Evolutionary aspects of inorganic pyrophosphatase
| Autor: | Anu Salminen, Reijo Lahti, Pekka Pohjanjoki, Alexey N. Parfenyev, Barry S. Cooperman, Alexander A. Baykov, Adrian Goldman, Toni Sivula |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Evolution Molecular Sequence Data Primary structure Biophysics Gene Biochemistry Protein Structure Secondary Evolution Molecular chemistry.chemical_compound Protein structure Structural Biology Phylogenetics Pyrophosphatase Genetics Animals Humans Amino Acid Sequence Pyrophosphatases Molecular Biology Peptide sequence Phylogeny Plant Proteins Inorganic pyrophosphatase Sequence Homology Amino Acid biology fungi Protein primary structure food and beverages Active site Cell Biology Inorganic Pyrophosphatase chemistry biology.protein |
| Zdroj: | FEBS Letters. 454:75-80 |
| ISSN: | 0014-5793 |
| Popis: | Based on the primary structure, soluble inorganic pyrophosphatases can be divided into two families which exhibit no sequence similarity to each other. Family I, comprising most of the known pyrophosphatase sequences, can be further divided into prokaryotic, plant and animal/fungal pyrophosphatases. Interestingly, plant pyrophosphatases bear a closer similarity to prokaryotic than to animal/fungal pyrophosphatases. Only 17 residues are conserved in all 37 pyrophosphatases of family I and remarkably, 15 of these residues are located at the active site. Subunit interface residues are conserved in animal/fungal but not in prokaryotic pyrophosphatases. |
| Databáze: | OpenAIRE |
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