3.2.1.142: limit dextrinase

This is an abbreviated version!
For detailed information about limit dextrinase, go to the full flat file.

Reaction

Synonyms

Ask, GH13 12-14, HvLD99, limit dextrinase, Pul3YH5, PULI, pullulanase, pullulanase type I, starch-debranching enzyme

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.142 limit dextrinase

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Results	in table
3	Activating Compound
8	AA Sequence
10	Application
1	CAS Registry Number
8	Cloned(Commentary)
4	Crystallization (Commentary)
2	Expression
6	General Information
33	Inhibitors
3	kcat/KM [mM/s]
22	KM Value [mM]
11	Metals/Ions
12	Molecular Weight [Da]
20	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
41	Organism
11	pH Optimum
2	pH Stability
1	pI Value
11	Protein Variants
7	Purification (Commentary)
1	Reaction
1	Reaction Type
39	Reference
12	Source Tissue
6	Specific Activity [micromol/min/mg]
70	Substrates and Products (Substrate)
9	Subunits
14	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
8	Temperature Stability [°C]
7	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.142 - limit dextrinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in complex with its endogenous inhibitor LDI, at 2.7 A resolution. A hydrophobic cluster flanked by ionic interactions in the protein-protein interface is vital for the picomolar affinity of LDI to the enzyme

Hordeum vulgare

O48541

738645

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

-

715920

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

O48541

731074

structures of barley limit dextrinase and active-site mutants in complex with natural substrates, products and substrate analogues. Avoidance of alpha-1,4-hydrolytic activity and strong preference for alpha-1,6-hydrolytic activity seems to be based on the strong interaction to Trp512 and Phe553 on each flank of the catalytic cleft, which will keep non-branched polysaccharides out of the reach of the catalytic nucleophile and acid-base catalyst

Hordeum vulgare

O48541

738874