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Query: UNIPROT:P06889 (Mol)
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Nod factors excreted by rhizobia are signal molecules that consist of a chitin oligomer backbone linked with a fatty acid at the nonreducing end. Modifications of the Nod factor structures influence their stability in the rhizosphere and their biological activity. To test the function of N-acetyl groups in Nod factors, NodSm-IV(C16:2,S) from Sinorhizobium meliloti was enzymatically N-deacetylated in vitro with purified chitin deacetylase from Colletotrichum lindemuthianum. A family of partially and completely deacetylated derivatives was produced and purified. The most abundant chemical structures identified by mass spectrometry were GlcN(C16:2)-GlcNAc-GlcNH2-GlcNAc(OH)(S), GlcN(C16,2)-GlcNAc-GlcNH2-GlcNH2(OH)(S), and GlcN(C16:2)-GlcNH2-GlcNH2-GlcNH2(OH)(S). In contrast to NodSm-IV(C16:2,S), the purified N-deacetylated derivatives were stable in the rhizosphere of Medicago sativa, indicating that the N-acetyl groups make the carbohydrate moiety of Nod factors accessible for glycosyl hydrolases of the host plant. The N-deacetylated derivatives displayed only a low level of activity in inducing root hair deformation. Furthermore, the N-deacetylated molecules were not able to stimulate Nod factor degradation by M. sativa roots, a response elicited by active Nod factors. These data show that N-acetyl groups of Nod factors are required for biological activity.
Mol Plant Microbe Interact 2000 Jan
PMID:N-deacetylation of Sinorhizobium meliloti Nod factors increases their stability in the Medicago sativa rhizosphere and decreases their biological activity. 1065 87

Chitinase and chitindeacetylase are enzymes capable of degrading chitin into chitooligomers and chitosan. The chitinases characterized and purified in this study were extracted from the acidophillic Bacillus sp. isolated from Kamojang Crater West Java Indonesia. When grown in liquid media containing colloidal chitin, the optimum chitinase activity of the acidophilic isolate was reached after 4-5 days of incubation. The optimum temperature and pH of the chitinase and chitin deacetylase were found at 37 degrees C and pH 5. When incubated at pH 5, the activity of chitin deacetylase was increased; after 3 h, the activity was 1.5 times of the control. The enzyme was stable at pH 4, after 2 h incubation, the activity was still 80% of the control. The chitinase and chitin deacetylase activities were not influenced by Mg(++) nor Ca(++), Ni(++) and Cu(++) inhibited the chitinase activity, while chitin deacetylase activity was not affected by Cu(++) addition. When 1 mM of EDTA was added, the enzyme activity was reduced 40 to 50%.
J Biochem Mol Biol Biophys 2002 Aug
PMID:Biochemical characteristics of chitinase enzyme from Bacillus sp. of Kamojang Crater, Indonesia. 1218 45

A novel midgut peritrophic membrane (PM) protein, TnPM-P42, was identified from the cabbage looper, Trichoplusia ni. TnPM-P42 was shown as a 42kDa protein by SDS-PAGE analysis and appeared to be associated with the PM throughout its entire length. In T. ni larvae, the midgut is the only tissue where TnPM-P42 could be detected during the feeding period of the larvae. TnPM-P42 has chitin-binding activity and is strongly associated with the PM, which is similar to the currently known peritrophin type PM proteins. However, TnPM-P42 represents a unique family of proteins distinctly different from the peritrophin type PM proteins in its sequence characteristics. TnPM-P42 does not contain the peritrophin domain which is present in all the currently known PM proteins, but instead has a chitin deacetylase-like domain. Sequence similarity search of the GenBank database did not result in identification of any known proteins with a significant overall sequence similarity to the TnPM-P42. However, expressed sequence tags (ESTs) from various arthropods were identified to code for proteins with high sequence similarities to TnPM-P42, indicating the presence of TnPM-P42 homologs in other arthropods. Consistent with the identification of various ESTs from arthropods, Western blot analysis demonstrated the presence of a TnPM-P42-like protein in the PMs from Heliothis virescens and Helicoverpa zea larvae. The sequence characteristics of TnPM-P42 indicate that TnPM-P42 represents a novel family of insect proteins. However, its biochemical and physiological functions require further investigation.
Insect Biochem Mol Biol 2005 Nov
PMID:A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni. 1620 4

The cyst wall of Entamoeba invadens (Ei), a model for the human pathogen Entamoeba histolytica, contains chitin, which is a homopolymer of beta-1, 4-linked N-acetyl-glucosamine (GlcNAc). In fungi and in bacteria that make nodulation factors, chitin deacetylases make chitosan, which is a mixture of GlcNAc and glucosamine and so has a positive charge. The activity of an Ei chitin deacetylase was revealed by a 3-4-fold increase in released GlcNAc when deproteinated cyst walls were chemically acetylated prior to treatment with a commerical chitinase. Because this chitinase releases GlcNAc but not GlcN, increases in released GlcNAc after acetylation suggested the presence of chitosan in Ei cyst walls. Five putative Ei and Eh chitin deacetylase genes resembled those of fungi and bacteria. A predicted Eh chitin deacetylase matched closely the three-dimensional structure of a Bacillus subtilis peptiodglycan deacetylase. A recombinant Eh chitin deacetylase, expressed in Saccharomyces cerevisiae, deacetylated chitooligosaccharides in vitro. These results are consistent with the idea that Ei chitin deacetylases modify chitin to produce chitosan in the Ei cyst wall.
Mol Biochem Parasitol 2006 Jul
PMID:The cyst wall of Entamoeba invadens contains chitosan (deacetylated chitin). 1662 Oct 70

A bioinformatics investigation of four insect species with annotated genome sequences identified a family of genes encoding chitin deacetylase (CDA)-like proteins, with five to nine members depending on the species. CDAs (EC 3.5.1.41) are chitin-modifying enzymes that deacetylate the beta-1,4-linked N-acetylglucosamine homopolymer. Partial deacetylation forms a heteropolysaccharide that also contains some glucosamine residues, while complete deacetylation produces the homopolymer chitosan, consisting exclusively of glucosamine. The genomes of the red flour beetle, Tribolium castaneum, the fruit fly, Drosophila melanogaster, the malaria mosquito, Anopheles gambiae, and the honey bee, Apis mellifera contain 9, 6, 5 and 5 genes, respectively, that encode proteins with a chitin deacetylase motif. The presence of alternative exons in two of the genes, TcCDA2 and TcCDA5, increases the protein diversity further. Insect CDA-like proteins were classified into five orthologous groups based on phylogenetic analysis and the presence of additional motifs. Group I enzymes include CDA1 and isoforms of CDA2, each containing in addition to a polysaccharide deacetylase-like catalytic domain, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa). Group II is composed of CDA3 orthologs from each insect species with the same domain organization as group I CDAs, but differing substantially in sequence. Group III includes CDA4s, which have the ChBD domain but do not have the LDLa domain. Group IV comprises CDA5s, which are the largest CDAs because of a very long intervening region separating the ChBD and catalytic domains. Among the four insect species, Tribolium is unique in having four CDA genes in group V, whereas the other insect genomes have either one or none. Most of the CDA-like proteins have a putative signal peptide consistent with their role in modifying extracellular chitin in both cuticle and peritrophic membrane during morphogenesis and molting.
Insect Biochem Mol Biol 2008 Apr
PMID:Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects. 1834 49

The peritrophic matrix from the midgut of the caterpillar, Helicovera armigera, was solubilized by treatment with anhydrous trifluoromethanesulfonic acid, apparently by depolymerisation of its chitin component. This allowed the efficient extraction of proteins in a technique that may be broadly applicable to the analysis of other structures containing chitin. Gel electrophoresis and mass spectrometry of tryptic peptides were used to identify the extracted proteins with gut-expressed cDNA sequences. The major proteins of this cohesive, digestion-resistant structure are chitin deacetylase-like and mucin-like proteins, the latter with multiple chitin-binding domains that may cross-link chitin fibrils to provide a barrier against abrasive food particles and parasites, one of the major functions of the matrix. Other proteins found in the H. armigera gut peritrophic matrix suggest that the matrix is a dynamic, complex structure that may participate in the immobilization of digestive enzymes, actively protect the gut from parasite invasion and intercept toxins such as lectins and Bacillus thuringiensis crystal proteins.
Insect Biochem Mol Biol 2008 Oct
PMID:Proteomic analysis of the peritrophic matrix from the gut of the caterpillar, Helicoverpa armigera. 1876 Mar 62

One- and two-dimensional gel electrophoresis coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify cDNA encoding a chitin deacetylase (McCDA1) and three insect intestinal lipases (McIIL1, McIIL2 and McIIL3) associated with the Mamestra configurata (bertha armyworm) peritrophic matrix. Recombinant McCDA1 was active and chitin deacetylase activities were detected in the midgut. McCDA1 and the McIIL genes were expressed exclusively in the midgut; however, McCDA1 and McIIL2 were expressed in all larval stages, whereas McIIL1 was expressed mainly in feeding larvae and McIIL3 primarily during the moult.
Insect Mol Biol 2008 Sep
PMID:A chitin deacetylase and putative insect intestinal lipases are components of the Mamestra configurata (Lepidoptera: Noctuidae) peritrophic matrix. 1882 43

The expression profiles of nine genes encoding chitin deacetylase (CDA)-like proteins were studied during development and in various tissues of the red flour beetle, Tribolium castaneum, by RT-PCR. TcCDA1, TcCDA2 and TcCDA5 were expressed throughout all stages of development, while TcCDA6-9 were expressed predominantly during larval feeding stages. In situ hybridization experiments revealed that both TcCDA1 and TcCDA2 were expressed in epidermal cells. Polyclonal antibody to TcCDA1 detected an immunoreactive protein in larval tracheae. TcCDA6 through TcCDA9, which belong to a distinct subgroup of gut-specific CDAs, were transcribed in the cells lining the midgut, including epithelial cells. TcCDA3 was expressed in the thoracic muscles, whereas TcCDA4 was expressed in early imaginal appendages. To study the function(s) of individual TcCDA genes, double-stranded RNAs (dsRNA) specific for each gene were injected into insects at different developmental stages and the phenotypes were monitored. No visible phenotypic changes were observed after injection of dsRNAs for TcCDA3 to 9, whereas injection of dsRNAs for TcCDA1 or TcCDA2 affected all types of molts, including larval-larval, larval-pupal and pupal-adult. Insects treated with these dsRNAs could not shed the old cuticle and were trapped in their exuviae. Interestingly, unique and very dissimilar adult phenotypes were observed after injection of dsRNAs that specifically down-regulated either of the two alternatively spliced transcripts of TcCDA2, namely TcCDA2a or TcCDA2b. These results reveal functional specialization among T. castaneum CDA genes and splice variants.
Insect Biochem Mol Biol
PMID:Analysis of functions of the chitin deacetylase gene family in Tribolium castaneum. 1926 6

Chitin, the second most important natural polymer in the world, and its N-deacetylated derivative chitosan are found in a wide variety of organisms. These versatile biopolymers are associated with a broad range of biological functions. This article is the first to report the potential functions of 2 chitin metabolic enzyme genes from Hyriopsis cumingii. A chitinase-3 gene (Chi-3) and a chitin deacetylase gene (Cda) were cloned from H. cumingii and characterized. Semi-quantitative reverse transcription polymerase chain reaction analysis revealed that the Cda gene was expressed in blood, mantle, liver, stomach, kidney, intestine, gill, and foot, whereas Chi-3 was also expressed in those tissues but not in blood. The tissue-specific expression of H. cumingii Chi-3 indicated that other Chi genes may be involved in the H. cumingii immune system. Real-time quantitative polymerase chain reaction analysis showed that the expression of Chi-3 was significantly (P < 0.05) upregulated 12 h after shell damage, suggesting that Chi-3 might hydrolyze superfluous chitin after shell recovery and play a role in shell formation. Conversely, Cda expression did not change significantly (P > 0.05) to maintain a certain degree of acetylation in chitin/chitosan. This study enriches the basic research on chitin metabolic genes and lays foundations for further research of shell regeneration in mussels.
Genet Mol Res 2012 Dec 19
PMID:Two chitin metabolic enzyme genes from Hyriopsis cumingii: cloning, characterization, and potential functions. 2309 18

Chitin deacetylase (CDA) catalyzes the conversion of chitin into chitosan, thereby modifying the physical properties of insect cuticles and peritrophic matrices. A lepidopteran chitin deacetylase gene (CfCDA2) was cloned from the spruce budworm, Choristoneura fumiferana, and found to generate two alternatively spliced transcripts, CfCDA2a and CfCDA2b. Transcriptional analysis using isoform-specific RT-PCR primers indicated that both isoforms were upregulated during the molt. Interestingly, CfCDA2b transcripts were most abundant in the head during the molting stage while those of CfCDA2a were predominant in the epidermis during the feeding period. Injection of CfCDA2-specific dsRNA into C. fumiferana larvae or pre-pupae induced both abnormal phenotypes and high mortality, which resulted from an inability to shed the old cuticle. These results suggest that CfCDA2 plays an important role in the molting process, and that the two alternatively spliced transcripts have different functions during insect development. This is the first detailed characterization of lepidopteran chitin deacetylase gene.
Insect Biochem Mol Biol 2013 Aug
PMID:Characterization of a spruce budworm chitin deacetylase gene: stage- and tissue-specific expression, and inhibition using RNA interference. 2362 57


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