Information on EC 2.4.1.64 - alpha,alpha-trehalose phosphorylase

Word Map on EC 2.4.1.64
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
2.4.1.64
-
RECOMMENDED NAME
GeneOntology No.
alpha,alpha-trehalose phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose + phosphate = D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Starch and sucrose metabolism
-
-
trehalose degradation IV
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose:phosphate beta-D-glucosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37205-59-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Glycine max Merril cv. Beeson 80 in symbiosis with Bradyrhizobium japonicum
-
-
Manually annotated by BRENDA team
strain SM-ZK
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-deoxy-D-glucose + alpha-D-glucose 1-phosphate
alpha-D-glucopyranosyl 6-deoxy-alpha-D-glucopyranoside + phosphate
show the reaction diagram
-
at 93% the activity with rate of glucose glucosylation
-
-
alpha,alpha-trehalose + phosphate
alpha-D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
alpha,alpha-trehalose + phosphate
beta-D-glucose 1-phosphate + D-glucose
show the reaction diagram
alpha,alpha-trehalose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
alpha-D-galactopyranosyl alpha-D-glucopyranoside + phosphate
D-glucose + beta-D-galactose 1-phosphate
show the reaction diagram
-
while the wild type enzyme shows very low activity, the mutant enzyme L649G/A693Q/W371Y displays a strict specificity (99%) for beta-D-galactose 1-phosphate as product
-
-
r
beta-D-glucose 1-phosphate + alpha-D-allose
?
show the reaction diagram
-
4.5% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-D-arabinose
?
show the reaction diagram
-
1.8% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-D-fucose
?
show the reaction diagram
-
22% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-D-galactose
?
show the reaction diagram
-
83.7% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-D-lyxose
?
show the reaction diagram
-
1.3% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-D-mannose
?
show the reaction diagram
-
14.1% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-D-xylose
?
show the reaction diagram
-
135.2% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + alpha-L-fucose
?
show the reaction diagram
-
109.2% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + beta-L-arabinose
?
show the reaction diagram
-
79.9% activity compared to D-glucose
-
-
r
beta-D-glucose 1-phosphate + D-galactose
? + phosphate
show the reaction diagram
low activity. The Km value for D-galactose is about 30fold higher than that for D-glucose
-
-
r
beta-D-glucose 1-phosphate + D-glucose
alpha,alpha-trehalose + phosphate
show the reaction diagram
-
100% activity with D-glucose
-
-
r
beta-D-glucose-1-phosphate + gentiobiose
6-O-beta-D-glucopyranosyl trehalose + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + isomaltose
6-O-alpha-D-glucopyranosyl trehalose + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + isomaltotriose
?
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + isopanose
?
show the reaction diagram
-
-
-
-
?
beta-D-glucose-1-phosphate + melibiose
6-O-alpha-D-galactopyranosyl trehalose + phosphate
show the reaction diagram
-
-
-
-
?
D-galactose + beta-D-glucose 1-phosphate
lactotrehalose + phosphate
show the reaction diagram
-
-
-
-
r
D-glucose + beta-D-galactose 1-phosphate
alpha-D-galactopyranosyl alpha-D-glucopyranoside + phosphate
show the reaction diagram
-
-
-
-
r
D-glucose + beta-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
show the reaction diagram
lactotrehalose + phosphate
D-galactose + beta-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
xylose + beta-D-glucose 1-phosphate
glucosyl-1,1-xylose 1-phosphate
show the reaction diagram
-
glucosylated at 23% of the rate of glucose glucosylation
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose + phosphate
D-glucose + beta-D-glucose 1-phosphate
show the reaction diagram
D-galactose + beta-D-glucose 1-phosphate
lactotrehalose + phosphate
show the reaction diagram
-
-
-
-
r
D-glucose + beta-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
show the reaction diagram
lactotrehalose + phosphate
D-galactose + beta-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
essential for enzymatic activity. Decreasing potassium ion concentrations significantly reduce thermal and pH stabilities of the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
-
1 mM, complete inhibition
alpha,alpha-trehalose
-
D-glucose
-
strong substrate inhibition, 500 mM D-glucose reduces the enzyme activity to 49.1% of the activity at the saturating concentration of 30 mM
fructose 2,6-diphosphate
-
inhibition in both directions
Ni2+
-
1 mM, 88% inhibition
validamycin A
-
10 mM, complete inhibition
validoxylamine A
-
0.2 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86
alpha,alpha-trehalose
recombinant enzyme, at pH 6.5 and 30C
64.8
alpha-D-arabinose
-
in 50 mM MES buffer (pH 6.0), at 60C
171.5
alpha-D-galactose
-
in 50 mM MES buffer (pH 6.0), at 60C
20.3
alpha-D-xylose
-
in 50 mM MES buffer (pH 6.0), at 60C
183.4
alpha-L-fucose
-
in 50 mM MES buffer (pH 6.0), at 60C
0.7 - 3.8
beta-D-galactose 1-phosphate
-
0.7 - 38
beta-D-glucose 1-phosphate
3 - 447.6
D-galactose
0.6 - 36.8
D-glucose
23 - 32
glucose
0.14 - 9.4
phosphate
0.97 - 33
trehalose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
210
alpha,alpha-trehalose
Bacillus selenitireducens
D6XSD4
recombinant enzyme, at pH 6.5 and 30C
51.4
alpha-D-arabinose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
54
alpha-D-galactose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
64.3
alpha-D-xylose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
68.1
alpha-L-fucose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
1.2 - 1.6
beta-D-galactose 1-phosphate
-
7.4 - 660
beta-D-glucose 1-phosphate
0.5 - 113
D-galactose
4.2 - 86
D-glucose
660
glucose
Kocuria varians
-
-
200
phosphate
Kocuria varians
-
-
200
trehalose
Kocuria varians
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.793
alpha-D-arabinose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
17683
0.315
alpha-D-galactose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
1087
3.17
alpha-D-xylose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
2945
0.371
alpha-L-fucose
Caldanaerobacter subterraneus subsp. pacificus
-
in 50 mM MES buffer (pH 6.0), at 60C
763
0.149 - 1.29
D-galactose
71
0.872 - 36
D-glucose
35
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
95
alpha,alpha-trehalose
recombinant enzyme, at pH 6.5 and 30C
0.0005 - 0.0012
fructose 2,6-diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity of trehalose phosphorylase in L3 larvae is 10times higher than in L4 larvae
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
the pH optimum is slightly different for both reaction directions, with a lower optimum (about pH 5.5) for the synthesis reaction
6
-
synthesis of trehalose
6 - 7
-
synthesis of trehalose
7 - 7.5
-
phosphorolysis of trehalose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
-
activity is over 90% in the range of pH 4.5 to 7.0
5.5 - 7.5
-
stable
5.7 - 7.8
-
about half-maximal activity at pH 5.7 and 7.8, trehalose synthesis
6 - 8
-
about half-maximal activity at pH 6 and 8, phosphorolysis
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
-
both directions
37
-
assay at
70
-
both directions
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from root nodule of Glycine max
Manually annotated by BRENDA team
-
and muscle, high activity
Manually annotated by BRENDA team
-
and cuticle, high activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84995
-
2 * 84995, calculated from amino acid sequence
87889
2 * 87889, calculated from amino acid sequence
90487
-
x * 90487, calculated from amino acid sequence
105000
-
6 * 105000, SDS-PAGE
170000
gel filtration
190000
-
gel filtration
344000
-
sucrose density gradient centrifugation
570000 - 580000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 105000, SDS-PAGE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using either 10% (w/v) PEG 4000, 0.1 M Tris-HCl pH 7.5, and 1% (v/v) 2-propanol or 10% (w/v) PEG 4000, 0.1 M Tris-HCl pH 7.5, and 1% (w/v) n-octyl-beta-D-glucoside
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
native enzyme, stable
489322
6 - 9
-
stable
489328
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable below
40
-
stable below, pH 7.0, at least 30 min
65
-
no loss of activity after 1 h of incubation at 65C
72
-
50% residual activity remains after 1 h of incubation at 72C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme retains full activity during 5 months at -14C with several freezings and thawings, in presence of 2 mM phosphate buffer, pH 7.0, beta-D-glucose-1-phosphate and alpha-D-glucose-1-phosphate
-
loss of activity when extracts are desalted by dialysis or passage through Sephadex G-25 in presence of water. When dialysis is carried out against 5 mM NaCl, glucose 6-phosphate, EDTA, or imidazole-HCl buffer, pH 7.0, the enzymatic activity is maintained only for a few h
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
14C,in presence of 2 mM phosphate buffer, pH 7.0, beta-D-glucose-1-phosphate and alpha-D-glucose-1-phosphate, enzyme retains full activity during 5 months with several freezings and thawings
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
Ni-NTA agarose resin column chromatography
-
Ni-Sepharose column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli XL10 Gold cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L649G
-
the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme
L649G/A693Q
-
the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme
L649G/A693Q/W371Y
-
the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme but displays a strict specificity (99%) for beta-D-galactose 1-phosphate as product
A431T
the mutant shows strongly decreased catalytic efficiency for D-glucose and decreased catalytic efficiency for D-galactose compared to the wild type enzyme
A440E
the mutant shows increased catalytic efficiency for D-glucose and wild type catalytic efficiency for D-galactose compared to the wild type enzyme
A440K
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440M
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/N657Y
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/R448S
the mutant shows increased catalytic efficiency for D-glucose and strongly increased catalytic efficiency for D-galactose compared to the wild type enzyme
N657D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657G
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657I
the mutant shows approximate 2fold increase in affinity for D-galactose
N657L
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657R
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657Y
the mutant shows approximate 2fold increase in affinity for D-galactose
P588H
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448F
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448N
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S/N657Y
the mutant shows about wild type catalytic efficiencies for D-glucose and D-galactose
R448V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
additional information
-
construction of chimeric phosphorylases of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
synthesis of trehalose from maltose by a coupled enzyme system with trehalose phosphorylase and maltose phosphorylase
Show AA Sequence (232 entries)
Please use the Sequence Search for a specific query.