3.2.1.2: beta-amylase
This is an abbreviated version!
For detailed information about beta-amylase, go to the full flat file.
Word Map on EC 3.2.1.2
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3.2.1.2
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starch
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alpha-amylase
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maltose
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barley
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potato
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soybean
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sweet
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amylopectin
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amylolytic
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glucoamylase
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endosperm
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hordeum
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amylases
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pullulanase
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debranching
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dextrin
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nutrition
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maltotetraose
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thermosulfurogenes
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isoamylase
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beta-limit
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starch-degrading
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amyloglucosidase
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polymyxa
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maltotriose
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maltopentaose
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granule-bound
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alpha-cyclodextrin
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extrachloroplastic
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industry
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sporamin
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molecular biology
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brewing
- 3.2.1.2
- starch
- alpha-amylase
- maltose
- barley
- potato
- soybean
-
sweet
- amylopectin
-
amylolytic
- glucoamylase
- endosperm
- hordeum
- amylases
- pullulanase
-
debranching
- dextrin
- nutrition
- maltotetraose
- thermosulfurogenes
- isoamylase
-
beta-limit
-
starch-degrading
- amyloglucosidase
- polymyxa
- maltotriose
- maltopentaose
-
granule-bound
- alpha-cyclodextrin
-
extrachloroplastic
- industry
-
sporamin
- molecular biology
- brewing
Reaction
Synonyms
(1-4)-alpha-D-glucan maltohydrolase, 1,4-alpha-D-glucan malto-hydrolase, 1,4-alpha-D-glucan maltohydrolase, 1-4-alpha-glucan maltohydrolase, alpha-1,4-glucan maltohydrolase, amylase, beta-, ARATH, BAM-1, BAM-2, BAM-3, BAM-5, BAM-6, BAM-7, BAM-8, BAM-9, BAM1, BAM3, BAM4, BCB, beta amylase, beta-amylase, beta-amylase 1, beta-amylase I, beta-amylase1, beta-amylase2, beta-amylase8, BMY, Bmy1, Bmy2, Cs-COR018, CT-BMY, glycogenase, More, PF0870, saccharogen amylase, saccharogenamylase, SBA, Sd1, Sd2H, Sd2L, spoII, TCMA, TR-BAMY, type I beta-amylase, type II beta-amylase
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Posttranslational Modification
Posttranslational Modification on EC 3.2.1.2 - beta-amylase
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glycoprotein
no glycoprotein
proteolytic modification
additional information
glycoprotein
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intracellular enzyme contains 0.8% carbohydrate
glycoprotein
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enzyme form F-A contains 9.7% carbohydrate, enzyme form F-B contains 9.3% carbohydrate
no glycoprotein
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extracellular enzyme contains no carbohydrate moiety
beta-amylase undergoes proteolytic cleavage of the C-terminal region after germination, removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity
proteolytic modification
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BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form, the uncleaved enzyme form shows reduced activity
proteolytic modification
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the 60000 Da enzyme form is 3000 Da larger than the mature enzyme from Bacillus circulans, suggesting that processing of the enzyme is different between the two species
apart from the removal of the N-terminal methionine no co- or posttranslational processing
additional information
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apart from the removal of the N-terminal methionine no co- or posttranslational processing