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Literature summary for 2.5.1.21 extracted from

  • Kalra, S.; Kumar, S.; Lakhanpal, N.; Kaur, J.; Singh, K.
    Characterization of Squalene synthase Gene from Chlorophytum borivilianum (Sant. and Fernand.) (2013), Mol. Biotechnol., 54, 944-953.
    View publication on PubMed

Cloned(Commentary)

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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
x * 46000, about, sequence calculation, x * 40000-50000, recombinant enzyme, SDS-PAGE Chlorophytum borivilianum

Organism

Organism UniProt Comment Textmining
Chlorophytum borivilianum I6Z427 gene CbSqS
-

Source Tissue

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

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

Synonyms Comment Organism
SQS
-
Chlorophytum borivilianum

pI Value

Organism Comment pI Value Maximum pI Value
Chlorophytum borivilianum sequence calculation
-
6.64

General Information

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