Cloned (Comment) | Organism |
---|---|
gene UGlcAE3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time quantitative PCR enzyme expression analysis, recombinant expression in Pichia pastoris strain GS115 in the microsomal fraction. The recombinant OcUGlcAE3 can form a microsomal protein by the N-terminal membrane anchor sequence, or can be secrete into the extracellular space through the guidance of the signal peptide. OcUGlcAE3 can be expressed in Escherichia coli strain Transetta (DE3) only as truncated enzyme with deletion of a putative transmembrane domain of 128 aa in the N-terminus | Albuca bracteata |
Protein Variants | Comment | Organism |
---|---|---|
additional information | deletion of a putative transmembrane domain of 128 aa in the N-terminus, allowing the recombinant expression of a soluble enzyme. Deletion of the conversed GxxGxxG motif in turn results in the activity loss of OcUGlcAE3 | Albuca bracteata |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | membrane-bound | Albuca bracteata | 16020 | - |
microsome | - |
Albuca bracteata | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucuronate | Albuca bracteata | - |
UDP-D-galacturonate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Albuca bracteata | A0A1J0KK43 | i.e. Albuca bracteata | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
bulb | sterile, moderate activity | Albuca bracteata | - |
leaf | low activity | Albuca bracteata | - |
additional information | negligible activity in non-sterile bulbs and flowers | Albuca bracteata | - |
root | UGlcAE3 expression is root-specific, high activity | Albuca bracteata | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucuronate | - |
Albuca bracteata | UDP-D-galacturonate | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 50579, sequence calculation | Albuca bracteata |
Synonyms | Comment | Organism |
---|---|---|
OcUGlcAE3 | - |
Albuca bracteata |
UDP-D-glucuronic acid 4-epimerase | - |
Albuca bracteata |
UGlcAE | - |
Albuca bracteata |
UGlcAE3 | - |
Albuca bracteata |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
optimum 1 | Albuca bracteata |
42 | - |
optimum 2 | Albuca bracteata |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
- |
60 | activity range, M-type temperature profile, overview | Albuca bracteata |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 8.5 | optimum 1 | Albuca bracteata |
10 | - |
optimum 2 | Albuca bracteata |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 11 | activity range, enzyme activity increases gradually with the increase of pH. When pH reaches the range of pH 8-8.5, the enzyme displays the highest activity. With the further increase of pH to about pH 9, the activity of the enzyme decreases slightly. At pH 9-10, the activity of OcUGlcAE3 increases gradually, and reaches the highest activity again at pH value of 10. Above the pH 10.0, the activity decreases, 80% of maximal activity at pH 12.0. M-type pH profile | Albuca bracteata |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | recombinant OcUGlcAE3 does not require exogenous NAD+, suggesting the recombinant OcUGlcAE3 contains tightly bound NAD+ | Albuca bracteata |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Albuca bracteata | sequence calculation | - |
9.77 |
Organism | Comment | Expression |
---|---|---|
Albuca bracteata | OcUGlcAE3 is proposed to be environmentally induced | up |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the UGlcAE family, a subfamily of the the SDR enzyme superfamily. The only three family members are OcUGlcAE1, OcUGlcAE2, and OcUGlcAE3, isolated from Ornithogalum caudatum. Phylogenetic relationships of OcUGlcAE with other UGlcAE, UGE (UDP-D-glucose 4-epimerase) and UXE (UDP-D-xylose 4-epimerase) enzymes are analyzed | Albuca bracteata |
malfunction | deletion of the conversed GxxGxxG motif result in the activity loss of OcUGlcAE3 | Albuca bracteata |
additional information | the N-terminus of UGlcAEs plays important roles in their soluble expression and 4-epimerase activity | Albuca bracteata |
physiological function | UDP-D-glucuronic acid 4-epimerase OcUGlcAE3 is involved in the biosynthesis of root polysaccharides | Albuca bracteata |