Cloned (Comment) | Organism |
---|---|
gene CbSqS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli strain M15 | Chlorophytum borivilianum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the aspartate side chains are involved in binding multiple Mg2? ions that stabilize binding of diphosphate groups in the substrate | Chlorophytum borivilianum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
46000 | - |
x * 46000, about, sequence calculation, x * 40000-50000, recombinant enzyme, SDS-PAGE | Chlorophytum borivilianum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlorophytum borivilianum | I6Z427 | gene CbSqS | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Chlorophytum borivilianum | - |
additional information | SqS expression is 14.3% higher in leaves compared to roots, semi-quantitative RT-PCR expression analysis, ovverview. CbSqS shows distinct pattern of expression in leaf and root tissues | Chlorophytum borivilianum | - |
root | - |
Chlorophytum borivilianum | - |
stem | - |
Chlorophytum borivilianum | - |
Subunits | Comment | Organism |
---|---|---|
? | x * 46000, about, sequence calculation, x * 40000-50000, recombinant enzyme, SDS-PAGE | Chlorophytum borivilianum |
More | sequence comparisons with other squalene synthases, analysis of reuired structure motifs, three-dimensional structure model, structure-function relationship, overview | Chlorophytum borivilianum |
Synonyms | Comment | Organism |
---|---|---|
SQS | - |
Chlorophytum borivilianum |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Chlorophytum borivilianum | sequence calculation | - |
6.64 |
General Information | Comment | Organism |
---|---|---|
metabolism | squalene synthase is the key enzyme of saponin biosynthesis pathway | Chlorophytum borivilianum |
additional information | the substrate binding site is present at the core region of the enzyme structure. The predicted active site involves Phe 204, Leu 205, Gln 206, Thr 208, Asn 209, Ala 293, and Leu 297. The aspartate side chains are involved in binding multiple Mg2+ ions that stabilize binding of diphosphate groups in the substrate. | Chlorophytum borivilianum |