Information on EC 5.4.99.16 - maltose alpha-D-glucosyltransferase

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

EC NUMBER
COMMENTARY
5.4.99.16
-
RECOMMENDED NAME
GeneOntology No.
maltose alpha-D-glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
maltose = alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycosyl bond isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Starch and sucrose metabolism
-
trehalose biosynthesis IV
-
SYSTEMATIC NAME
IUBMB Comments
maltose alpha-D-glucosylmutase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
57-KDa trehalose synthase (Saccharomyces cerevisiae)
-
-
-
-
Maltose alpha-D-glucosylmutase
-
-
-
-
Maltose alpha-D-glucosyltransferase
-
-
-
-
Maltose glucosylmutase
-
-
-
-
Protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced)
-
-
-
-
Protein (Saccharomyces cerevisiae gene CIF1 reduced)
-
-
-
-
Synthase, trehalose
-
-
-
-
Synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
-
-
-
-
Synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
-
-
-
-
Synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
-
-
-
-
Synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
-
-
-
-
Trehalose synthase
-
-
-
-
Trehalose synthase
A8QX00
-
Trehalose synthase
A8QX00
-
-
Trehalose synthase
B8YM30
-
Trehalose synthase
Arthrobacter aurescens CGMCC 1.1892
B8YM30
-
-
Trehalose synthase
-
-
Trehalose synthase
Corynebacterium glutamicum ATCC13032
-
-
-
Trehalose synthase
B6E9W1
-
Trehalose synthase
-
-
Trehalose synthase
-
-
Trehalose synthase
-
-
Trehalose synthase
Thermus thermophilus HJ6
-
-
-
Trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
-
-
-
-
Trehalose synthetase
-
-
-
-
TreS
A8QX00
-
TreS
A8QX00
-
-
TreS
Arthrobacter aurescens CGMCC 1.1892
B8YM30
-
-
TreS
Corynebacterium glutamicum ATCC13032
-
-
-
TSase
Thermus thermophilus HJ6
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
147994-22-7
protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced) /57-KDa trehalose synthase (Saccharomyces cerevisiae gene CIF1) /protein (Saccharomyces cerevisiae gene CIF1 reduced) /synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
178604-93-8
synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced) /trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
187285-67-2
synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
211621-92-0
synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
395644-91-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain SN223/29
UniProt
Manually annotated by BRENDA team
strain SN223/29
UniProt
Manually annotated by BRENDA team
strain CGMCC 1.1892
UniProt
Manually annotated by BRENDA team
Arthrobacter aurescens CGMCC 1.1892
strain CGMCC 1.1892
UniProt
Manually annotated by BRENDA team
Corynebacterium glutamicum ATCC13032
-
-
-
Manually annotated by BRENDA team
locus Dgeo-0537
UniProt
Manually annotated by BRENDA team
Deinococcus geothermalis 11300
locus Dgeo-0537
UniProt
Manually annotated by BRENDA team
strain CBS-01
Uniprot
Manually annotated by BRENDA team
strain R48
-
-
Manually annotated by BRENDA team
Pimelobacter sp. R48
strain R48
-
-
Manually annotated by BRENDA team
strain F1
-
-
Manually annotated by BRENDA team
strain F1
-
-
Manually annotated by BRENDA team
ATCC 33923
-
-
Manually annotated by BRENDA team
-
Q7WUI5
SwissProt
Manually annotated by BRENDA team
strain HJ6
-
-
Manually annotated by BRENDA team
Thermus thermophilus HJ6
strain HJ6
-
-
Manually annotated by BRENDA team
Meiothermus ruber CBS-01
strain CBS-01
Uniprot
Manually annotated by BRENDA team
additional information
no activity in Thermoproteus tenax strain Kra1
-
-
Manually annotated by BRENDA team
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
maltose
show the reaction diagram
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose
-
-
r
high-maltose rice syrup
alpha,alpha-trehalose
show the reaction diagram
-
-
the highest alpha,alpha-trehalose yield (54.6%) can be obtained by 3.5 units/maltose (g) of trehalose synthase from the maltose syrup at 50C for 20-24 h
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
A8QX00
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
B6E9W1, -
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Q1J0Z5
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
30% yield
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Q7WUI5, -
-
wild-type, 80% yield
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
wild-type, 92% yield
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-, B8YM30
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
r
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose. Maximum conversion rate for maltose into trehalose is independent of substrate concentration and reaches 71% at 20C
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
B1PK99, -
the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate
TreS also has a weak hydrolytic property with D-glucose as the byproduct
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
the maximum conversion yield reaches 69% at 25C after 9 h of reaction
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Pimelobacter sp. R48
-
r
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
Deinococcus geothermalis 11300
Q1J0Z5
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
A8QX00
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
Arthrobacter aurescens CGMCC 1.1892
B8YM30
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Corynebacterium glutamicum ATCC13032
-
the maximum conversion yield reaches 69% at 25C after 9 h of reaction
-
-
r
starch
?
show the reaction diagram
-
-
-
-
?
starch
alpha,alpha-trehalose
show the reaction diagram
-
substrate of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
-
-
?
Sucrose
Trehalulose
show the reaction diagram
-
activity is very low compared to that with maltose
i.e. 1-O-alpha-D-glucopyranosyl-D-fructose
-
sucrose
D-glucose + D-fructose + [alpha-D-glucopyranosyl-(1,1)-D-fructofuranose]
show the reaction diagram
-
low activity on sucrose
-
-
?
maltose
alpha,alpha-trehalose + D-glucose + maltose
show the reaction diagram
Thermus thermophilus, Thermus thermophilus HJ6
-
-
the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
additional information
?
-
-
no substrates: glucose, fructose, lactose, sucrose, starch
-
-
-
additional information
?
-
A8QX00
does not use acarbose and glucose as substrates
-
-
-
additional information
?
-
-
TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
-
-
-
additional information
?
-
A8QX00
does not use acarbose and glucose as substrates
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-, B8YM30
123% relative activity at 1 mM
Fe2+
-
114% activity at 1 mM
K+
-
10 mM, 22% increase in activity
Mg2+
-
10 mM, 29% increase in activity
Mg2+
-, B8YM30
118% relative activity at 1 mM
Mg2+
-
112% activity at 1 mM
Mn2+
-, B8YM30
116% relative activity at 1 mM
Mn2+
B6E9W1, -
Mn2+ shows an enhancing effect by 11% at 1 mM
additional information
B6E9W1, -
TreS activity is not affected by NH4+, Ca2+, and Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Al3+
-
1 mM, complete inhibition
Al3+
B1PK99, -
complete inhibition at 2 mM
beta-mercaptoethanol
B6E9W1, -
complete inhibition at 1 mM
Ca2+
-
the MTase activity of TreS is inhibited by 5 mM Ca2+ and other divalent cations
Ca2+
-, B8YM30
98% residual activity at 5 mM
Ca2+
B1PK99, -
about 10% residual activity at 10 mM
Ca2+
-
93% residual activity at 5 mM
Co2+
B1PK99, -
about 5% residual activity at 10 mM
Co2+
Q1J0Z5
1 mM, 55% residual activity
Cu2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Cu2+
-
10 mM, 85% residual activity
Cu2+
-, B8YM30
complete inhibition at 5 mM
Cu2+
B1PK99, -
complete inhibition at 2 mM
Cu2+
B6E9W1, -
52% residual activity at 1 mM
Cu2+
-
45.4% residual activity at 5 mM
Cu2+
Q1J0Z5
1 mM, 5% residual activity
D-glucose
B1PK99, -
in the presence of 10 mM D-glucose, TreS shows a 3.6fold increase in Km and a nearly unchanged Vmax for maltose, implying that D-glucose is a competitive inhibitor of TreS
EDTA
-, B8YM30
86% residual activity at 5 mM
EDTA
-
68.5% residual activity at 5 mM
EDTA
Q1J0Z5
inhibitory above 1 mM
Fe2+
B1PK99, -
complete inhibition at 2 mM
-
Fe2+
B6E9W1, -
92% residual activity at 1 mM
-
Fe3+
Q1J0Z5
1 mM, 60% residual activity
-
Hg2+
-
1 mM, complete inhibition
Hg2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Hg2+
B6E9W1, -
57% residual activity at 1 mM
Hg2+
Q1J0Z5
1 mM, 15% residual activity
Mg2+
-, B8YM30
92% residual activity at 5 mM
Mg2+
Q1J0Z5
1 mM, 75% residual activity
Mn2+
-
10 mM, 60% residual activity
Mn2+
-, B8YM30
86% residual activity at 5 mM
Mn2+
B1PK99, -
about 10% residual activity at 10 mM
Na+
B6E9W1, -
90% residual activity at 1 mM
Ni2+
B1PK99, -
about 10% residual activity at 10 mM
Ni2+
-
49.4% residual activity at 5 mM
Pb2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
SDS
-, B8YM30
complete inhibition at 1 mM
SDS
B6E9W1, -
10% residual activity at 1 mM
SDS
-
0.25% residual activity at 5 mM
sodium dodecylsulfate
-
1 mM, complete inhibition
Sucrose
-
competitive inhibition of the interconversion between maltose and trehalose
Tris
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Tris
Q1J0Z5
10 mM, 9% residual activity
Zn2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Zn2+
-
10 mM, 20% residual activity
Zn2+
B1PK99, -
complete inhibition at 2 mM
Zn2+
B6E9W1, -
59% residual activity at 1 mM
Zn2+
-
71.6% residual activity at 5 mM
Zn2+
Q1J0Z5
1 mM, 29% residual activity
Mn2+
-
60.9% residual activity at 5 mM
additional information
-
not inhibited by acarbose
-
additional information
B6E9W1, -
TreS activity is not affected by EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
Q1J0Z5
1 mM, 110% of initial activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
75
-
alpha,alpha-trehalose
B6E9W1, -
in 50 mM phosphate buffer (pH 6) at 37C
90
-
alpha,alpha-trehalose
-
in 40 mM potassium phosphate buffer (pH 6.8), at 37C
98.9
-
alpha,alpha-trehalose
B1PK99, -
-
1.1
-
maltose
-
-
10
-
maltose
-
in 40 mM potassium phosphate buffer (pH 6.8), at 37C
25
-
maltose
B6E9W1, -
in 50 mM phosphate buffer (pH 6) at 37C
34.5
-
maltose
-
-
42.4
-
maltose
-
45C, pH 6.0
126.2
-
maltose
B1PK99, -
-
137.8
-
maltose
-
45C, pH 6.0, presence of 10 mM glucose
254
-
maltose
Q1J0Z5
pH 7.6, 40C
96.5
-
Sucrose
-
-
26
-
trehalose
-
-
158
-
trehalose
-
-
210.3
-
trehalose
-
45C, pH 6.0
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
68.9
-
alpha,alpha-trehalose
B1PK99, -
-
31.9
-
maltose
Q1J0Z5
pH 7.6, 40C
95
-
maltose
-
45C, pH 6.0
97.8
-
maltose
-
45C, pH 6.0, presence of 10 mM glucose
147
-
maltose
B1PK99, -
-
187.6
-
trehalose
-
45C, pH 6.0
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.7
-
alpha,alpha-trehalose
B1PK99, -
-
6709
1.17
-
maltose
B1PK99, -
-
12854
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.76
-
D-glucose
B1PK99, -
-
0.000025
-
validoxylamine
-
in 40 mM potassium phosphate buffer (pH 6.8), at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.05
-
-
cell-free extract, at pH 6.0 and 45C for 25 min using maltose as substrate
0.25
-
-
after 5.3fold purification, at pH 6.0 and 45C for 25 min using maltose as substrate
0.96
-
-
Mn2+-loaded, immobilized enzyme at pH 6.0 and 40C
1.17
-
-
Fe3+-loaded, immobilized enzyme at pH 6.0 and 40C
1.55
-
-
Cu2+-loaded, immobilized enzyme at pH 6.0 and 40C
2.84
-
-
Ni2+-loaded, immobilized enzyme at pH 6.0 and 40C
3.3
-
-
Zn2+-loaded, immobilized enzyme at pH 6.0 and 40C
3.98
-
-
Co2+-loaded, immobilized enzyme at pH 6.0 and 40C
14.95
-
Q1J0Z5
pH 7.6, 40C
16.8
-
-
-
18.5
-
B6E9W1, -
purified enzyme, at 37C
41.2
-
-
-
80
-
-
45C, pH 6.0
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
pH optimum for enzyme and for recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
6
-
-
both the free and the immobilized enzyme exhibit an optimal reaction pH of 6.0
6.5
-
Q7WUI5
-
6.5
-
-, B8YM30
-
6.5
-
B1PK99, -
-
7
-
A8QX00
in 100 mM phosphate buffer
7
-
-
both free and chitosan-immobilized enzymes
7
-
-
at 35C in Na-phosphate buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
7
-
pH 5: about 25% of maximal activity, pH 7: about 55% of maximal activity
5
7.5
-
more than 80% of maximum activity within this range
6
7
B1PK99, -
-
6.5
9
-
more than 80% of activity is maintained from pH 6.5 and 7.5, the activities of the enzyme markedly decrease in 50 mM Tris-HCl buffer from pH 7.0-9.0
6.8
8.8
Q1J0Z5
more than 80% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
-
wild-type
35
-
-, B8YM30
-
40
-
-
maximal yield of trehalulose from sucrose
40
-
-
fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus
40
-
Q7WUI5
both deletion mutant lacking 415 amino acids from C-terminus, and fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus
40
-
A8QX00
in 100 mM phosphate buffer
40
-
-
immobilized enzyme
45
-
-
free enzyme
50
-
B1PK99, -
-
65
-
Q7WUI5
wild-type
70
80
-
both free and chitosan-immobilized enzymes
70
-
-
temperature optimum for enzyme and for recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
55
Q1J0Z5
more than 80% of maximum activity
50
-
-
at 50C a higher relative activity, 88.8%, is observed for the immobilized enzyme, compared to 76.92% for the free enzyme
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
calculated
4.9
-
Q1J0Z5
calculated
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
61800
-
B6E9W1, -
predicted from amino acid sequence
65000
-
B6E9W1, -
His-tagged enzyme, SDS-PAGE
68000
-
-, B8YM30
SDS-PAGE
110000
-
B1PK99, -
SDS-PAGE
132300
-
Q1J0Z5
gel filtration, recombinant protein
250000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 105000, SDS-PAGE
?
-
x * 110000, calculation from nucleotide sequence
?
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
?
-
x * 60700, wild-type, calculated, x * 61000, wild-type, SDS-PAGE, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
Q7WUI5
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 65000, SDS-PAGE
?
-
x * 70000, calculated from amino acid sequence
?
Corynebacterium glutamicum ATCC13032
-
x * 70000, calculated from amino acid sequence
-
dimer
Q1J0Z5
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
dimer
Deinococcus geothermalis 11300
-
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
-
homohexamer
-
6 * 65000, SDS-PAGE; 6 * 68000, gel filtration
tetramer
-
4 * 67000, SDS-PAGE
tetramer
-
4 * 67000, SDS-PAGE
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
B1PK99, -
the enzyme can maintain very high activity (above 90%) at pH 4.0-8.0 for 5 h, below pH 5.0 the enzyme shows no activity
5
7
-
both enzyme and recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa, stable
5.5
7.5
-, B8YM30
-
5.5
8
-
wild-type
5.5
9.5
-
60C, 60 min, stable
6
9
-
20C, 60 min, stable
6.5
8
-
the enzyme activity declines significantly at pH above 6.5. At pH 8.0 a complete loss in enzyme activity is observed for both the free and the immobilized enzyme. At pH5.0, the immobilized enzyme exhibits a relative activity, 82.13%, higher than the free enzyme, 50.57%.
6.6
7.4
-
30 min, more than 80% residual activity
7
9
-
37C, 1 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
pH 7.0, 60 min, stable up to
35
-
-
60 min, more than 80% residual activity
40
60
-, B8YM30
the enzyme remains stable up to 40C, and shows complete loss of activity at 60C
40
-
-
30 min, more than 80% residual activity
40
-
-
about 80% of activity is retained at 40C, but the enzyme is not stable at higher temperature than 40C
40
-
Q1J0Z5
half-life 42 h
55
-
-
pH 7.0, 1 h, stable below
55
-
Q1J0Z5
8 h, 57% residual activity
60
-
-
pH 6.0, stable for 20 min
60
-
-
30 min, wild-type, almost complete loss of activity, fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, 83% residual activity
60
-
B1PK99, -
the enzyme maintains very high activity (above 90%) at 60C for 5 h
60
-
Q1J0Z5
2 h, 20% residual activity
65
-
-
the wild type enzyme retains 40% of activity after 120 min at 65C
70
80
-
the half-life of heat inactivation for free and chitosan-immobilized enzymes is 5.7 and 6.3 days at 70C, respectively. The free enzyme displays complete loss of activity after 8 days at 80C, whereas the chitosan-immobilized enzyme still retains about 25% of the initial activity
80
-
-
pH 7.0, 60 min, stable up to
80
-
Q7WUI5
30 min, wild-type, 88% residual activity, fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, 83% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme immobilized with highly porous cross-linked polystyrene divinylbezene-based metal chelator maintains a residual activity of ca. 80% after 24 cycles
-
when tested in batch reaction, the immobilized enzyme retains its relative activity of 53% after 30 reuses of reaction within 12 days
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 150 days, retains 82% of its initial activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA column chromatography
A8QX00
Ni-NTA column chromatography
-, B8YM30
Ni-NTA column chromatography
-
Ni-NTAcolumn chromatography
B6E9W1, -
Ni-NTA column chromatography
B1PK99, -
Ni column chromatography, DEAE-cellulose column chromatography, hydroxyapatite column chromatography, aminohexylagarose column chromatography, phenyl-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Ni column chromatography
-
HiTrap Chelating HP column chromatography
-
recombinant enzyme
-
recombinant enzyme
-
recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase and vice versa having both activities
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
A8QX00
expressed in Escherichia coli BL21(DE3) cells
-, B8YM30
expressed in Escherichia coli MC1061 cells
-
expression in Escherichia coli
Q1J0Z5
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
B6E9W1, -
expressed in Escherichia coli Rosetta gami (DE3) cells
B1PK99, -
expressed in Escherichia coli Rosetta-gami B cells
-
expression in Escherichia coli
-
expression in Escherichia coli
-
construction of fusion genes from beta-amylase gene of Clostridium thermofluorogenes and trehalose synthase and overexpression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
Q7WUI5
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression induction with 0.4 mM IPTG at 25C for 5 h is the best condition for the expression of soluble TreS, higher temperature or IPTG concentrations lead to a higher rate of inclusion bodies, whereas a temperature below 20C and lower IPTG concentrations decreases the total amount of TreS
-, B8YM30
expression induction with 0.4 mM IPTG at 25C for 5 h is the best condition for the expression of soluble TreS, higher temperature or IPTG concentrations lead to a higher rate of inclusion bodies, whereas a temperature below 20C and lower IPTG concentrations decreases the total amount of TreS
Arthrobacter aurescens CGMCC 1.1892
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A255P
-
2.0% activity compared to the wild type enzyme
D411P
-
3.2% activity compared to the wild type enzyme
D41P
-
99.6% activity compared to the wild type enzyme
E469P
-
50% activity compared to the wild type enzyme
I121P
-
21.3% activity compared to the wild type enzyme
I385P
-
5.1% activity compared to the wild type enzyme
K332P
-
96.7% activity compared to the wild type enzyme
N503P
-
the mutant shows about 39% higher relative activity than that of the wild type at 65C for 120 min. The trehalose yield of the mutant is 1.3fold higher than that of the wild type with sweet potato starch as substrate at 50C for 4 h
R523P
-
90.8% activity compared to the wild type enzyme
synthesis
-
use of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa for production of trehalose from starch. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
additional information
-
fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
S439P
-
20.8% activity compared to the wild type enzyme
additional information
Q7WUI5
deletion mutant lacking 415 amino acids from C-terminus has a lower thermostability and produces more byproducts than wild-type. Fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
immobilization of recombinant enzyme on Eupergit C250L for the production of trehalose. Immobilization does not affect optimum pH value, optimum temperature is shifted from 45C to 65C. Immobilized enzyme is stable at 70C for 16 days and can be used more than 10times in batch reaction. A maximum yield of 42% trehalose can be reached from 50 g/l maltose