BRENDA - Enzyme Database show
show all sequences of 5.3.1.15

Substrate specificity of a recombinant D-lyxose isomerase from Serratia proteamaculans that produces D-lyxose and D-mannose

Park, C.S.; Yeom, S.J.; Lim, Y.R.; Kim, Y.S.; Oh, D.K.; Lett. Appl. Microbiol. 51, 343-350 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli ER2566 cells
Serratia proteamaculans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Serratia proteamaculans
EDTA
-
Serratia proteamaculans
Fe2+
-
Serratia proteamaculans
Ni2+
-
Serratia proteamaculans
Zn2+
-
Serratia proteamaculans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.83
-
D-xylulose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
13.3
-
D-Lyxose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
19.4
-
D-fructose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
32.2
-
D-mannose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
the addition of Ca2+ ion to EDTA-treated enzyme enhances the activity of D-lyxose isomerization
Serratia proteamaculans
Mn2+
maximum activity (190%) in the presence of 1 mM Mn2+
Serratia proteamaculans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26756
-
2 * 26756, calculated from amino acid sequence
Serratia proteamaculans
27000
-
2 * 27000, SDS-PAGE
Serratia proteamaculans
54000
-
gel filtration
Serratia proteamaculans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Serratia proteamaculans
D5MTT1
-
-
Serratia proteamaculans KCTC 2936
D5MTT1
-
-
Purification (Commentary)
Commentary
Organism
His-Trap column chromatography
Serratia proteamaculans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.02
-
using L-sorbose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.14
-
using L-ribose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.19
-
using D-talose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.28
-
using D-tagatose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.4
-
using L-ribulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
1.05
-
using L-gulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
1.41
-
using D-fructose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
5.42
-
using D-mannose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
10
-
using D-lyxose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
26.2
-
using D-xylulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose
-
716074
Serratia proteamaculans
D-mannose
-
-
-
r
D-Lyxose
highest activity
716074
Serratia proteamaculans
D-Xylulose
-
-
-
r
D-Lyxose
highest activity
716074
Serratia proteamaculans KCTC 2936
D-Xylulose
-
-
-
r
D-Mannose
-
716074
Serratia proteamaculans
D-Fructose
-
-
-
r
D-Mannose
-
716074
Serratia proteamaculans KCTC 2936
D-Fructose
-
-
-
r
D-talose
-
716074
Serratia proteamaculans
D-tagatose
-
-
-
r
D-talose
-
716074
Serratia proteamaculans KCTC 2936
D-tagatose
-
-
-
r
D-xylulose
-
716074
Serratia proteamaculans
D-lyxose
-
-
-
r
L-gulose
-
716074
Serratia proteamaculans
L-sorbose
-
-
-
r
L-ribose
-
716074
Serratia proteamaculans
L-ribulose
-
-
-
r
L-ribose
-
716074
Serratia proteamaculans KCTC 2936
L-ribulose
-
-
-
r
additional information
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
716074
Serratia proteamaculans
?
-
-
-
-
additional information
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
716074
Serratia proteamaculans KCTC 2936
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
homodimer
2 * 26756, calculated from amino acid sequence; 2 * 27000, SDS-PAGE
Serratia proteamaculans
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
-
Serratia proteamaculans
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
50
the enzyme shows half-lives of 84 h, 17 h, 2.6 h, 0.3 h, and 0.09 h at 30C, 35C, 40C, 45C, and 50C, respectively
Serratia proteamaculans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4297
-
D-fructose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
16170
-
D-mannose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
30810
-
D-Lyxose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
31620
-
D-xylulose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Serratia proteamaculans
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli ER2566 cells
Serratia proteamaculans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Serratia proteamaculans
EDTA
-
Serratia proteamaculans
Fe2+
-
Serratia proteamaculans
Ni2+
-
Serratia proteamaculans
Zn2+
-
Serratia proteamaculans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.83
-
D-xylulose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
13.3
-
D-Lyxose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
19.4
-
D-fructose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
32.2
-
D-mannose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
the addition of Ca2+ ion to EDTA-treated enzyme enhances the activity of D-lyxose isomerization
Serratia proteamaculans
Mn2+
maximum activity (190%) in the presence of 1 mM Mn2+
Serratia proteamaculans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26756
-
2 * 26756, calculated from amino acid sequence
Serratia proteamaculans
27000
-
2 * 27000, SDS-PAGE
Serratia proteamaculans
54000
-
gel filtration
Serratia proteamaculans
Purification (Commentary) (protein specific)
Commentary
Organism
His-Trap column chromatography
Serratia proteamaculans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.02
-
using L-sorbose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.14
-
using L-ribose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.19
-
using D-talose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.28
-
using D-tagatose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
0.4
-
using L-ribulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
1.05
-
using L-gulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
1.41
-
using D-fructose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
5.42
-
using D-mannose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
10
-
using D-lyxose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
26.2
-
using D-xylulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-fructose
-
716074
Serratia proteamaculans
D-mannose
-
-
-
r
D-Lyxose
highest activity
716074
Serratia proteamaculans
D-Xylulose
-
-
-
r
D-Lyxose
highest activity
716074
Serratia proteamaculans KCTC 2936
D-Xylulose
-
-
-
r
D-Mannose
-
716074
Serratia proteamaculans
D-Fructose
-
-
-
r
D-Mannose
-
716074
Serratia proteamaculans KCTC 2936
D-Fructose
-
-
-
r
D-talose
-
716074
Serratia proteamaculans
D-tagatose
-
-
-
r
D-talose
-
716074
Serratia proteamaculans KCTC 2936
D-tagatose
-
-
-
r
D-xylulose
-
716074
Serratia proteamaculans
D-lyxose
-
-
-
r
L-gulose
-
716074
Serratia proteamaculans
L-sorbose
-
-
-
r
L-ribose
-
716074
Serratia proteamaculans
L-ribulose
-
-
-
r
L-ribose
-
716074
Serratia proteamaculans KCTC 2936
L-ribulose
-
-
-
r
additional information
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
716074
Serratia proteamaculans
?
-
-
-
-
additional information
no activity with D-mannose 6-phosphate, D-glucose 6-phosphate, and D-ribose 6-phosphate
716074
Serratia proteamaculans KCTC 2936
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 26756, calculated from amino acid sequence; 2 * 27000, SDS-PAGE
Serratia proteamaculans
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
-
Serratia proteamaculans
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
50
the enzyme shows half-lives of 84 h, 17 h, 2.6 h, 0.3 h, and 0.09 h at 30C, 35C, 40C, 45C, and 50C, respectively
Serratia proteamaculans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4297
-
D-fructose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
16170
-
D-mannose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
30810
-
D-Lyxose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
31620
-
D-xylulose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Serratia proteamaculans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
222
-
D-fructose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
502
-
D-mannose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
2333
-
D-Lyxose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
9560
-
D-xylulose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
222
-
D-fructose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
502
-
D-mannose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
2333
-
D-Lyxose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
9560
-
D-xylulose
at pH 7.5 and 40C, in the presence of 1 mM Mn2+
Serratia proteamaculans
Other publictions for EC 5.3.1.15
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748502
Huang
Production of D-mannose from ...
Thermosediminibacter oceani, Thermosediminibacter oceani DSM 16646
J. Sci. Food. Agric.
98
4895-4902
2018
-
1
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747682
Patel
A single and two step isomeri ...
Cohnella laeviribosi
Enzyme Microb. Technol.
97
27-33
2017
-
1
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
749201
Yu
-
Efficient biotransformation o ...
Thermosediminibacter oceani, Thermosediminibacter oceani DSM 1664
Process Biochem.
51
2026-2033
2016
-
1
-
-
-
-
3
3
-
4
1
-
-
2
-
-
-
-
-
-
-
-
6
1
1
-
3
3
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
3
-
4
1
-
-
-
-
-
-
-
-
-
6
1
1
-
3
3
1
1
-
-
-
-
-
-
3
3
727225
Choi
Characterization of a recombin ...
Dictyoglomus turgidum, Dictyoglomus turgidum DSM 6724
Biotechnol. Lett.
34
1079-1085
2012
-
-
1
-
-
-
2
4
-
2
2
2
-
2
-
-
1
-
-
-
11
-
16
1
1
-
1
4
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
4
-
2
2
2
-
-
-
1
-
-
11
-
16
1
1
-
1
4
1
-
-
-
-
-
-
-
4
4
713845
Patel
Substrate specificity of the B ...
Bacillus licheniformis
Appl. Environ. Microbiol.
77
3343-3350
2011
-
-
1
-
-
-
-
2
-
4
1
-
-
4
-
-
1
-
-
-
2
-
3
1
-
1
1
2
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
4
1
-
-
-
-
1
-
-
2
-
3
1
-
1
1
2
1
-
-
-
-
-
-
-
2
2
716872
Marles-Wright
The structure of a D-lyxose is ...
Bacillus subtilis 168, Bacillus subtilis
Proteins Struct. Funct. Bioinform.
79
2015-2019
2011
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714568
Park
Mannose production from fructo ...
Providencia stuartii
Biotechnol. Lett.
32
1305-1309
2010
-
-
-
-
-
2
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
715675
Kwon
Substrate specificity of a rec ...
Providencia stuartii, Providencia stuartii KCTC 2568
J. Biosci. Bioeng.
110
26-31
2010
-
1
1
-
-
-
7
4
-
2
3
-
-
3
-
-
1
-
-
-
20
-
18
1
1
1
1
4
1
1
-
-
-
-
-
-
1
1
-
-
-
-
-
7
-
4
-
2
3
-
-
-
-
1
-
-
20
-
18
1
1
1
1
4
1
1
-
-
-
-
-
-
4
4
716074
Park
Substrate specificity of a rec ...
Serratia proteamaculans, Serratia proteamaculans KCTC 2936
Lett. Appl. Microbiol.
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