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Literature summary for 3.2.1.133 extracted from

  • Park, K.H.; Jung, J.H.; Park, S.G.; Lee, M.E.; Holden, J.F.; Park, C.S.; Woo, E.J.
    Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04 (2014), Acta Crystallogr. Sect. D, 70, 1659-1668.
    View publication on PubMed
Search for more literature for 3.2.1.133

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells Pyrococcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 1.0 M ammonium citrate dibasic, 0.8 M sodium acetate trihydrate pH 4.6 Pyrococcus sp.

Protein Variants

Protein Variants Comment Organism
E580Q strongly reduced activity compared to the wild type enzyme Pyrococcus sp.
F218A the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme Pyrococcus sp.
F452A inactive Pyrococcus sp.
W453A strongly reduced activity compared to the wild type enzyme Pyrococcus sp.

Inhibitors

Inhibitors Comment Organism Structure
acarbose about 80% residual activity at 1 mM Pyrococcus sp.
maltose about 75% residual activity at 1 mM Pyrococcus sp.
additional information not inhibited by panose and isomaltose Pyrococcus sp.

Organism

Organism UniProt Comment Textmining
Pyrococcus sp. I3RE04
-
-
Pyrococcus sp. ST04 I3RE04
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltotriose + H2O
-
 Pyrococcus sp. maltose + D-glucose
-
 ?
maltotriose + H2O
-
 Pyrococcus sp. ST04 maltose + D-glucose
-
 ?
additional information acarbose is not cleaved by the enzyme Pyrococcus sp. ?
-
 ?
additional information the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner Pyrococcus sp. ?
-
 ?
additional information acarbose is not cleaved by the enzyme Pyrococcus sp. ST04 ?
-
 ?
additional information the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner Pyrococcus sp. ST04 ?
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Pyrococcus sp.

Synonyms

Synonyms Comment Organism
maltose-forming alpha-amylase
-
 Pyrococcus sp.