Literature summary for 3.2.1.142 extracted from

Moeller, M.S.; Abou Hachem, M.; Svensson, B.; Henriksen, A.
Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21 (2012), Acta Crystallogr. Sect. F, 68, 1008-1012.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant epression in Pichia pastoris	Hordeum vulgare

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified free enzyme with a glycerol molecule in the active site or purified enzyme in complex with competitive inhibitors alpha- and beta-cyclodextrin, hanging drop vapour diffusion method, streak-seeding, mixing of 10 mg/mlprotein in 50 mM MES buffer pH 6.6, 250 mM NaCl, 0.5 mM CaCl2, 0.67mM maltotriose, with a reservoir solution consisting of 30% w/v PEG 3350, 5% glycerol, 0.3 M NaI, cysteine is added to the crystallization drops to a final concentration of 5-7 mM, one week, 20°C, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, molecular replacement and modelling	Hordeum vulgare

Crystallization (Comment)

Organism

purified free enzyme with a glycerol molecule in the active site or purified enzyme in complex with competitive inhibitors alpha- and beta-cyclodextrin, hanging drop vapour diffusion method, streak-seeding, mixing of 10 mg/mlprotein in 50 mM MES buffer pH 6.6, 250 mM NaCl, 0.5 mM CaCl2, 0.67mM maltotriose, with a reservoir solution consisting of 30% w/v PEG 3350, 5% glycerol, 0.3 M NaI, cysteine is added to the crystallization drops to a final concentration of 5-7 mM, one week, 20°C, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, molecular replacement and modelling

Hordeum vulgare

Inhibitors

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
limit dextrin + H2O	Hordeum vulgare	the enzyme hydrolyses alpha-1,6-glucosidic linkages in limit dextrins derived from amylopectin	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Hordeum vulgare	O48541	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
limit dextrin + H2O	the enzyme hydrolyses alpha-1,6-glucosidic linkages in limit dextrins derived from amylopectin	Hordeum vulgare	?	-	?

Synonyms

Synonyms	Comment	Organism
starch-debranching enzyme	-	Hordeum vulgare

General Information

General Information	Comment	Organism
evolution	the debranching enzyme belongs to the glycoside hydrolase family 13 subfamily 13, GH13_13	Hordeum vulgare