3.2.1.133: glucan 1,4-alpha-maltohydrolase

This is an abbreviated version!
For detailed information about glucan 1,4-alpha-maltohydrolase, go to the full flat file.

Reaction

Synonyms

alpha-amylase, AmyB, BbmA, BSMA, BSTA, BTMA, CAZy-GH13, glucan 1,4-alpha-maltohydrolase, glucan-1,4-alpha-maltohydrolase, Gt-MamyIII, LGMA, MAase, MABS, MAG1, maltogenase L, maltogenic alpha-amylase, maltogenic amylase, maltose-forming alpha-amylase, MAmy, MAUS149, More, NM319, NM326, NM398, NM404, NM447, Novamyl, PSMA, Smar_0613, SMMA, TCMA, Thermus maltogenic amylase, ThMA, TK4MA

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.133 glucan 1,4-alpha-maltohydrolase

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Results	in table
8	Activating Compound
70	AA Sequence
35	Application
1	CAS Registry Number
36	Cloned(Commentary)
7	Crystallization (Commentary)
3	General Information
3	General Stability
69	Inhibitors
15	kcat/KM [mM/s]
1	Ki Value [mM]
57	KM Value [mM]
13	Localization
22	Metals/Ions
39	Molecular Weight [Da]
34	Natural Substrates/ Products (Substrates)
6	Organic Solvent Stability
106	Organism
5	Pathway
4	PDB ID
22	pH Optimum
12	pH Range
6	pH Stability
1	pI Value
95	Protein Variants
32	Purification (Commentary)
1	Reaction
7	Reaction Type
83	Reference
3	Source Tissue
48	Specific Activity [micromol/min/mg]
253	Substrates and Products (Substrate)
49	Subunits
134	Synonyms
1	Systematic Name
40	Temperature Optimum [°C]
15	Temperature Range [°C]
39	Temperature Stability [°C]
88	Turnover Number [1/s]

General Stability

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General Stability on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

at atmospheric pressure the enzyme is unstable at 60 and 70°C, while under negative pressure (_-200 mbar) the enzyme shows its activity on the starch at up to 70°C

Aspergillus niger

-

732920

stable in presence of 1 mM Ca2+

Geobacillus sp. SK70

-

750727

the highest thermostability of the enzyme among bacterial maltogenic amylases is attributed to the presence of four salt bridges. Among four salt bridges, the key structural determinants that govern its thermostabilization are intra-chain cross-domain, buried and networked salt bridges

Geobacillus thermoleovorans

I6RE37

750819