3.2.1.B8: malto-alpha-amylase (reducing end)

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For detailed information about malto-alpha-amylase (reducing end), go to the full flat file.

Reaction

hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains =

Synonyms

cyclodextrinase, MAase, maltogenic amylase, MalZ, More, SMMA, TMG, YvdF

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.B8 malto-alpha-amylase (reducing end)

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Results	in table
1	AA Sequence
1	Application
4	Cloned(Commentary)
7	Inhibitors
7	kcat/KM [mM/s]
7	KM Value [mM]
4	Localization
3	Molecular Weight [Da]
21	Natural Substrates/ Products (Substrates)
105	Organism
2	Pathway
2	pH Optimum
2	pH Range
1	pH Stability
3	Protein Variants
2	Purification (Commentary)
2	Reaction
5	Reference
5	Specific Activity [micromol/min/mg]
40	Substrates and Products (Substrate)
2	Subunits
13	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
2	Temperature Range [°C]
3	Temperature Stability [°C]
7	Turnover Number [1/s]

Temperature Stability

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Temperature Stability on EC 3.2.1.B8 - malto-alpha-amylase (reducing end)

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

100 - 109

Staphylothermus marinus

-

the enzyme is extremely thermostable, with a temperature optimum of 100°C and a melting temperature of 109°C

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20 - 130

Staphylothermus marinus

-

differential scanning calorimetric analysis of SMMA, profile, overview

710128

additional information

Staphylothermus marinus

-

in SMMA, non-polar side chains at 357W, 408W, 449Y, 451W, 463Y, 490Y, 501Y, 517Y 519Y, 529Y, 593W, and 608Y are located at the termini of alpha-helixes and beta-sheets contributing to the extreme thermostability of the enzyme

710128