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Literature summary for 3.2.1.1 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

Inhibitors Comment Organism Structure
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]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudoalteromonas haloplanktis
-
a psychrophilic alpha-amylase
-

Reaction

Reaction Comment Organism Reaction ID
(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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Ki Value [mM]

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