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Literature summary for 3.2.1.1 extracted from

  • Zorgani, M.A.; Patron, K.; Desvaux, M.
    New insight in the structural features of haloadaptation in alpha-amylases from halophilic Archaea following homology modeling strategy: folded and stable conformation maintained through low hydrophobicity and highly negative charged surface (2014), J. Comput. Aided Mol. Des., 28, 721-734.
    View publication on PubMed

General Stability

General Stability Organism
compared to non-halophilic ones, haloarchaeal alpha-amylases present a different 3D structure organization, to maintain their stability and activity in high salt concentrations. Their structure is characterized by (1) an increase in strategically positioned coil regions, (2) an under-representation of alpha-helix and beta-strand forming regions, (3) highly acidic and negatively charged surface, and (4) the presence of intraprotein interactions such as salt bridges and significantly lower proportion of hydrophobic interactions. In a salty environment, the hydrophobic residues of newly synthesized proteins are exposed to high salt concentrations, leading to non-specific inter- or intramolecular interactions of their side chains, which may compete with proper intramolecular burial within the correct conformation. These features might contribute to avoid aggregation by enabling flexible but stable conformation changes at high salt concentrations Haloarcula hispanica
compared to non-halophilic ones, haloarchaeal alpha-amylases present a different 3D structure organization, to maintain their stability and activity in high salt concentrations. Their structure is characterized by (1) an increase in strategically positioned coil regions, (2) an under-representation of alpha-helix and beta-strand forming regions, (3) highly acidic and negatively charged surface, and (4) the presence of intraprotein interactions such as salt bridges and significantly lower proportion of hydrophobic interactions. In a salty environment, the hydrophobic residues of newly synthesized proteins are exposed to high salt concentrations, leading to non-specific inter- or intramolecular interactions of their side chains, which may compete with proper intramolecular burial within the correct conformation. These features might contribute to avoid aggregation by enabling flexible but stable conformation changes at high salt concentrations Halalkalicoccus jeotgali
compared to non-halophilic ones, haloarchaeal alpha-amylases present a different 3D structure organization, to maintain their stability and activity in high salt concentrations. Their structure is characterized by (1) an increase in strategically positioned coil regions, (2) an under-representation of alpha-helix and beta-strand forming regions, (3) highly acidic and negatively charged surface, and (4) the presence of intraprotein interactions such as salt bridges and significantly lower proportion of hydrophobic interactions. In a salty environment, the hydrophobic residues of newly synthesized proteins are exposed to high salt concentrations, leading to non-specific inter- or intramolecular interactions of their side chains, which may compete with proper intramolecular burial within the correct conformation. These features might contribute to avoid aggregation by enabling flexible but stable conformation changes at high salt concentrations Haloarcula marismortui

Organism

Organism UniProt Comment Textmining
Halalkalicoccus jeotgali D8J7H2
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Halalkalicoccus jeotgali DSM 18796 D8J7H2
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Haloarcula hispanica Q4A3E0
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Haloarcula marismortui Q5UZY3
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Haloarcula marismortui DSM 3752 Q5UZY3
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