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

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
27
300-307
2010
Staphylothermus marinus
Manually annotated by BRENDA team