alpha-trehalase
-
-
-
-
Alpha,alpha-trehalose glucohydrolase
-
-
-
-
ATM1
mature enzyme
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
alpha-D-glucopyranose + D-glucose
show the reaction diagram
-
-
-
?
alpha,alpha-trehalose + H2O
2 D-glucose
show the reaction diagram
-
-
-
?
alpha,alpha-trehalose + H2O
beta-D-glucose + alpha-D-glucose
show the reaction diagram
i.e. alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranoside
-
-
?
trehalose + H2O
D-glucose
show the reaction diagram
additional information
?
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
trehazolin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.11 - 1.74
alpha,alpha-trehalose
2.3 - 2.6
trehalose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.02
alpha,alpha-trehalose
-
0.91 - 0.99
alpha,alpha-trehalose
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000013 - 0.000019
trehazolin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.224
culture filtrate, in 20 mM MES buffer, pH 5.5, at 30°C
101.3
recombinant enzyme, after purification, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
recombinant enzyme, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q6UDD9_METAN
711
0
82219
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
114300
calculated from amino acid sequence
130000
SDS-PAGE, deglycosylated enzyme
170000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
23.5% carbohydrate content
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8
after incubation at pH values of 3.5-8.0 and 30°C for 1 h, all residual activities of reATM1 are over 80%
682673
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
the enzyme is stable below 50°C, but it loses activity rapidly above 50°C
55
activity decreases rapidly at 55°C or above
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
High Q Sepharose column chromatography, 25Q Sepharose column chromatography, and Sephacryl-200s HR gel filtration
Ni-NTA affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris strain KM71
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Small, C.L.; Donaldson, N.; Bidochka, M.J.
Nucleotide sequence variation does not relate to differences in kinetic properties of neutral trehalase from the insect pathogenic fungus Metarhizium anisopliae
Curr. Microbiol.
48
428-434
2004
Metarhizium flavoviride, Metarhizium anisopliae (Q6UDD9), Metarhizium anisopliae (Q6UDE0), Metarhizium anisopliae (Q9HDE9), Metarhizium anisopliae, Metarhizium anisopliae SCB1-2i (Q6UDE0), Metarhizium anisopliae TIB2-1ii (Q9HDE9), Metarhizium flavoviride SCB1-2i, Metarhizium anisopliae SCB2-2i (Q6UDD9), Metarhizium anisopliae Ma2575 (Q9HDE9), Metarhizium anisopliae Ma473 (Q9HDE9)
Manually annotated by BRENDA team
Zhao, H.; Charnley, A.K.; Wang, Z.; Yin, Y.; Li, Z.; Li, Y.; Cao, Y.; Peng, G.; Xia, Y.
Identification of an extracellular acid trehalase and its gene involved in fungal pathogenesis of Metarhizium anisopliae
J. Biochem.
140
319-327
2006
Metarhizium anisopliae (A9XE63), Metarhizium anisopliae
Manually annotated by BRENDA team
Liu, Y.; Wang, Z.; Yin, Y.; Cao, Y.; Zhao, H.; Xia, Y.
Expression, purification, and characterization of recombinant Metarhizium anisopliae acid trehalase in Pichia pastoris
Protein Expr. Purif.
54
66-72
2007
Metarhizium anisopliae (A9XE63), Metarhizium anisopliae
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