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3.2.1.68: isoamylase

This is an abbreviated version!
For detailed information about isoamylase, go to the full flat file.

Word Map on EC 3.2.1.68

Reaction

alpha-Glcp-(1-3)-alpha-Glcp-(1-6)-[alpha-Glcp-(1-3)-alpha-Glcp-(1-6)-alpha-Glcp-(1-3)-alpha-Glcp-(1-3)]-alpha-Glcp-(1-3)-alpha-Glcp
+ 2 H2O = 2 alpha-Glcp-(1-3)-alpha-Glcp +
alpha-Glcp-(1-3)-alpha-Glcp-(1-3)-alpha-Glcp-(1-3)-alpha-Glcp

Synonyms

alkaline isoamylase, alpha 1,6-glucan hydrolase, alpha-1,6-glucosidase, ArDBEp, AtISA1, AtISA1/AtISA2 isoamylase, AtISA2, AtISA3, bacterial isoamylase, CrISA1, Cythophaga isoamylase, DBE, DBEI, debranching enzyme, GlgX, glycogen 6-glucanohydrolase, glycogen alpha-1,6-glucanohydrolase, glycogen debranching enzyme, glycogen-6-glucanogydrolase, glycogen-6-glucanohydrolase, glycogen-debranching enzyme, IAM, ISA, ISA1, ISA1-type DBE, ISA2, ISA3, isoamylase, isoamylase 1, isoamylase 2, isoamylase 3, isoamylase II, isoamylase-type debranching enzyme, isoamylase-type starch debranching enzyme 1, isoamylase-type starch debranching enzyme 2, isoamylase-type starch-debranching enzyme, isoamylase1, maize Sugary-1 isoamylase, OsISA1, OsISA2, pancreatic isoamylase isoA, plant isoamylase, potato isoamylase, Pseudomonas isoamylase, PvISA1, PvISA2, PvISA3, rice isoamylase, starch debranching enzyme, SU1 isoamylase, TreX, yeast isoamylase, ZmISA1, ZmISA2

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.68 isoamylase

Engineering

Engineering on EC 3.2.1.68 - isoamylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D367A
site-directed mutagenesis of the catalytic nucleophile Asp-367 in ISA1, the mutation abolishes the catalytic activity of the enzyme complex
G608A
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
G608K
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
G608V
-
the kcat/Km values of the mutant are promoted by 49% and the specific activity increases by 33% as compared to the wild type enzyme
N513A
-
the kcat/Km values of the mutant are slightly decreased and the specific activity is decreased as compared to the wild type enzyme
N513K
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
N513V
-
the kcat/Km values and the specific activity of the mutant are strongly decreased as compared to the wild type enzyme
R505A
-
the kcat/Km values of the mutant are promoted and the specific activity is decreased as compared to the wild type enzyme
R505E
-
the acidic stability is enhanced and the specific activity of the mutant is increased by 13% compared to the wild type enzyme
R505P
-
the thermal stability of the mutant is enhanced compared to the wild type enzyme
G608A
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
-
G608V
-
the kcat/Km values of the mutant are promoted by 49% and the specific activity increases by 33% as compared to the wild type enzyme
-
R505A
-
the kcat/Km values of the mutant are promoted and the specific activity is decreased as compared to the wild type enzyme
-
R505E
-
the acidic stability is enhanced and the specific activity of the mutant is increased by 13% compared to the wild type enzyme
-
R505P
-
the thermal stability of the mutant is enhanced compared to the wild type enzyme
-
additional information