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Information on EC 3.2.1.1 - alpha-amylase and Organism(s) Haloarcula marismortui and UniProt Accession Q5UZY3

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EC Tree
IUBMB Comments
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
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This record set is specific for:
Haloarcula marismortui
UNIPROT: Q5UZY3
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Word Map
The taxonomic range for the selected organisms is: Haloarcula marismortui
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-amylase, diastase, alpha amylase, pancreatic alpha-amylase, crustacean cardioactive peptide, maltogenic amylase, taka-amylase a, human salivary alpha-amylase, bacillus licheniformis alpha-amylase, alpha-amylase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
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Alpha-amylase carcinoid
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Amy c6
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AMY1
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Amylase THC 250
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amylase, alpha-
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Amylopsin
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Bactosol TK
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Buclamase
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Clarase
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Clone 103
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Clone 168
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Clone PHV19
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Clones GRAMY56 and 963
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diastase
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endoamylase
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Fortizyme
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G 995
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glycogenase
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High pI alpha-amylase
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Isozyme 1B
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Kleistase L 1
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Low pI alpha-amylase
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Maxamyl
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Maxilase
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Meiotic expression upregulated protein 30
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Pancreatic alpha-amylase
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Pivozin
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Ptyalin
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Spitase CP 1
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TAA
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Taka-amylase A
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Takatherm
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Thermamyl
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Thermolase
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucanohydrolase
Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration. The term "alpha" relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-90-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Comput. Aided Mol. Des.
28
721-734
2014
Halalkalicoccus jeotgali (D8J7H2), Haloarcula hispanica (Q4A3E0), Haloarcula marismortui (Q5UZY3), Halalkalicoccus jeotgali DSM 18796 (D8J7H2), Haloarcula marismortui DSM 3752 (Q5UZY3)
Manually annotated by BRENDA team