3.2.1.200: exo-chitinase (non-reducing end)
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For detailed information about exo-chitinase (non-reducing end), go to the full flat file.
Reaction
Hydrolysis of N,N'-diacetylchitobiose from the non-reducing end of chitin and chitodextrins =
Synonyms
At4g19810, ChiA, ChiA 65, ChiB, ChiC, chitinase B, GH18 chitinase, TdsC, Tfu0868
ECTree
3.2.1.200 exo-chitinase (non-reducing end)Advanced search results
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Engineering on EC 3.2.1.200 - exo-chitinase (non-reducing end)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D142A
the mutation leads to almost complete loss of enzyme activity
Y214A
the mutation leads to reduced activity compared to the wild type enzyme
Y214F
the mutation leads to reduced activity compared to the wild type enzyme
Y240W
the mutant retains its substrate-binding ability but shows significantly decreased hydrolytic activity against crystalline beta-chitin compared to the wild type enzyme
Y240W/Y481W
the mutant retains its substrate-binding ability but shows significantly decreased hydrolytic activity against crystalline beta-chitin compared to the wild type enzyme
Y481W
the mutant retains its substrate-binding ability and shows wild type hydrolytic activity against crystalline beta-chitin
Y240W
-
the mutant retains its substrate-binding ability but shows significantly decreased hydrolytic activity against crystalline beta-chitin compared to the wild type enzyme
-
Y240W/Y481W
-
the mutant retains its substrate-binding ability but shows significantly decreased hydrolytic activity against crystalline beta-chitin compared to the wild type enzyme
-
Y481W
-
the mutant retains its substrate-binding ability and shows wild type hydrolytic activity against crystalline beta-chitin
-
