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]

Reference

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

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707349

Lee, M.; Kim, Y.-W.; Kim, T.-J.; Park, C.-S.; Kim, J.-W.; Moon, T.-W.; Park, K.-H.

A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates

Biochem. Biophys. Res. Commun.

295

818-825

2002

Thermotoga maritima MSB8 (Q9X2F4)

12127967

708926

Shim, J.H.; Park, J.T.; Hong, J.S.; Kim, K.W.; Kim, M.J.; Auh, J.H.; Kim, Y.W.; Park, C.S.; Boos, W.; Kim, J.W.; Park, K.H.

Role of maltogenic amylase and pullulanase in maltodextrin and glycogen metabolism of Bacillus subtilis 168

J. Bacteriol.

191

4835-4844

2009

Bacillus subtilis, Escherichia coli K-12, Bacillus subtilis 168

19465663

710128

Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.

Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinus

New Biotechnol.

300-307

2010

Staphylothermus marinus

20385261