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Literature summary extracted from

  • Patel, D.; Wi, S.; Lee, S.; Lee, D.; Song, Y.; Bae, H.
    Substrate specificity of the Bacillus licheniformis lyxose isomerase YdaE and its application in in vitro catalysis for bioproduction of lyxose and glucose by two-step isomerization (2011), Appl. Environ. Microbiol., 77, 3343-3350.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.15 expressed in Escherichia coli BL21(DE3) cells Bacillus licheniformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.15 26
-
 D-mannose in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis
5.3.1.15 30.4
-
 D-Lyxose in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.15 Co2+ about 40% activity in the presence of 1 mM Co2+ as compared to Mn2+ Bacillus licheniformis
5.3.1.15 Mg2+ about 50% activity in the presence of 1 mM Mg2+ as compared to Mn2+ Bacillus licheniformis
5.3.1.15 Mn2+ highest activity (100%) in the presence of 1.0 mM Mn2+ Bacillus licheniformis
5.3.1.15 additional information not activated by Zn2+, Cu2+, and Ni2+ Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.15 19500
-
 x * 19500, estimated from SDS-PAGE Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.15 Bacillus licheniformis Q65N98
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.15 Ni-NTA agarose bead column chromatography and ultrafiltration Bacillus licheniformis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.3.1.15 4.2
-
 crude extract, in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis
5.3.1.15 24
-
 after 10fold purification, in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.15 D-Lyxose
-
 Bacillus licheniformis D-Xylulose
-
 r
5.3.1.15 D-Mannose
-
 Bacillus licheniformis ?
-
 ?
5.3.1.15 additional information no activity with D-glucose, D-xylose, L-arabinose, and L-rhamnose Bacillus licheniformis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.1.15 ? x * 19500, estimated from SDS-PAGE Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
5.3.1.15 D-Lyxose isomerase
-
 Bacillus licheniformis
5.3.1.15 YdaE
-
 Bacillus licheniformis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.3.1.15 40 65 the enzyme activity increases as the temperature increases, showing higher activity at 40°C to 45°C, and is completely lost at temperatures greater than 65°C Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.15 30 50 the enzyme shows half-lives of 140 h, 62 h, 30 h, 18 h, and 7 h at 30°C, 35°C, 40°C, 45°C, and 50°C, respectively Bacillus licheniformis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.15 43
-
 D-mannose in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis
5.3.1.15 98
-
 D-Lyxose in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.15 7.5 8
-
 Bacillus licheniformis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.3.1.15 1.6
-
 D-mannose in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis
5.3.1.15 3.2
-
 D-Lyxose in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C Bacillus licheniformis