Limits...
In silico study for diversing the molecular pathway of pigment formation: an alternative to manual coloring in cotton fibers.

Ahad A, Ahmad A, Din SU, Rao AQ, Shahid AA, Husnain T - Front Plant Sci (2015)

Bottom Line: Dihydroflavonol 4-reductase (DFR) is a vital enzyme of the flavonoid pathway which displays major impact on the formation of anthocyanins, flavan 3-ols and flavonols.Further, "Expasy ProtParam tool" results showed that Iris × hollandica DFR amino acids (Asn 9: Asp 23) are favorable for reducing DHQ and DHM thus accumulating delphinidin, while Gossypium hirsutum DFR has (Asn 13: Asp 21) hypothesized to consume DHK.It will help in color manipulations in different plant species.

View Article: PubMed Central - PubMed

Affiliation: Center of Excellence in Molecular Biology, University of the Punjab Lahore, Pakistan.

ABSTRACT
Diversity of colors in flowers and fruits is largely due to anthocyanin pigments. The flavonoid/anthocyanin pathway has been most extensively studied. Dihydroflavonol 4-reductase (DFR) is a vital enzyme of the flavonoid pathway which displays major impact on the formation of anthocyanins, flavan 3-ols and flavonols. The substrate specificity of the DFR was found to play a crucial role in determination of type of anthocyanidins. Altering the flavonoid/anthocyanin pathway through genetic engineering to develop color of our own choice is an exciting subject of future research. In the present study, comparison among four DFR genes (Gossypium hirsutum, Iris × hollandica, Ang. DFRI and DFRII), sequence alignment for homology as well as protein modeling and docking is demonstrated. Estimation of catalytic sites, prediction of substrate preference and protein docking were the key features of this article. For specific substrate uptake, a proline rich region and positions 12 plus 26 along with other positions emphasizing the 26-amino acid residue region (132-157) was tested. Results showed that proline rich region position 12, 26, and 132-157 plays an important role in selective attachment of DFRs with respective substrates. Further, "Expasy ProtParam tool" results showed that Iris × hollandica DFR amino acids (Asn 9: Asp 23) are favorable for reducing DHQ and DHM thus accumulating delphinidin, while Gossypium hirsutum DFR has (Asn 13: Asp 21) hypothesized to consume DHK. Protein docking data showed that amino acid residues in above mentioned positions were just involved in attachment of DFR with substrate and had no role in specific substrate uptake. Advanced bioinformatics analysis has revealed that all above mentioned positions have role in substrate attachment. For substrate specificity, other residues region is involved. It will help in color manipulations in different plant species.

No MeSH data available.


Two and three dimensional interaction diagrams of DFR Iris × hollandica with dihydroflavonols. Interaction diagrams were attained by using ligand interaction analysis feature of MOE.
© Copyright Policy
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4584984&req=5

Figure 7: Two and three dimensional interaction diagrams of DFR Iris × hollandica with dihydroflavonols. Interaction diagrams were attained by using ligand interaction analysis feature of MOE.

Mentions: Docking results in case of Iris × hollandica showed that position 130 has Asp as well as Gln in all: DHK, DHQ, and DHM. Additional Glutamine at position 135 also showed attachment with DHK. However, Lys at positions 132 (of Iris × hollandica DFR) has been engaged in DHM and DHQ binding. Ala in position 126 (DHM) and His 218 (DHQ) had an impact on substrate binding (Figure 7).


In silico study for diversing the molecular pathway of pigment formation: an alternative to manual coloring in cotton fibers.

Ahad A, Ahmad A, Din SU, Rao AQ, Shahid AA, Husnain T - Front Plant Sci (2015)

Two and three dimensional interaction diagrams of DFR Iris × hollandica with dihydroflavonols. Interaction diagrams were attained by using ligand interaction analysis feature of MOE.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4584984&req=5

Figure 7: Two and three dimensional interaction diagrams of DFR Iris × hollandica with dihydroflavonols. Interaction diagrams were attained by using ligand interaction analysis feature of MOE.
Mentions: Docking results in case of Iris × hollandica showed that position 130 has Asp as well as Gln in all: DHK, DHQ, and DHM. Additional Glutamine at position 135 also showed attachment with DHK. However, Lys at positions 132 (of Iris × hollandica DFR) has been engaged in DHM and DHQ binding. Ala in position 126 (DHM) and His 218 (DHQ) had an impact on substrate binding (Figure 7).

Bottom Line: Dihydroflavonol 4-reductase (DFR) is a vital enzyme of the flavonoid pathway which displays major impact on the formation of anthocyanins, flavan 3-ols and flavonols.Further, "Expasy ProtParam tool" results showed that Iris × hollandica DFR amino acids (Asn 9: Asp 23) are favorable for reducing DHQ and DHM thus accumulating delphinidin, while Gossypium hirsutum DFR has (Asn 13: Asp 21) hypothesized to consume DHK.It will help in color manipulations in different plant species.

View Article: PubMed Central - PubMed

Affiliation: Center of Excellence in Molecular Biology, University of the Punjab Lahore, Pakistan.

ABSTRACT
Diversity of colors in flowers and fruits is largely due to anthocyanin pigments. The flavonoid/anthocyanin pathway has been most extensively studied. Dihydroflavonol 4-reductase (DFR) is a vital enzyme of the flavonoid pathway which displays major impact on the formation of anthocyanins, flavan 3-ols and flavonols. The substrate specificity of the DFR was found to play a crucial role in determination of type of anthocyanidins. Altering the flavonoid/anthocyanin pathway through genetic engineering to develop color of our own choice is an exciting subject of future research. In the present study, comparison among four DFR genes (Gossypium hirsutum, Iris × hollandica, Ang. DFRI and DFRII), sequence alignment for homology as well as protein modeling and docking is demonstrated. Estimation of catalytic sites, prediction of substrate preference and protein docking were the key features of this article. For specific substrate uptake, a proline rich region and positions 12 plus 26 along with other positions emphasizing the 26-amino acid residue region (132-157) was tested. Results showed that proline rich region position 12, 26, and 132-157 plays an important role in selective attachment of DFRs with respective substrates. Further, "Expasy ProtParam tool" results showed that Iris × hollandica DFR amino acids (Asn 9: Asp 23) are favorable for reducing DHQ and DHM thus accumulating delphinidin, while Gossypium hirsutum DFR has (Asn 13: Asp 21) hypothesized to consume DHK. Protein docking data showed that amino acid residues in above mentioned positions were just involved in attachment of DFR with substrate and had no role in specific substrate uptake. Advanced bioinformatics analysis has revealed that all above mentioned positions have role in substrate attachment. For substrate specificity, other residues region is involved. It will help in color manipulations in different plant species.

No MeSH data available.