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Literature summary extracted from

  • Yeom, S.J.; Kim, Y.S.; Lim, Y.R.; Jeong, K.W.; Lee, J.Y.; Kim, Y.; Oh, D.K.
    Molecular characterization of a novel thermostable mannose-6-phosphate isomerase from Thermus thermophilus (2011), Biochimie, 93, 1659-1667.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.8 expressed in Escherichia coli ER2566 cells Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.8 D138A the mutant shows 59% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 E132A the mutant shows 1.9% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 E132D the mutant shows 0.4% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 E132K inactive Thermus thermophilus
5.3.1.8 E132Q inactive Thermus thermophilus
5.3.1.8 E132W inactive Thermus thermophilus
5.3.1.8 E67A the mutant shows 2.5% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 E67D the mutant shows 3.7% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 E67K inactive Thermus thermophilus
5.3.1.8 E67Q the mutant shows 0.8% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 E67W inactive Thermus thermophilus
5.3.1.8 H122A the mutant shows 2.8% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 H122D inactive Thermus thermophilus
5.3.1.8 H122K inactive Thermus thermophilus
5.3.1.8 H122Q the mutant shows 2.0% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 H122W inactive Thermus thermophilus
5.3.1.8 H50A the mutant shows 2.2% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 H50D inactive Thermus thermophilus
5.3.1.8 H50K inactive Thermus thermophilus
5.3.1.8 H50Q the mutant shows 2.0% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 H50W inactive Thermus thermophilus
5.3.1.8 K37A the mutant shows 21% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 K65A the mutant shows 15% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 L18A the mutant shows 78% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 L39A the mutant shows 84% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 Q48A the mutant shows 2.0% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 Q48D inactive Thermus thermophilus
5.3.1.8 Q48K inactive Thermus thermophilus
5.3.1.8 Q48N inactive Thermus thermophilus
5.3.1.8 Q48W inactive Thermus thermophilus
5.3.1.8 R11A the mutant shows 260% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 R142A the mutant shows 2.6% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 R142D inactive Thermus thermophilus
5.3.1.8 R142K inactive Thermus thermophilus
5.3.1.8 R142N inactive Thermus thermophilus
5.3.1.8 R142W inactive Thermus thermophilus
5.3.1.8 W13A the mutant shows 0.4% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 W13D inactive Thermus thermophilus
5.3.1.8 W13F the mutant shows 41% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 W13H the mutant shows 52% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 W13K inactive Thermus thermophilus
5.3.1.8 W13Q inactive Thermus thermophilus
5.3.1.8 W13Y the mutant shows 68% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 W69A the mutant shows 50% activity compared to the wild type enzyme Thermus thermophilus
5.3.1.8 Y124A the mutant shows 52% activity compared to the wild type enzyme Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.8 Ba2+ about 30% inhibition at 0.5 mM Thermus thermophilus
5.3.1.8 EDTA complete inhibition at 0.5 mM Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.8 0.18
-
D-mannose 6-phosphate mutant enzyme E132A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.18
-
D-mannose 6-phosphate mutant enzyme E67A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.21
-
D-mannose 6-phosphate wild type enzyme, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.22
-
D-fructose 6-phosphate wild type enzyme, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.27
-
D-mannose 6-phosphate mutant enzyme H122A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.33
-
D-mannose 6-phosphate mutant enzyme H50A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.53
-
D-mannose 6-phosphate mutant enzyme Q48A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 0.85
-
D-mannose 6-phosphate mutant enzyme W13A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 1.29
-
D-mannose 6-phosphate mutant enzyme R142A, pH 7.0, 80°C Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.8 Ca2+ the enzyme is not stimulated by Ca2+ Thermus thermophilus
5.3.1.8 Co2+ about 230% activity at 0.5 mM Thermus thermophilus
5.3.1.8 Cu2+ about 135% activity at 0.5 mM Thermus thermophilus
5.3.1.8 Fe2+ about 125% activity at 0.5 mM Thermus thermophilus
5.3.1.8 Mg2+ about 175% activity at 0.5 mM Thermus thermophilus
5.3.1.8 Mn2+ about 175% activity at 0.5 mM Thermus thermophilus
5.3.1.8 Zn2+ Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+ Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.8 29000
-
1 * 29000, SDS-PAGE Thermus thermophilus
5.3.1.8 29054
-
1 * 29054, calculated from amino acid sequence Thermus thermophilus
5.3.1.8 29100
-
gel filtration Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.8 Thermus thermophilus Q5SIM4
-
-
5.3.1.8 Thermus thermophilus KCCM 40879 Q5SIM4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.8 HisTrap HP column chromatography Thermus thermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.1.8 0.01
-
wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 0.3
-
mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 0.3
-
mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 0.6
-
mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 0.74
-
wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.4
-
mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.5
-
mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.5
-
mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.5
-
mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.7
-
mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.9
-
mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 1.9
-
mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 2.1
-
mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 2.8
-
mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 3 8 mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 4.5
-
wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 11
-
mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 16
-
mutant enzyme K37A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 31
-
mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 39
-
mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 39
-
mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 40
-
mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 44
-
mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 51
-
mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 58
-
mutant enzyme L18A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 75
-
wild type enzyme, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus
5.3.1.8 194
-
mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.8 D-fructose 6-phosphate
-
Thermus thermophilus D-mannose 6-phosphate
-
r
5.3.1.8 D-fructose 6-phosphate
-
Thermus thermophilus KCCM 40879 D-mannose 6-phosphate
-
r
5.3.1.8 D-Mannose 6-phosphate best substrate Thermus thermophilus D-Fructose 6-phosphate
-
r
5.3.1.8 D-Mannose 6-phosphate best substrate Thermus thermophilus KCCM 40879 D-Fructose 6-phosphate
-
r
5.3.1.8 D-ribose 5-phosphate very low activity Thermus thermophilus D-ribulose 5-phosphate
-
r
5.3.1.8 D-ribose 5-phosphate very low activity Thermus thermophilus KCCM 40879 D-ribulose 5-phosphate
-
r
5.3.1.8 additional information no activity with D-glucose 6-phosphate and arabinose 5-phosphate Thermus thermophilus ?
-
?
5.3.1.8 additional information no activity with D-glucose 6-phosphate and arabinose 5-phosphate Thermus thermophilus KCCM 40879 ?
-
?

Subunits

EC Number Subunits Comment Organism
5.3.1.8 monomer 1 * 29000, SDS-PAGE Thermus thermophilus
5.3.1.8 monomer 1 * 29054, calculated from amino acid sequence Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
5.3.1.8 mannose-6-phosphate isomerase
-
Thermus thermophilus
5.3.1.8 MPI
-
Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.8 80
-
-
Thermus thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.3.1.8 70 90
-
Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.8 64 85 the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.8 11
-
D-mannose 6-phosphate mutant enzyme W13A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 19
-
D-mannose 6-phosphate mutant enzyme E132A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 31
-
D-mannose 6-phosphate mutant enzyme E67A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 37
-
D-mannose 6-phosphate mutant enzyme Q48A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 54
-
D-mannose 6-phosphate mutant enzyme H50A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 70
-
D-mannose 6-phosphate mutant enzyme R142A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 75
-
D-mannose 6-phosphate mutant enzyme H122A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 141
-
D-fructose 6-phosphate wild type enzyme, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 1371
-
D-mannose 6-phosphate wild type enzyme, pH 7.0, 80°C Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.8 7
-
-
Thermus thermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.3.1.8 6.5 8.5
-
Thermus thermophilus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.3.1.8 13
-
D-mannose 6-phosphate mutant enzyme W13A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 54
-
D-mannose 6-phosphate mutant enzyme R142A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 69
-
D-mannose 6-phosphate mutant enzyme Q48A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 109
-
D-mannose 6-phosphate mutant enzyme E132A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 166
-
D-mannose 6-phosphate mutant enzyme H50A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 174
-
D-mannose 6-phosphate mutant enzyme E67A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 278
-
D-mannose 6-phosphate mutant enzyme H122A, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 641
-
D-fructose 6-phosphate wild type enzyme, pH 7.0, 80°C Thermus thermophilus
5.3.1.8 6685
-
D-mannose 6-phosphate wild type enzyme, pH 7.0, 80°C Thermus thermophilus