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Literature summary for 5.3.1.4 extracted from

  • Kim, J.H.; Prabhu, P.; Jeya, M.; Tiwari, M.K.; Moon, H.J.; Singh, R.K.; Lee, J.K.
    Characterization of an L-arabinose isomerase from Bacillus subtilis (2010), Appl. Microbiol. Biotechnol., 85, 1839-1847.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene araA, DNA and amino acid sequence determination and analysis, His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
E305A site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme Bacillus subtilis
E305A site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme Bacillus subtilis
E330A site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme Bacillus subtilis
E330A site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme Bacillus subtilis
H347A site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme Bacillus subtilis
H446A site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required, 42% activation at 1 mM Bacillus subtilis
additional information the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
2 * 56000, recombinant His6-tagged wild-type enzyme, SDS-PAGE Bacillus subtilis
115000
-
recombinant His6-tagged wild-type enzyme, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arabinose Bacillus subtilis L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways L-ribulose
-
r
L-arabinose Bacillus subtilis L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways L-ribulose
-
r
L-arabinose Bacillus subtilis 168 L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways L-ribulose
-
r
L-arabinose Bacillus subtilis 168 L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways L-ribulose
-
r
L-ribulose Bacillus subtilis L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways L-arabinose
-
r
L-ribulose Bacillus subtilis 168 L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways L-arabinose
-
r

Organism

Organism UniProt Comment Textmining
Bacillus subtilis C7F8M0 gene araA
-
Bacillus subtilis 168 C7F8M0 gene araA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
262
-
purified recombinant enzyme Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aldose
-
Bacillus subtilis ?
-
?
L-arabinose L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways Bacillus subtilis L-ribulose
-
r
L-arabinose the enzyme shows high substrate specificity Bacillus subtilis L-ribulose
-
r
L-arabinose L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways Bacillus subtilis L-ribulose
-
r
L-arabinose L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways Bacillus subtilis 168 L-ribulose
-
r
L-arabinose the enzyme shows high substrate specificity Bacillus subtilis 168 L-ribulose
-
r
L-arabinose L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways Bacillus subtilis 168 L-ribulose
-
r
L-ribulose L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways Bacillus subtilis L-arabinose
-
r
L-ribulose L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways Bacillus subtilis 168 L-arabinose
-
r
additional information no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview Bacillus subtilis ?
-
?
additional information no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview Bacillus subtilis 168 ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 56000, recombinant His6-tagged wild-type enzyme, SDS-PAGE Bacillus subtilis
More wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview Bacillus subtilis

Synonyms

Synonyms Comment Organism
L-AI
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
32
-
-
Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
241.7
-
L-ribulose pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme Bacillus subtilis
241.7
-
L-aldose pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
6 9 31%, 68%, 87%, and 48% of maximum activity at pH 6.0, pH 7.0, pH 8.0, and pH 9.0, respectively Bacillus subtilis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus subtilis isoelectric focusing
-
4.9

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.02
-
L-ribulose pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme Bacillus subtilis
2.02
-
L-aldose pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme Bacillus subtilis