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Literature summary extracted from

  • D'Amico, S.; Sohier, J.S.; Feller, G.
    Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic alpha-amylase (2006), J. Mol. Biol., 358, 1296-1304.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 maltose product inhibition, the active site able to accomodate larger inhibitory complxes, resulting in a mixed type inhibition of starch hydrolysis Pseudoalteromonas haloplanktis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information isothermal titration and microcalorimetric analysis, thermodynamics and kinetics Pseudoalteromonas haloplanktis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 chloride is a weak allosteric enzyme activator Pseudoalteromonas haloplanktis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.1 2 starch + H2O Pseudoalteromonas haloplanktis
-
 2 malto-oligosaccharides + maltose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Pseudoalteromonas haloplanktis
-
 a psychrophilic alpha-amylase
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.1 (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose active site mobility and structure of the psychrophilic alpha-amylase, ligand binding mechanism and conformational changes, side chains involved in substrate binding are strictly conserved, overview Pseudoalteromonas haloplanktis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 2 starch + H2O
-
 Pseudoalteromonas haloplanktis 2 malto-oligosaccharides + maltose
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 cold-active, psychrophilic alpha-amylase Pseudoalteromonas haloplanktis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.1 additional information
-
 additional information inhibition kinetics Pseudoalteromonas haloplanktis