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| Content Provider | Springer Nature Link |
|---|---|
| Author | Ghannad Sabzevary, A. Hosseini, R. |
| Copyright Year | 2016 |
| Abstract | β-Galactosidases (β-gals) are a wide family of glycosyl hydrolases thought to be involved in the metabolic recycling of galactolipids, glycoproteins, and cell wall polysaccharides in plants. A full-length cDNA, designated STBG2, was isolated and cloned from tomato (Solanum lycopersicum L. cv. Falcato) by reverse transcription–polymerase chain reaction. The cDNA was 2996 bp in length and encoded a typical β-gal protein, designated SlGal2, consisting of 892 residues. A comparison of SlGal2 with its counterpart isoform in the cultivar Rutgers revealed that SlGal2 had identical residues, except for 44 amino acids. Noteworthy, 42 different residues were located in a limited area in the middle of the protein. An alignment of SlGal2 with other plant β-gals clearly showed the existence of a non-conserved short polypeptide, as a connector between the N- and C-terminal domains. A deeper bioinformatic analysis referring to recent experimental findings strongly suggested different roles for the N- and C-terminal domains. As a result, the N-terminal domain is responsible for the catalytic activity and the C-terminal domain is responsible for the stability and the substrate binding of the enzyme. In addition, a substantial difference in physiochemical characteristics of similar β-gals was found to be in their isoelectric points. In conclusion, the differential role of C-terminal domains and also the significant differences in isoelectric points provided insights into the unknown mechanism of substrate specificity of plant β-gals, which in turn will help in protein engineering studies. |
| Starting Page | 522 |
| Ending Page | 531 |
| Page Count | 10 |
| File Format | |
| ISSN | 10681620 |
| Journal | Russian Journal of Bioorganic Chemistry |
| Volume Number | 42 |
| Issue Number | 5 |
| e-ISSN | 1608330X |
| Language | English |
| Publisher | Pleiades Publishing |
| Publisher Date | 2016-09-27 |
| Publisher Place | Moscow |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | RT-PCR lectin protein function sequence annotation Biochemistry Bioorganic Chemistry Organic Chemistry Biomedicine general |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Biochemistry |
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