3.2.1.41: pullulanase

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

Reaction

Synonyms

1,4-alpha-D-glucan glucanohydrolase, Alpha-dextrin endo-1,6-alpha-glucosidase, amylase-pullulanase, amylopectin 6-glucanohydrolase, amylopullulanase, AmyX, Apu, ApuK885, ApuM957, Ask, BaPul13A, BDPulA324, BmPul, BNPulA324, CAC60157, debranching enzyme, EC 3.2.1.69, glucanohydrolase, amylopectin 6-, limit dextrinase, More, Nostoc punctiforme debranching enzyme, NPDE, PbPulA, Pcal-1616, PelBsp-PulA, PfAPU, Promozyme 200 L, PUL US105, Pul13A, Pul3YH5, PulA, PulASK, PulB, pulGT, Pullulan 6-glucanohydrolase, pullulan-6-glucanohydrolase, pullulanase, pullulanase type 1, pullulanase type I, pullulanase type II, PulWB42, R-enzyme, Saci_1162, TPApu, TTC1198, TTHpu, type II pullulanase, ZUP1

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.41 pullulanase

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Results	in table
35	Activating Compound
6506	AA Sequence
20	Application
1	CAS Registry Number
38	Cloned(Commentary)
10	Crystallization (Commentary)
1	Expression
7	General Information
2	General Stability
233	Inhibitors
8	kcat/KM [mM/s]
50	KM Value [mM]
45	Localization
89	Metals/Ions
73	Molecular Weight [Da]
97	Natural Substrates/ Products (Substrates)
11	Organic Solvent Stability
437	Organism
2	Pathway
44	PDB ID
72	pH Optimum
36	pH Range
28	pH Stability
8	pI Value
11	Posttranslational Modification
47	Protein Variants
63	Purification (Commentary)
1	Reaction
9	Reaction Type
139	Reference
25	Source Tissue
26	Specific Activity [micromol/min/mg]
2	Storage Stability
410	Substrates and Products (Substrate)
57	Subunits
145	Synonyms
1	Systematic Name
70	Temperature Optimum [°C]
36	Temperature Range [°C]
81	Temperature Stability [°C]
39	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.41 - pullulanase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

X-ray diffraction structure determination and analysis at 1.7 A resolution

Bacillus acidopullulyticus

-

710509

hanging dop method, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 70.568, b = 127.68, c = 189.25 A. The crystal contains two molecules of pullulanase in the asymmetric unit, with a solvent content of 53.15%

Bacillus subtilis

-

663542

in presence of inhibitor beta-cyclodextrin

Fervidobacterium pennivorans

-

654044

ammonium sulfate precipitation

Klebsiella aerogenes

-

136422, 136423

hanging-drop vapor diffusion method. Characterization of the Ins subdomain by X-ray crystallography

Klebsiella pneumoniae

P07206

752281

hanging-drop vapour-diffusion method, crystal structure of pullulanase and its complex with glucose, maltose, isomaltose, maltotriose and maltotetraose, 1.7-1.9 A resolution

Klebsiella pneumoniae

-

666082

purified recombinant enzyme, mixing of 0.0012 ml of 14 mg/ml protein in 50 mM Na-phosphate buffer, pH 7.5, with 0.0012 ml reservoir solution containing 20% w/v PEG 8000, 200 mM Tris-HCl buffer, pH 8.5, and 100 mM MgCl2, X-ray diffraction structure determination and analysis at 2.37 A resolution, molecular structure modelling

Nostoc punctiforme

-

710514

vapour diffusion method

Pyrococcus woesei

-

136434

N-terminal truncated form lacking the carbohydrate binding module, but containing the catalytic domain, in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively

Streptococcus sp.

-

698616