Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants
The alpha-glucan water dikinase (GWD) enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation. The high phosphate content in stored starch has great industrial value, due to its physio–chemical properties making it more versatile, although the phosphate content of...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-08-01
|
| Series: | Plants |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2223-7747/9/9/1101 |
| _version_ | 1797555392327188480 |
|---|---|
| author | Muyiwa S. Adegbaju Olanrewaju B. Morenikeji Eli J. Borrego André O. Hudson Bolaji N. Thomas |
| author_facet | Muyiwa S. Adegbaju Olanrewaju B. Morenikeji Eli J. Borrego André O. Hudson Bolaji N. Thomas |
| author_sort | Muyiwa S. Adegbaju |
| collection | DOAJ |
| description | The alpha-glucan water dikinase (GWD) enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation. The high phosphate content in stored starch has great industrial value, due to its physio–chemical properties making it more versatile, although the phosphate content of stored starch varies depending on the botanical source. In this study, we used various computational approaches to gain insights into the evolution of the GWD protein in 48 plant species with possible roles in enzyme function and alteration of phosphate content in their stored starch. Our analyses identified deleterious mutations, particularly in the highly conserved 5 aromatic amino acid residues in the dual tandem carbohydrate binding modules (CBM-45) of GWD protein in <i>C. zofingiensis</i>, <i>G. hirsutum</i>, <i>A. protothecoides</i>, <i>P. miliaceum</i>, and <i>C. reinhardtii.</i> These findings will inform experimental designs for simultaneous repression of genes coding for GWD and the predicted interacting proteins to elucidate the role this enzyme plays in starch degradation. Our results reveal significant diversity in the evolution of GWD enzyme across plant species, which may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. |
| first_indexed | 2024-03-10T16:46:50Z |
| format | Article |
| id | doaj.art-54f3fd4f111b4d8488e617f755ddb922 |
| institution | Directory Open Access Journal |
| issn | 2223-7747 |
| language | English |
| last_indexed | 2024-03-10T16:46:50Z |
| publishDate | 2020-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Plants |
| spelling | doaj.art-54f3fd4f111b4d8488e617f755ddb9222023-11-20T11:32:17ZengMDPI AGPlants2223-77472020-08-0199110110.3390/plants9091101Differential Evolution of α-Glucan Water Dikinase (GWD) in PlantsMuyiwa S. Adegbaju0Olanrewaju B. Morenikeji1Eli J. Borrego2André O. Hudson3Bolaji N. Thomas4Institute for Plant Biotechnology, Stellenbosch University, Stellenbosch 7600, South AfricaDepartment of Biomedical Sciences, College of Health Science and Technology, Rochester Institute of Technology, Rochester, NY 14623, USAThomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, Rochester, NY 14623, USAThomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, Rochester, NY 14623, USADepartment of Biomedical Sciences, College of Health Science and Technology, Rochester Institute of Technology, Rochester, NY 14623, USAThe alpha-glucan water dikinase (GWD) enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation. The high phosphate content in stored starch has great industrial value, due to its physio–chemical properties making it more versatile, although the phosphate content of stored starch varies depending on the botanical source. In this study, we used various computational approaches to gain insights into the evolution of the GWD protein in 48 plant species with possible roles in enzyme function and alteration of phosphate content in their stored starch. Our analyses identified deleterious mutations, particularly in the highly conserved 5 aromatic amino acid residues in the dual tandem carbohydrate binding modules (CBM-45) of GWD protein in <i>C. zofingiensis</i>, <i>G. hirsutum</i>, <i>A. protothecoides</i>, <i>P. miliaceum</i>, and <i>C. reinhardtii.</i> These findings will inform experimental designs for simultaneous repression of genes coding for GWD and the predicted interacting proteins to elucidate the role this enzyme plays in starch degradation. Our results reveal significant diversity in the evolution of GWD enzyme across plant species, which may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments.https://www.mdpi.com/2223-7747/9/9/1101GWDstarch phosphorylationenzymeevolutionplants |
| spellingShingle | Muyiwa S. Adegbaju Olanrewaju B. Morenikeji Eli J. Borrego André O. Hudson Bolaji N. Thomas Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants Plants GWD starch phosphorylation enzyme evolution plants |
| title | Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants |
| title_full | Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants |
| title_fullStr | Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants |
| title_full_unstemmed | Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants |
| title_short | Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants |
| title_sort | differential evolution of α glucan water dikinase gwd in plants |
| topic | GWD starch phosphorylation enzyme evolution plants |
| url | https://www.mdpi.com/2223-7747/9/9/1101 |
| work_keys_str_mv | AT muyiwasadegbaju differentialevolutionofaglucanwaterdikinasegwdinplants AT olanrewajubmorenikeji differentialevolutionofaglucanwaterdikinasegwdinplants AT elijborrego differentialevolutionofaglucanwaterdikinasegwdinplants AT andreohudson differentialevolutionofaglucanwaterdikinasegwdinplants AT bolajinthomas differentialevolutionofaglucanwaterdikinasegwdinplants |