3.5.1.41: chitin deacetylase
This is an abbreviated version!
For detailed information about chitin deacetylase, go to the full flat file.
Word Map on EC 3.5.1.41
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3.5.1.41
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chitosan
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deacetylases
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colletotrichum
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peritrophic
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lindemuthianum
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chitooligosaccharides
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rouxii
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chitosanase
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chitin-binding
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chitinolytic
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n-deacetylated
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acetamido
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synthesis
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absidia
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peritrophin-a
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larval-pupal
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agriculture
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medicine
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drug development
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analysis
- 3.5.1.41
- chitosan
- deacetylases
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colletotrichum
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peritrophic
- lindemuthianum
- chitooligosaccharides
- rouxii
- chitosanase
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chitin-binding
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chitinolytic
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n-deacetylated
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acetamido
- synthesis
- absidia
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peritrophin-a
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larval-pupal
- agriculture
- medicine
- drug development
- analysis
Reaction
Synonyms
AN9380.2, AnCDA, ANIA_09380, ArCE4, Blcda, BmCDA6, BmCDA7, BmCDA8, CDA, CDA-like protein, CDA1, Cda1p, CDA2, cda2aa, cda2b, Cda2p, CDA3, cda4, cda5a, cda5b, cdaYJ, CE4 deacetylase, CHD, chitin amidohydrolase,, chitin deacetylase, chitin deacetylase 1, chitin deacetylase 2, chitin deacetylase 2A, chitin deacetylase 2B, chitin deacetylase 3, chitin deacetylase 4, chitin deacetylase 5A, chitin deacetylase 5B, chitin deacetylase 6, chitin deacetylase 7, chitin deacetylase 8, chitin deacetylase 9, chitin deacetylase RC, chitin deacetylase-like protein, chitin deacetylase2, ChlD, ClCDA, D2 chitin deacetylase, Fpd1, FV-PDA, Hacda2, I3/2 chitin deacetylase, LmCDA1, LmCDA2, LmCDA2a, LmCDA2b, LmCDA4, LmCDA5a, LmCDA5b, midgut chitin deacetylase, More, MrCDA, N-acetylglucosamine deacetylase, NodB, NodB deacetylase, NodB homology domain-containing protein, PaCDA, PcCDA, pc_2566, PesCDA, PgtCDA, PODANS_1_4780, RC chitin deacetylase, ScCDA2, TcCDA1, TcCDA2A, TcCDA2B, TcCDA3, TcCDA4, TcCDA5A, TcCDA5B, TcCDA6, TcCDA7, TcCDA8, TcCDA9, VcCDA, VpCDA
ECTree
3.5.1.41 chitin deacetylaseAdvanced search results
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Source Tissue on EC 3.5.1.41 - chitin deacetylase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
stage-specific expression of TcCDA
tissue specificity of expression of TcCDA gene
tissue specificity of expression of TcCDA gene
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chitin as sole carbon resource of culture medium. The enzyme activity is 10-11 units/ml culture supernatant after the strain is shaken at 200 rpm and 29°C for 96 h
tissue specificity of expression of TcCDA gene
stage-specific expression of TcCDA
tissue specificity of expression of TcCDA gene
stage-specific expression of TcCDA
additional information
optimization of CDA production method and parameters, detailed overview. Total inhibition of CDA production when Ag2+, Co2+, Hg2+, Mn2+ and Ni2+ are added to the medium even at 5 mM concentration
Aspergillus flavus P6B2
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optimization of CDA production method and parameters, detailed overview. Total inhibition of CDA production when Ag2+, Co2+, Hg2+, Mn2+ and Ni2+ are added to the medium even at 5 mM concentration
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enzyme production by submerged fermentation, highest specific activity of 0.018 U/mg protein is obtained after 96 h of cultivation at pH 6 and 28°C
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enzyme production by submerged fermentation, highest specific activity of 0.018 U/mg protein is obtained after 96 h of cultivation at pH 6 and 28°C
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stage-specific expression of TcCDA
tissue specificity of expression of TcCDA gene
tissue specificity of expression of TcCDA gene
5th instar nymph, high expression level especially at the first and second days
the BmCDA7 gene is expressed by the newly hatched silkworm larvae until day seven of the fifth instar and is expressed at a high level in the newly exuviated larvae of different instars
young and mature, stage-specific expression of TcCDA
young and meture, stage-specific expression of TcCDA
tissue specificity of expression of TcCDA gene
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solid-substrate fermentation, wheat bran is used as the substrate
an acellular structure secreted by midgut cells lines the digestive tract in most insects that has important roles in facilitating food digestion and providing protection to the gut epithelium
additional information
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diverse chitinases are inducible dependent on the types of chitin used as growth substrates, chitin deacetylase is best induced by fungal chitin, overview
additional information
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the CDA production in SSF increases 1.79fold in comparison to the unoptimized basal level medium. Optimization of significant parameters affecting CDA production in SSF by response surface methodology (RSM)
additional information
enzyme expression analysis by reverse transcription-PCR, temporal expression profiles and tissue distribution, overview
additional information
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enzyme expression analysis by reverse transcription-PCR, temporal expression profiles and tissue distribution, overview
additional information
the signal is absent or faint in the midgut and larval fat body, tissue- and stage-specific expression of the isozyme, overview
additional information
the signal is absent or faint in the midgut and larval fat body, tissue- and stage-specific expression of the isozyme, overview
additional information
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the signal is absent or faint in the midgut and larval fat body, tissue- and stage-specific expression of the isozyme, overview
additional information
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the enzyme activity is growth phase dependent
additional information
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the enzyme activity is growth phase dependent
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additional information
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the enzyme activity is growth phase dependent
additional information
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the enzyme activity is growth phase dependent
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additional information
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the enzyme activity is growth phase dependent
additional information
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the enzyme activity is growth phase dependent
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additional information
Cunninghamella ramosa URM 1918
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the enzyme activity is growth phase dependent
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additional information
comparion of CDA isozymes expression in different larvae
additional information
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comparion of CDA isozymes expression in different larvae
additional information
both isozymes LmCDA2a and LmCDA2b have the highest expression levels in the foregut, while their expression is low in the other tissues tested. Stage-dependent expression pattern of LmCDA2, mRNA expression levels in the integument at days 1-7 of fifth-instar nymphs are monitored by quantitative RT-PCR expression analysis
additional information
both isozymes LmCDA2a and LmCDA2b have the highest expression levels in the foregut, while their expression is low in the other tissues tested. Stage-dependent expression pattern of LmCDA2, mRNA expression levels in the integument at days 1-7 of fifth-instar nymphs are monitored by quantitative RT-PCR expression analysis
additional information
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both isozymes LmCDA2a and LmCDA2b have the highest expression levels in the foregut, while their expression is low in the other tissues tested. Stage-dependent expression pattern of LmCDA2, mRNA expression levels in the integument at days 1-7 of fifth-instar nymphs are monitored by quantitative RT-PCR expression analysis
additional information
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the highest enzyme activity is observed at 3 days of cultivation, where glucose is added. Powder chitin and swollen chitin also induced the extracellular CDA but in a lesser extent than glucose. Little CDA activity is detected in MeOH addition. The mixtures of glucose plus maltose and glucose plus swollen chitin (1% each) also induce CDA, but the addition of glucose plus swollen chitin delays the maximum induction of enzyme to the 5th day. Enzyme production is maximal at initial pH 4.5-5.0 and decreases dramatically below pH 4.0. About 60% of the maximum CDA production can be achieved at pH 6.0. The optimum temperature is 25-28°C, and less than 60% of the maximum activity was observed at 20°C and 30°C. The optimum agitation speed for enzyme production is 150 rpm
additional information
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the highest enzyme activity is observed at 3 days of cultivation, where glucose is added. Powder chitin and swollen chitin also induced the extracellular CDA but in a lesser extent than glucose. Little CDA activity is detected in MeOH addition. The mixtures of glucose plus maltose and glucose plus swollen chitin (1% each) also induce CDA, but the addition of glucose plus swollen chitin delays the maximum induction of enzyme to the 5th day. Enzyme production is maximal at initial pH 4.5-5.0 and decreases dramatically below pH 4.0. About 60% of the maximum CDA production can be achieved at pH 6.0. The optimum temperature is 25-28°C, and less than 60% of the maximum activity was observed at 20°C and 30°C. The optimum agitation speed for enzyme production is 150 rpm
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additional information
propagation in suspension-cultured rice cells
additional information
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solid state and submerged culture, 10times higher activity in solid state fermentation
additional information
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the enzyme activity is growth phase dependent
