3.2.1.84: glucan 1,3-alpha-glucosidase
This is an abbreviated version!
For detailed information about glucan 1,3-alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.84
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3.2.1.84
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oligosaccharide
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n-linked
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trimming
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monoglucosylated
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glucosyltransferase
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calnexin
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glucosidases
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castanospermine
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deglucosylation
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protein-linked
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mannosidase
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man9glcnac2
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udp-glc:glycoprotein
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udp-glucose:glycoprotein
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glc2man9glcnac2
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prkcsh
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alpha-d-glucopyranoside
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high-mannose-type
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deoxynojirimycin
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hepatocystin
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endomannosidase
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glycoprotein-processing
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endoglucosaminidase
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alpha-1,3-linked
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mannose-type
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bromoconduritol
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unglucosylated
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1-deoxymannojirimycin
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ganab
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biotechnology
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medicine
- 3.2.1.84
- oligosaccharide
-
n-linked
-
trimming
-
monoglucosylated
-
glucosyltransferase
- calnexin
-
glucosidases
- castanospermine
-
deglucosylation
-
protein-linked
-
mannosidase
- man9glcnac2
-
udp-glc:glycoprotein
-
udp-glucose:glycoprotein
- glc2man9glcnac2
- prkcsh
- alpha-d-glucopyranoside
-
high-mannose-type
- deoxynojirimycin
-
hepatocystin
- endomannosidase
-
glycoprotein-processing
-
endoglucosaminidase
-
alpha-1,3-linked
-
mannose-type
- bromoconduritol
-
unglucosylated
- 1-deoxymannojirimycin
- ganab
- biotechnology
- medicine
Reaction
Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans =
Synonyms
alpha-(1->3)-glucanase, exo-1,3-alpha-glucanase, exomutanase, glucosidase II, MalA, mutanase, Mutanase RM1, Saci1160
ECTree
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Source Tissue
Source Tissue on EC 3.2.1.84 - glucan 1,3-alpha-glucosidase
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the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars
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the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars
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the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 10fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars
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the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 10fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars
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