Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.28 - alpha,alpha-trehalase and Organism(s) Neurospora crassa and UniProt Accession O42783

for references in articles please use BRENDA:EC3.2.1.28
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Neurospora crassa
UNIPROT: O42783
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Neurospora crassa
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
-
-
-
-
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
2 D-glucopyranose
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
absolutely required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42
alpha,alpha-trehalose
pH 7.0, 30°C
0.52
trehalose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 150
pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
trehalase function is central in carbon partitioning and energy homeostasis regulation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81000
gel filtration
84000
1 * 84000, SDS-PAGE and calculated
437000
-
gel filtration
92000
-
4 * 92000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 84000, SDS-PAGE and calculated
tetramer
-
4 * 92000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
enzyme is phosphorylated by cAMP-dependent protein kinase, but not significantly activated
glycoprotein
-
contains 43% carbohydrate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
half-life 2.5 min
50
-
stable for at least 6 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bharadwaj, G.; Maheshwari, R.
A comparison of thermal characteristics and kinetic parameters of trehalase from a thermophilic and a mesophilic fungus
FEMS Microbiol. Lett.
181
187-193
1999
Thermomyces lanuginosus, Neurospora crassa
Manually annotated by BRENDA team
de Almeida, F.M.; Bonini, B.M.; Beton, D.; Jorge, J.A.; Terenzi, H.F.; da Silva, A.M.
Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme
Protein Expr. Purif.
65
185-189
2009
Neurospora crassa (O42783), Neurospora crassa
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