Literature summary for 3.2.1.142 extracted from

Vester-Christensen, M.B.; Abou Hachem, M.; Svensson, B.; Henriksen, A.
Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins (2010), J. Mol. Biol., 403, 739-750.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Pichia pastoris	Hordeum vulgare

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with the competitive inhibitor beta-cyclodextrin, hanging drop vapor diffusion method, with streak seeding in a reservoir solution of 22% (w/v) PEG 3350, 5% (v/v) Gol, and 0.3 M NaI, or without seeding in a reservoir solution of 30% (w/v) PEG 3350, 10% (v/v) Gol, and 0.3 M NaI. In complex with the competitive inhibitor alpha-cyclodextrin, hanging drop vapor diffusion method, without seeding in a reservoir solution of 30% (w/v) PEG 3350 and 0.3 M NaI	Hordeum vulgare

Crystallization (Comment)

Organism

in complex with the competitive inhibitor beta-cyclodextrin, hanging drop vapor diffusion method, with streak seeding in a reservoir solution of 22% (w/v) PEG 3350, 5% (v/v) Gol, and 0.3 M NaI, or without seeding in a reservoir solution of 30% (w/v) PEG 3350, 10% (v/v) Gol, and 0.3 M NaI. In complex with the competitive inhibitor alpha-cyclodextrin, hanging drop vapor diffusion method, without seeding in a reservoir solution of 30% (w/v) PEG 3350 and 0.3 M NaI

Hordeum vulgare

Inhibitors

Inhibitors	Comment	Organism	Structure
alpha-cyclodextrin	competitive inhibitor	Hordeum vulgare
beta-cyclodextrin	competitive inhibitor	Hordeum vulgare

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	contains Ca2+	Hordeum vulgare

Organism

Organism	UniProt	Comment	Textmining
Hordeum vulgare	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
limit dextrins + H2O	limit dextrinase catalyzes the hydrolysis of alpha-1,6 glucosidic linkages in limit dextrins	Hordeum vulgare	?	-	?
additional information	the enzyme has low activity towards amylopectin	Hordeum vulgare	?	-	?
pullulan + H2O	-	Hordeum vulgare	?	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
78	-	pullulan	pH and temperature not specified in the publication	Hordeum vulgare

General Information

General Information	Comment	Organism
physiological function	limit dextrinase activity plays a role in starch degradation during germination and in starch biosynthesis during grain filling	Hordeum vulgare