The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein
| Autor: | Sabrina Castellano, Augusto Parente, Maria Rosaria Faraone-Mennella, Anna De Maio, Benedetta Farina, Antimo Di Maro |
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| Přispěvatelé: | DI MARO, Antimo, DE MAIO, A, Castellano, S, Parente, A, Farina, B, FARAONE MENNELLA, Mr, Di Maro, A, DE MAIO, Anna, FARAONE MENNELLA, MARIA ROSARIA |
| Rok vydání: | 2008 |
| Předmět: |
Archaeal Proteins
Poly ADP ribose polymerase Amino Acid Motifs Molecular Sequence Data Clinical Biochemistry ved/biology.organism_classification_rank.species Biochemistry Edman degradation Humans Amino Acid Sequence Molecular Biology Peptide sequence Conserved Sequence Sequence (medicine) chemistry.chemical_classification Poly(ADP-ribose) polymerase ved/biology DING protein Thermoprotein Sulfolobus solfataricus Tryptic peptide Sulfolobus solfataricu Adenosine Diphosphate Enzyme chemistry Archaeon Poly(ADP-ribose) Polymerases Sequence Alignment |
| Zdroj: | bchm. 390:27-30 |
| ISSN: | 1437-4315 1431-6730 |
| DOI: | 10.1515/bc.2009.006 |
| Popis: | The partial amino acid sequence of the sulfolobal thermoprotein biochemically characterized as poly(ADP-ribose)polymerase-like enzyme overlaps those of DING proteins. This group of proteins, widely occurring in animals, plants and eubacteria, shows a characteristic and highly conserved N-terminus, DINGGGATL. The sequence of the N-terminal region and of the analyzed tryptic peptides of the sulfolobal thermozyme shows a high similarity with most of the DING proteins from databases. This is the first example of a DING protein from a sulfolobal source. |
| Databáze: | OpenAIRE |
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