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

BRENDA support

Literature summary extracted from

  • Lim, Y.R.; Yeom, S.J.; Oh, D.K.
    Production of L-ribose from L-ribulose by a triple-site variant of mannose-6-phosphate isomerase from Geobacillus thermodenitrificans (2012), Appl. Environ. Microbiol., 78, 3880-3884.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.8 expressed in Escherichia coli ER2566 cells Geobacillus thermodenitrificans

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.8 L129F the activity of the mutant is 204% of the activity of the wild type enzyme Geobacillus thermodenitrificans
5.3.1.8 L129W the activity of the mutant is 10% of the activity of the wild type enzyme Geobacillus thermodenitrificans
5.3.1.8 L129Y the activity of the mutant is 94% of the activity of the wild type enzyme Geobacillus thermodenitrificans
5.3.1.8 N90A/L129F the activity of the mutant is about 6fold higher than the activity of the wild type enzyme Geobacillus thermodenitrificans
5.3.1.8 W17Q/N90A/L129F the specific activity and catalytic efficiency for L-ribulose isomerization of this variant are 3.1 and 7.1fold higher, respectively, than those of the wild type enzyme at pH 7.0 and 70°C in the presence of 1mM Co2+ Geobacillus thermodenitrificans

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.8 EDTA
-
 Geobacillus thermodenitrificans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.8 8 9 D-mannose 6-phosphate mutant enzyme N90A/L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 100
-
 D-mannose 6-phosphate mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 149
-
 D-mannose 6-phosphate wild type enzyme, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 243
-
 D-mannose 6-phosphate mutant enzyme L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.8 Co2+ strong stimulation of activity Geobacillus thermodenitrificans
5.3.1.8 Cu2+ significantly stimulated by Cu2+ Geobacillus thermodenitrificans
5.3.1.8 Mn2+ significantly stimulated by Mn2+ Geobacillus thermodenitrificans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.1.8 D-Mannose 6-phosphate Geobacillus thermodenitrificans
-
 D-Fructose 6-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.8 Geobacillus thermodenitrificans A4ITT1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.8 D-Mannose 6-phosphate
-
 Geobacillus thermodenitrificans D-Fructose 6-phosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.8 23550
-
 D-mannose 6-phosphate wild type enzyme, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 55120
-
 D-mannose 6-phosphate mutant enzyme L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 85720
-
 D-mannose 6-phosphate mutant enzyme N90A/L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 112100
-
 D-mannose 6-phosphate mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.3.1.8 158
-
 D-mannose 6-phosphate wild type enzyme, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 227
-
 D-mannose 6-phosphate mutant enzyme L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 965
-
 D-mannose 6-phosphate mutant enzyme N90A/L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans
5.3.1.8 1120
-
 D-mannose 6-phosphate mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C Geobacillus thermodenitrificans