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3.2.1.B36: maltose-forming alpha-amylase

This is an abbreviated version!
For detailed information about maltose-forming alpha-amylase, go to the full flat file.

Reaction

An exo-type maltose-forming alpha-amylase alpha-1,4- and alpha-1,6-glucan hydrolytic activity. It acts on the non-reducing end of the substrate and requires at least a G2 unit at its working site =

Synonyms

maltose-forming alpha-amylase, PSMA, Py04_0872, Pyrococcus ST04 alpha-amylase, TCMA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.B36 maltose-forming alpha-amylase

Reference

Reference on EC 3.2.1.B36 - maltose-forming alpha-amylase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jung, J.H.; Seo, D.H.; Holden, J.F.; Park, C.S.
Maltose-forming alpha-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04
Appl. Microbiol. Biotechnol.
98
2121-2131
2014
Pyrococcus sp. (I3RE04), Pyrococcus sp. ST04 (I3RE04)
Manually annotated by BRENDA team
Jeon, E.J.; Jung, J.H.; Seo, D.H.; Jung, D.H.; Holden, J.F.; Park, C.S.
Bioinformatic and biochemical analysis of a novel maltose-forming alpha-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1
Enzyme Microb. Technol.
60
9-15
2014
Thermococcus sp. (I3ZTN9), Thermococcus sp. CL1 (I3ZTN9)
Manually annotated by BRENDA team
Park, K.H.; Jung, J.H.; Park, S.G.; Lee, M.E.; Holden, J.F.; Park, C.S.; Woo, E.J.
Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04
Acta Crystallogr. Sect. D
70
1659-1668
2014
Pyrococcus sp. (I3RE04), Pyrococcus sp. ST04 (I3RE04)
Manually annotated by BRENDA team