3.2.1.54: cyclomaltodextrinase

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

Reaction

Synonyms

AfCda13, AglB, alpha-amylase, alpha-amylase II, CD-/pullulan-hydrolyzing enzyme, CD-ase, CD-degrading enzyme, CD-hydrolyzing amylase, CDA, CDase, CDase I-5, CMD, cyclodextrinase, cycloheptaglucanase, cyclohexaglucanase, cyclomaltodextrin dextrin-hydrolase, Cyclomaltodextrin hydrolase, decycling, cyclomaltodextrinase, CymH, cytoplasmic decycling maltodextrinase, EC 3.2.1.12, Env cda13A, FspCMD, H-17 CDase, H-17 thermostable CDase, LLCD, LsCda13, Lsp26X-Mdase, maltodextrin glucosidase, More, neopullulanase, PFTA, RA.04, thermophilic CDase, TK1770, TVA II

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.54 cyclomaltodextrinase

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Results	in table
12	Activating Compound
531	AA Sequence
17	Application
1	CAS Registry Number
35	Cloned(Commentary)
5	Crystallization (Commentary)
5	General Information
6	General Stability
97	Inhibitors
11	kcat/KM [mM/s]
110	KM Value [mM]
17	Localization
24	Metals/Ions
52	Molecular Weight [Da]
26	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
174	Organism
8	Pathway
17	PDB ID
50	pH Optimum
18	pH Range
12	pH Stability
2	pI Value
23	Protein Variants
45	Purification (Commentary)
23	Reaction
20	Reaction Type
103	Reference
4	Source Tissue
47	Specific Activity [micromol/min/mg]
1	Storage Stability
573	Substrates and Products (Substrate)
86	Subunits
162	Synonyms
1	Systematic Name
56	Temperature Optimum [°C]
19	Temperature Range [°C]
38	Temperature Stability [°C]
59	Turnover Number [1/s]

General Stability

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General Stability on EC 3.2.1.54 - cyclomaltodextrinase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

denaturation and unfolding induced with 2 M guanidine hydrochloride pH 7.0 or 25 mM glycine phosphate buffer, pH 2 for 4 h at 25°C, chaperons GroEL, GroES assist in vivo and in vitro folding of the enzyme, a trans folding mechanism for GroEL/GroES-assisted refolding of MalZ is proposed

Escherichia coli

-

679727

denaturation and unfolding induced with 20 mM sodium phosphate buffer,

Escherichia coli

-

679794

denatured MalZ is enhanced five-fold

Escherichia coli

-

679794

more than 90% of the enzyme activity remains in the pH range of 8.0-10.0 and at 4°C in the absence of CaCl2 after pH and temperature treatments, respectively. Cda is efficiently stabilized by CaCl2. In the presence of CaCl2. Cda is stable in the pH range of 7.0-10.5 and at temperatures below 30°C.

Evansella clarkii

B9A1J7

696419

pH 7.0, 8 M urea and 20 mM dithiothreitol, glycerol, dimethylsulfoxide, trimethylamine-N-oxide, trehalose and proline act as chemical chaperones in the refolding of the denatured MalZ, GroEL, GroES and ATP-mediated refolding of urea

Escherichia coli

-

679794

stable in the presence of up to 2% Triton X-100, completely inactivated in the presence of SDS at concentrations higher than 50 mM

additional information

-

678864