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
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sweet
- amylopectin
-
amylolytic
- glucoamylase
- endosperm
- hordeum
- amylases
- pullulanase
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debranching
- dextrin
- nutrition
- maltotetraose
- thermosulfurogenes
- isoamylase
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beta-limit
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starch-degrading
- amyloglucosidase
- polymyxa
- maltotriose
- maltopentaose
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granule-bound
- alpha-cyclodextrin
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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
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 3.2.1.2 - beta-amylase
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REACTION DIAGRAM
starch + H2O
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beta-amylase is an exo-amylase acting on starch with the successive removal of maltose molecules from the non-reducing ends of the glucose polymers with inversion of the anomeric configuration
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starch + H2O
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beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination
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starch + H2O
beta-maltose
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beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant
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starch + H2O
maltose + ?
enzyme induction upon a cold shock at 4°C leads to starch-dependent maltose accumulation, which might be required for protection of the photosynthetic electron transport chain and sensitization of PSII during freezing, maltose influences the carbohydrate metabolism, overview
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starch + H2O
maltose + ?
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role of beta-amylase in starch breakdown during temperature stress, product maltose acts as a cryoprotectant and precursor of soluble sugar metabolism, overview
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starch + H2O
maltose + ?
the isozyme is involved in leaf starch degradation
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starch + H2O
maltose + ?
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in roots during storage, the starch hydrolysis at low temperatures is required for improvement of gustative quality of roots from tuberous-rooted chervil, at higher storage temperature the alpha-amylase activity is increased
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plants mechanism of cold adaptation, enzyme regulation by phytohormones, light, and by abiotic stess, e.g. by osmotic, cold, salt, and drought stress, the enzyme is also regulated by the circadian clock, detailed overview
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additional information
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the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
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additional information
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the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
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additional information
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rhizome beta-amylase is a cytoplasmic vegetative storage protein
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additional information
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rhizome beta-amylase is a cytoplasmic vegetative storage protein
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additional information
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maltose is the main product of soluble starch hydrolysis
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additional information
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maltose is the main product of soluble starch hydrolysis
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additional information
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germination markedly increases the beta-amylase
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additional information
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germination markedly increases the beta-amylase
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