Domain-centric dissection and classification of prokaryotic poly(3-hydroxyalkanoate) synthases
Abstract Although many enzymes and multiple pathways involve in Polyhydroxyalkanoates (PHAs) synthesis, PHA synthases play a determinant role in the process, which include three subunits of PhaC, PhaE, and PhaR. Currently, PHA synthases are categorized into four classes according to its primary sequences, substrate specificity, and subunit composition. However, theoretical analysis of PHA synthases from the domain perspective has not been performed. In this study, we dissected PHA synthases thoroughly through analysis of domain organization. Both referenced bacterial and archaeal proteomes were then screened for the presence and absence of different PHA synthases along NCBI taxonomy ID-based phylogenetic tree. In addition, sequences annotated as bacterial and archaeal PhaCs in UniProt database were also analyzed for domain organizations and interactions. In sum, the in-silico study provided a better understanding of the domain features of PHA synthases in prokaryotes, which also assisted in the production of PHA polymers with optimized chemical properties..
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Preprint| Erscheinungsjahr: |
2019 |
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| Erschienen: |
2019 |
| Enthalten in: |
bioRxiv.org - (2019) vom: 07. Juli Zur Gesamtaufnahme - year:2019 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Liu, Zhanzhong [VerfasserIn] |
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| Links: |
Volltext [kostenfrei] |
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| doi: |
10.1101/693432 |
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| PPN (Katalog-ID): |
XBI000561428 |
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| 245 | 1 | 0 | |a Domain-centric dissection and classification of prokaryotic poly(3-hydroxyalkanoate) synthases |
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| 520 | |a Abstract Although many enzymes and multiple pathways involve in Polyhydroxyalkanoates (PHAs) synthesis, PHA synthases play a determinant role in the process, which include three subunits of PhaC, PhaE, and PhaR. Currently, PHA synthases are categorized into four classes according to its primary sequences, substrate specificity, and subunit composition. However, theoretical analysis of PHA synthases from the domain perspective has not been performed. In this study, we dissected PHA synthases thoroughly through analysis of domain organization. Both referenced bacterial and archaeal proteomes were then screened for the presence and absence of different PHA synthases along NCBI taxonomy ID-based phylogenetic tree. In addition, sequences annotated as bacterial and archaeal PhaCs in UniProt database were also analyzed for domain organizations and interactions. In sum, the in-silico study provided a better understanding of the domain features of PHA synthases in prokaryotes, which also assisted in the production of PHA polymers with optimized chemical properties. | ||
| 700 | 1 | |a Zhu, Zuobin |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Jianye |e verfasserin |4 aut | |
| 700 | 1 | |a Wu, Sheng |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Qinghua |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Mengmeng |e verfasserin |4 aut | |
| 700 | 1 | |a Cheng, Huiling |e verfasserin |4 aut | |
| 700 | 1 | |a Yan, Jiawei |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Liang |e verfasserin |4 aut | |
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