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Enzyme Nomenclature
Information on EC 2.4.1.16 - chitin synthase
Word Map on EC 2.4.1.16
- 2.4.1.16
- fungus
- candida
- albicans
- nikkomycins
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antifungal
- hyphal
- septum
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zymogen
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polyoxins
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calcofluor
- chitinase
- glucans
- chitosomes
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cytokinesis
- conidia
- rouxii
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echinocandins
- dermatitidis
- mucor
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peritrophic
- trichophyton
- microfibrils
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dermatophytes
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septins
- beta-1,3-glucan
- phycomyces
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chitin-binding
- mentagrophytes
- conidiophore
- diflubenzuron
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exophiala
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exoskeleton
- caspofungin
- arthroderma
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mother-bud
- castaneum
- agriculture
- microsporum
- malassezia
- analysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.1.16
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RECOMMENDED NAME
GeneOntology No.
chitin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + [4)-N-acetyl-beta-D-glucosaminyl-(1->]n = UDP + [4)-N-acetyl-beta-D-glucosaminyl-(1->]n+1
UDP-N-acetyl-alpha-D-glucosamine + [4)-N-acetyl-beta-D-glucosaminyl-(1->]n = UDP + [4)-N-acetyl-beta-D-glucosaminyl-(1->]n+1
mechanism
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UDP-N-acetyl-alpha-D-glucosamine + [4)-N-acetyl-beta-D-glucosaminyl-(1->]n = UDP + [4)-N-acetyl-beta-D-glucosaminyl-(1->]n+1
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase
Converts UDP-N-acetyl-alpha-D-glucosamine into chitin and UDP.
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CAS REGISTRY NUMBER
COMMENTARY
9030-18-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chitin synthase 2; f. sp. lycopersici, myosin motor-like chitin synthase gene chsVb
UniProt
LeChs1; an edible basidiomycetous mushroom, strain strain SB1226, gene Lechs1, isozyme LeChs1
UniProt
an edible basidiomycetous mushroom, class IV chitin synthase isozyme, gene Pochs1
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strain YPH499 and ECY38-38A, isozyme CHS2p encoded by gene CHS2; strain YPH499 and ECY38-38A, isozymes CHS1p and CHS3p encoded by genes CHS1 and CHS3
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the fungus contains 10 chitin synthase isozymes of different classes, overview
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i.e. Exophiala dermatitidis, strain 8656, ATCC 34100, isozyme WdChs5p
UniProt
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488635, 488640, 488644, 488654, 488659, 488666, 488669, 658577, 659776, 673420, 688579, 702573, 720092, 735750, 735772
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chitin synthase 1 is examide in wild-type strain ATCC 26109 and D3C (MATalphaura3-52), chitin synthase 2 is investigated in a strain D3B freed of chitin synthase 1 by gene disruption; chitin synthetase 1 and 2
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gene chs3coding for the catalytic subunit of the chitin synthase III
SwissProt
strain YPH499 and ECY38-38A, isozyme CHS2p encoded by gene CHS2; strain YPH499 and ECY38-38A, isozymes CHS1p and CHS3p encoded by genes CHS1 and CHS3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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chitin production in arthropods is a complicated process and a series of biochemical pathways are involved in individual chitin polymer biosynthesis in which the terminal step is catalyzed by chitin synthase
physiological function
additional information
evolution
chitin synthase genes (chs) constitute a complex family in filamentous fungi and are involved in fungal development, morphogenesis, pathogenesis and virulence, phylogenetic analysis of chsI-VII
evolution
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chitin synthase genes (chs) constitute a complex family in filamentous fungi and are involved in fungal development, morphogenesis, pathogenesis and virulence, phylogenetic analysis of chsI-VII
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malfunction
exposure to nikkomycin Z, a CHS inhibitor, reduces the amount of chitin in the peritrophic membrane of molted larvae
malfunction
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the chs2DELTA mutant forms chained cells in which daughter cells are connected with mother cells and have abnormally thick septa at the bud neck. The chs4DELTA mutant shows remarkably reduced chitin content in its cell wall. The chs2DELTA, csm1DELTA, and csm2DELTA mutants are highly sensitive to chitin binding dyes, calcofluor white and Congo red, whereas the chs4DELTA mutant is resistant to calcofluor white. The lengths of the cellular long and short axes of populations of filamentous cells are decreased in the chs3DELTA mutant
malfunction
the Bcchs6 disruption mutant exhibits a 45.5% increasing in its chitin content when compared with the wild-type strain. In Bcchs6 mutant the expression of BcChs6 is significantly decreased, while the expression of genes BcChs2 and BcChs3a is increased when compared with wild-type. It is probable that the disruption of gene Bcchs6 provokes a compensatory mechanism regulatingthe cellular response to cell wall damage. The radial growth of Bcchs6 mutant is drastically reduced when 50% solute is removed from the regular PDA medium, and they are more sensitive to Calcofluor white and other cell wall disturbing chemicals. Pathogenicity assays on tomato leaves indicate that the mutant is significantly reduced in their ability to cause disease. The radial lesion produced by Bcchs6 mutant is almost not detected even at 6 days after inoculation, indicating the pathogenicity is drastically reduced in Bcchs6 mutant
malfunction
PdchsVII mutants have reduced virulence on citrus fruit. Disruption of gene chsVII has an effect on the expression of other isozymes during growth in liquid PDB medium. The largest increase of expression is shown in both disruption mutant strains PDMG672 and PDMG439 by gene PdchsII, which is induced up to 50fold during growth, while in strain CECT20796 it remains almost constant or even declines. Expression of PdchsIV, PdchsV and PdchsVI genes is also induced in disruption mutants compared to the parental strain. Expression of PdchsI and PdchsIII remaines at similar levels in the mutant and wild-type strains
malfunction
isozyme mutant DELTAchs-6 strain displays less chitin content, slow colony growth, and apical hyperbranching. Mycelium biomass (dry weight) is reduced in the mutant strain with reduced chitin content; mycelium biomass (dry weight) is reduced in the mutant strain with no apparent reduction in chitin content or growth rate, but less production of aerial hyphae and conidia; mycelium biomass (dry weight) is reduced in the mutant strain with no apparent reduction in chitin content or growth rate, but less production of aerial hyphae and conidia
malfunction
knockdown of BmChsA gene in third instar larvae increases the number of non-molting and abnormal molting larvae
malfunction
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the Bcchs6 disruption mutant exhibits a 45.5% increasing in its chitin content when compared with the wild-type strain. In Bcchs6 mutant the expression of BcChs6 is significantly decreased, while the expression of genes BcChs2 and BcChs3a is increased when compared with wild-type. It is probable that the disruption of gene Bcchs6 provokes a compensatory mechanism regulatingthe cellular response to cell wall damage. The radial growth of Bcchs6 mutant is drastically reduced when 50% solute is removed from the regular PDA medium, and they are more sensitive to Calcofluor white and other cell wall disturbing chemicals. Pathogenicity assays on tomato leaves indicate that the mutant is significantly reduced in their ability to cause disease. The radial lesion produced by Bcchs6 mutant is almost not detected even at 6 days after inoculation, indicating the pathogenicity is drastically reduced in Bcchs6 mutant
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malfunction
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isozyme mutant DELTAchs-6 strain displays less chitin content, slow colony growth, and apical hyperbranching. Mycelium biomass (dry weight) is reduced in the mutant strain with reduced chitin content; mycelium biomass (dry weight) is reduced in the mutant strain with no apparent reduction in chitin content or growth rate, but less production of aerial hyphae and conidia; mycelium biomass (dry weight) is reduced in the mutant strain with no apparent reduction in chitin content or growth rate, but less production of aerial hyphae and conidia
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malfunction
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PdchsVII mutants have reduced virulence on citrus fruit. Disruption of gene chsVII has an effect on the expression of other isozymes during growth in liquid PDB medium. The largest increase of expression is shown in both disruption mutant strains PDMG672 and PDMG439 by gene PdchsII, which is induced up to 50fold during growth, while in strain CECT20796 it remains almost constant or even declines. Expression of PdchsIV, PdchsV and PdchsVI genes is also induced in disruption mutants compared to the parental strain. Expression of PdchsI and PdchsIII remaines at similar levels in the mutant and wild-type strains
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malfunction
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the chs2DELTA mutant forms chained cells in which daughter cells are connected with mother cells and have abnormally thick septa at the bud neck. The chs4DELTA mutant shows remarkably reduced chitin content in its cell wall. The chs2DELTA, csm1DELTA, and csm2DELTA mutants are highly sensitive to chitin binding dyes, calcofluor white and Congo red, whereas the chs4DELTA mutant is resistant to calcofluor white. The lengths of the cellular long and short axes of populations of filamentous cells are decreased in the chs3DELTA mutant
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physiological function
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gene disruption mutant is not significantly affected in either growth characteristics or pathogenicity on tomato leaves. Mutant exhibits a 31% increase in its chitin content and displays increased sensitivity to Caclofluor White and slightly enhanced tolerance to cell-wall disturbing substances and osmosis regulators
physiological function
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mutants lacking isoform CHS7 or isoform CHS5 do not produce perithecia or cause disease on barley heads. Mutant cells form balloon-shaped hyphae and intrahyphal hyphae, their cell wall rigidity is weaker than that of wild-type
physiological function
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deletion mutants of isoform ChsB show multilayered cell walls and intrahyphal hyphae in their hyphae. ChsB functions in the formation of normal cell walls of hyphae, as well as in conidiophore and conidia development
physiological function
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specific disruption of the CHS1 gene results in a 58% reduction of chitin synthase activity, accompanied by decreases of 35% in chitin content, 22% in conidiation, and 16% in macroconidium length. The mutant strain has a growth rate comparable to that of the wild-type on PDA medium but has a 35% increase in the number of nuclear cellulae and exhibits a remarkably increased sensitivity to osmosis stresses. Mutant shows substantial changes in cell wall structures of the macroconidium, ascospore, and mycelium, with the most profound changes in the mycelium. The mutant displays significantly reduced pathogenicity on wheat spikes and seedlings
physiological function
enzyme deletion mutants are unable to form appressoria on artificial surfaces, except following the application of the exogenous inducers 1,16-hexadecanediol and cyclic adenosine monophosphate. The appressoria formed have a reduced chitin content and are often smaller and misshapen compared with the wild-type. Mutants are significantly reduced in their ability to enter rice plants, but growth in planta is not affected
physiological function
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treatment of Candida albicans with low levels of echinocandins such as caspofungin, echinocandin B, cilofungin and anidulafungin stimulates chitin synthase gene expression, increases Chs activity, elevates chitin content and reduced efficacy of these drugs. Elevation of chitin synthesis is mediated via the PKC, HOG, and Ca2+-calcineurin signalling pathways. Stimulation of isoforms Chs2p and Chs8p by activators of these pathways enables cells to survive otherwise lethal concentrations of echinocandins, even in the absence of Chs3p and the normally essential Chs1p, which synthesize the chitinous septal ring and primary septum of the fungus. Under such conditions, a novel proximally offset septum is synthesized that restores the capacity for cell division, sustaines the viability of the cell, and abrogates morphological and growth defects associated with echinocandin treatment and the chs mutations
physiological function
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in the conidia, chitin content in the cell wall of a mutant strain lacking activity of isoform csmA is less than half the amount found in the parental strain. The isoform csmB mutant strain and the isoform csmA/csmB double mutant strain do not show any modification of chitin content in their conidial cell walls. In contrast to the hydrophobic conidia of the parental strain, conidia of all of the chitin synthase mutants are hydrophilic due to the presence of an amorphous material covering the hydrophobic surface-rodlet layer. The deletion of chitin synthase genes also results in an increased susceptibility of resting and germinating conidia to echinocandins
physiological function
isoform CHS5 and CHS7 single deletion mutants and the CHS5/CHS7 double mutant grow poorly and exhibit small, hyperpigmented colonies with very little aerial mycelia as compared to the wild-type strain. The mutant strains also tend to grow into the potato dextrose agar media rather than growing evenly over the surface as compared to the wild type. The addition of 0.2 M KCl into the medium suppresses the mutant phenotype. Both isoforms are required for normal hyphal growth and maximal disease of maize seedlings and ear. Mutant strains are more sensitive to cell wall stressing compounds, e.g., Nikkomycin Z, than wild type. Mutant strains are significantly reduced in their ability to cause disease; isoform CHS5 and CHS7single deletion mutants and the CHS5/CHS7 double mutant grow poorly and exhibit small, hyperpigmented colonies with very little aerial mycelia as compared to the wild-type strain. The mutant strains also tend to grow into the potato dextrose agar media rather than growing evenly over the surface as compared to the wild type. The addition of 0.2 M KCl into the medium suppresses the mutant phenotype. Both isoforms are required for normal hyphal growth and maximal disease of maize seedlings and ear. Mutant strains are more sensitive to cell wall stressing compounds, e.g., Nikkomycin Z, than wild type. Mutant strains are significantly reduced in their ability to cause disease
physiological function
presence of alternative exons CHSA-2a and CHSA-2b. Transcripts of both exons are preferentially expressed in epidermis. Gene silencing of CHSA-2a causes incomplete molting, while silencing of CHSA-2b exclusively influences the head cuticle formation of the 3rd instar larval
physiological function
isoform Mcs1 consists of a myosin motor domain fused to a membrane-spanning chitin synthase region. Both domains are required for fungal virulence. Fungi carrying mutations in the chitin synthase domain are rapidly recognized and killed by the plant, whereas fungi carrying a deletion of the motor domain show alterations in cell wall composition but can invade host tissue and cause a moderate plant response. Mcs1-bound vesicles exhibit long-range movement for up to 20 mm at a velocity of ;1.75 microm/s. Apical Mcs1 localization depends on F-actin and the motor domain, whereas Mcs1 motility requires microtubules and persists when the Mcs1 motor domain is deleted
physiological function
isoform Chs1 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis. Chitin is vital for the micro-organisms despite its very low abundance in the cell walls. It is most likely synthesized transiently at the apex of the cells before cellulose, the major cell wall component in oomycetes; isoform Chs2 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis. Chitin is vital for the micro-organisms despite its very low abundance in the cell walls. It is most likely synthesized transiently at the apex of the cells before cellulose, the major cell wall component in oomycetes
physiological function
chitin synthase is the key regulatory enzyme in chitin synthesis and excretion in insects, and a specific target of insecticides. Expression of BmChsB is regulated by insect hormones, and directly affects the chitin-synthesis-dependent form of the peritrophic membrane and protects the food intake and molting process of silkworm larvae. Gene BmChsB is a midgut-specific gene induced by insect hormones and involved in protecting the food intake of Bombyx mori larvae
physiological function
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isozymes Chs2 and Chs4 may play major roles in septum formation and cell wall chitin synthesis respectively, whereas isozymes Csm1 and Csm2 are involved in the maintenance of cell wall architecture and/or cell wall integrity. Isozyme Chs3 seems to be involved in cellular morphogenesis
physiological function
enzyme BcChsVI is necessary for proper hyphal growth and pathogenicity of Botrytis cinerea on tomato leaves, the radial lesion induced by the wild-type strain B05.10 spread rapidly and totally invaded the leaf at 4 days post inoculation
physiological function
chitin synthase PdChsVII is required for development, cell wall integrity and virulence in the citrus postharvest pathogen Penicillium digitatum. Differential expression of chitin synthase genes in PdchsVII mutants in response to infection
physiological function
isozyme CHS-6 is important for apical growth and hyphal morphology, it is involved in vegetative growth; isozymes CHS-3 and CHS-5 have an important role during asexual and sexual reproduction; isozymes CHS-3 and CHS-5 have an important role during asexual and sexual reproduction
physiological function
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CHS catalyzes the transfer of sugar moieties from activated sugar donors to specific acceptors in all chitin-containing organisms
physiological function
chitin synthases transfer GlcNAc from UDP-GlcNAc to preexisting chitin chains in reactions that are typically stimulated by free GlcNAc. The enzyme is involved in biosynthesis of chitin, a homopolymer of beta-1,4-linked GlcNAc residues and a key component of fungal cell walls and the arthropod exoskeleton
physiological function
the extracellular domain ArCS1_E22 is involved in regulating the multiple enzyme activities of Ar-CS1 such as chitin synthesis and myosin movements by interaction with mineral surfaces and eventually by protein assembly. The protein complexes can locally probe the status of mineralization according to pH unless ions and pCO2 are balanced with suitable buffer substances. The intact enzyme can act as a force sensor. The shell formation is coordinated physiologically with precise adjustment of cellular activities to the structure, topography and stiffness at the mineralizing interface
physiological function
chitin synthase is the key regulatory enzyme for chitin synthesis and excretion in insects, as well as a specific target of insecticides. Chitin synthase A gene BmChsA is an epidermis-specific expressed gene during the molting stage. Expression of gene BmChsA is regulated by endocrine hormones, which directly affect the chitin synthesis-dependent epidermal regeneration and molting process. BmChsA gene expression is strongly regulated by 20-hydroxyecdysone
physiological function
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enzyme BcChsVI is necessary for proper hyphal growth and pathogenicity of Botrytis cinerea on tomato leaves, the radial lesion induced by the wild-type strain B05.10 spread rapidly and totally invaded the leaf at 4 days post inoculation
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physiological function
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mutants lacking isoform CHS7 or isoform CHS5 do not produce perithecia or cause disease on barley heads. Mutant cells form balloon-shaped hyphae and intrahyphal hyphae, their cell wall rigidity is weaker than that of wild-type
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physiological function
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isozyme CHS-6 is important for apical growth and hyphal morphology, it is involved in vegetative growth; isozymes CHS-3 and CHS-5 have an important role during asexual and sexual reproduction; isozymes CHS-3 and CHS-5 have an important role during asexual and sexual reproduction
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physiological function
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chitin synthase PdChsVII is required for development, cell wall integrity and virulence in the citrus postharvest pathogen Penicillium digitatum. Differential expression of chitin synthase genes in PdchsVII mutants in response to infection
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physiological function
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isozymes Chs2 and Chs4 may play major roles in septum formation and cell wall chitin synthesis respectively, whereas isozymes Csm1 and Csm2 are involved in the maintenance of cell wall architecture and/or cell wall integrity. Isozyme Chs3 seems to be involved in cellular morphogenesis
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additional information
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chitin content in and morphological features of wild-type and enzyme mutant cells, overview
additional information
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chitin content in and morphological features of wild-type and enzyme mutant cells, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-O-dansyl-N-acetylglucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
?
Kluyveromyces bulgaricus
-
-
-
-
?
acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Kluyveromyces bulgaricus
-
-
-
-
?
chitobiose + N-acetyl-D-glucosamine
UDP + 1,4-(N-acetyl-beta-D-glucosaminyl)x
-
-
-
-
?
UDP-GlcNAc + GlcNAc
UDP + N-acetyl-beta-D-glucosaminyl-(1,4)-N-acetyl-beta-D-glucosamine
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosamine
UDP + 1,4-(N-acetyl-beta-D-glucosaminyl)2
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [(1-4)-N-acetyl-beta-D-glucosaminyl-]n
UDP + [(1-4)-N-acetyl-beta-D-glucosaminyl-]n+1
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
UDP-N-acetyl-D-glucosamine + [4-N-acetyl-beta-D-glucosaminyl-(1-)]n
UDP + [4-N-acetyl-beta-D-glucosaminyl-(1-)]n+1
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [(1-4)-N-acetyl-beta-D-glucosaminyl-]n
UDP + [(1-4)-N-acetyl-beta-D-glucosaminyl-]n+1
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [(1-4)-N-acetyl-beta-D-glucosaminyl-]n
UDP + [(1-4)-N-acetyl-beta-D-glucosaminyl-]n+1
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
key enzyme in chitin biosynthesis
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Apodachlya sp.
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase B is essential for hyphal growth
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase 1 is involved in repair functions at the end of cytokinesis, chitin synthase 2 is responsible for the synthesis of the primary septum that separates mother and daughter cells, chitin synthase 3 is responsible for the formation of the ring where most of the cell wall chitin is located
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
deletion of chsE causes a significant decrease in the chitin content of the cell wall during early sexual development. Expression of chsE is increased by substituting glucose with lactose or by addition of 0.6 M KCl or NaCl, but affected little by substituting glucose with sodium acetate. ChsE has a mode of expression distinct from those of the other chitin synthase genes, chsA, chsB and chsC
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
subapical branching may be regulated though an interplay between chitinolytic enzymes and chitin synthases, chitin synthase B may represent the main chitin synthase activity involved in apical hyphal extension
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
the enzyme is likely to be essential to oogenesis and embryonic development
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase III from Candida albicans plays an important role in maintaining cell wall integrity, being essential when invading surrounding tissues. Candida albicans strains deficient in CHS7, a key regulator of chitin synthase III, exhibit morphogenetic alterations and attenuated virulence
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Chlorovirus CVK2
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Chlorovirus CVK2
-
chlorovirus CVK2 encodes a chitin synthase gene and produces hairy chitin polysaccharides on the infected cell surface
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
chitin
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase activity is required for normal development of nematodes and removal of this activity delays emergency of juveniles in Meloidogyne artiellia
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Mortierella candelabrum
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Mortierella pusilla
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
chitin
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
existence of a unique secretory pathway based on chitosome microvesicles as the main conveyors of chitin synthetase to the cell surface
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
chitin
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
chitin
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
chitin
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
the enzyme itself is capable both of initiating chitin chains without a primer and of determining their length
at low concentrations of UDP-GlcNAc, no insoluble chitin is formed. Instead N-acetylglucosamine is incorporated into water-soluble products
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthetase 2 is responsible for chitin synthesis in vivo, chitin synthase 1 is not essential
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthetase 2 is the physiological agent for chitin deposition in strains with a disrupted CHS1 gene
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthetase 2 is essential for primary septum formation, chitin synthetase 1 is a repair enzyme
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
chitin synthase III activity is required for remedial septa formation in Saccharomyces cerevisiae
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
most chitin is synthesized by Chs3p, which deposites chitin in the lateral cell wall and in the bud-neck region during cell division. Chs3p-dependent chitin synthesis is regulated both by the level of intermediates of the UDP-GlcNAc-biosynthetic pathways and by an increase in the activity of the enzyme in the plasma membrane
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
chitin
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [4-N-acetyl-beta-D-glucosaminyl-(1-)]n
UDP + [4-N-acetyl-beta-D-glucosaminyl-(1-)]n+1
-
-
-
?
UDP-N-acetyl-D-glucosamine + [4-N-acetyl-beta-D-glucosaminyl-(1-)]n
UDP + [4-N-acetyl-beta-D-glucosaminyl-(1-)]n+1
-
-
-
?
additional information
?
-
-
method optimzation to assay chitin synthase activity, overview
-
-
-
additional information
?
-
ChsA and ChsC share overlapping roles in septum formation
-
-
-
additional information
?
-
CsmA and CsmB play compensatory roles that are essential for normal tip growth
-
-
-
additional information
?
-
CsmA and CsmB play compensatory roles that are essential for normal tip growth
-
-
-
additional information
?
-
-
chitin synthase, CsmA contains a myosin motor-like domain
-
-
-
additional information
?
-
-
chs-1 is critical for eggshell production. Complete loss of function in a chs-1 deletion results in embryos that lack chitin in their eggshells and fail to divide
-
-
-
additional information
?
-
-
knocking down chs-2 by RNAi causes a defect in the pharynx and leads to L1 larval arrest, indicating that chitin is involved in the development and function of the pharynx
-
-
-
additional information
?
-
-
chitin synthesis and hydrolysis are not coupled, but both are regulated during yeast - hyphe morphogenesis in Candida albicans
-
-
-
additional information
?
-
-
class II CaChs1p is involved in septum formation in both the yeast and hyphal forms and for cell integrity
-
-
-
additional information
?
-
-
the hyphal-specific chitin synthase gene CHS2 is not essential for growth, dimorphism, or virulence. The class I CaChs2p enzyme is responsible for part of the hyphal chitin
-
-
-
additional information
?
-
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
Q5A7T2
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
-
the chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola, overview
-
-
-
additional information
?
-
the chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola, overview
-
-
-
additional information
?
-
the chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola, overview
-
-
-
additional information
?
-
-
CHS3 is the most important chitin synthase for vegetative growth. Deletion of chs3 gene leads to cell death at 37°C
-
-
-
additional information
?
-
CHS3 is the most important chitin synthase for vegetative growth. Deletion of chs3 gene leads to cell death at 37°C
-
-
-
additional information
?
-
-
insect development is dependent on the precisely tuned expression of chitin synthase genes. Ecdysterone has a regulatory role on CHS-1 (DmeChSB) and CHS-2
-
-
-
additional information
?
-
WdChs1p is more responsible than WdChs2p for normal yeast cell reproductive growth because strains with defects in the latter exhibited no morphological abnormalities, whereas those with defects in WdChs1p are frequently impaired in one or more yeast developmental processes
-
-
-
additional information
?
-
class V chitin synthase is required for sustained cell growth at the temperature of infection, 37°C, with increased WdCHS5 mRNA synthesis being the major factor responsible for the increased WdCHS5 transcript
-
-
-
additional information
?
-
class VII chitin synthase involved in septation is critical for pathogenicity in Fusarium oxysporum, gene chsVb is likely to function in polarized growth and confirm the critical importance of cell wall integrity in the complex infection process of this fungus, overview
-
-
-
additional information
?
-
-
MsCHS1 appears to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
-
-
-
additional information
?
-
MsCHS1 appears to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
-
-
-
additional information
?
-
MsCHS1 appears to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
-
-
-
additional information
?
-
chitin synthesis is controlled by an intestinal proteolytic signalling cascade linking chitin synthase activity to the nutritional state of the larvae, overview
-
-
-
additional information
?
-
CHS2 interacts with the extracellular chymotrypsin-like protease CTLP1 in the midgut, overview
-
-
-
additional information
?
-
-
Chs4p (Cal2/Csd4/Skt5) is a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Abolition of Chs4p prenylation causes about 60% decrease in CSIII activity, which is correlated with about 30% decrease in chitin content. Lack of Chs4p prenylation decreases the average chain length of the chitin polymer
-
-
-
additional information
?
-
Chs2 synthesizes the primary septum after mitosis is completed. It is essential for proper cell separation and expected to be highly regulated. Chs2 is hyperactivated by a soluble yeast protease, which is expressed during logarithmic growth phase, when budding cells require Chs2 activity
-
-
-
additional information
?
-
-
Chs4p is required for chitin synthase III activity and hence for chitin synthesis
-
-
-
additional information
?
-
-
proper CSIII turnover is maintained through the endocytic internalization of Chs3p, overview
-
-
-
additional information
?
-
formation of chitin oligosaccharides and insoluble chitin, and by replacing GlcNAc with 2-acylamido analogues of GlcNAc. Synthesis of chitin oligosaccharides is strongly dependent on inclusion of GlcNAc in chitin synthase incubations, and N,N'-diacetylchitobiose is the major reaction product. Formation of both chitin oligosaccharides and insoluble chitin is also stimulated by GlcNAc2 and by N-propanoyl-, N-butanoyl-, and N-glycolylglucosamine
-
-
-
additional information
?
-
Chs2 synthesizes the primary septum after mitosis is completed. It is essential for proper cell separation and expected to be highly regulated. Chs2 is hyperactivated by a soluble yeast protease, which is expressed during logarithmic growth phase, when budding cells require Chs2 activity
-
-
-
additional information
?
-
chitin synthase B is very important in midgut formation and development
-
-
-
additional information
?
-
the enzyme is involved in larval development, and is important for the growth and development of cuticles and trachea in the beet armyworm, Spodoptera exigua, overview
-
-
-
additional information
?
-
-
the enzyme is involved in larval development, and is important for the growth and development of cuticles and trachea in the beet armyworm, Spodoptera exigua, overview
-
-
-
additional information
?
-
Chitin synthases are large membrane proteins that catalyze the polymerization of N-acetylglucosamine into chitin, a major component of the exoskeletons and peritrophic membranes of insects
-
-
-
additional information
?
-
-
Chitin synthases are large membrane proteins that catalyze the polymerization of N-acetylglucosamine into chitin, a major component of the exoskeletons and peritrophic membranes of insects
-
-
-
additional information
?
-
RNAi-mediated down-regulation of TcCHS2, but not TcCHS1, leads to cessation of feeding, a dramatic shrinkage in larval size and reduced chitin content in the midgut
-
-
-
additional information
?
-
-
RNAi-mediated down-regulation of TcCHS2, but not TcCHS1, leads to cessation of feeding, a dramatic shrinkage in larval size and reduced chitin content in the midgut
-
-
-
additional information
?
-
splice variant 8a of TcCHS1 is required for both the larval-pupal and pupal-adult moults, whereas splice variant 8b is required only for the latter
-
-
-
additional information
?
-
-
splice variant 8a of TcCHS1 is required for both the larval-pupal and pupal-adult moults, whereas splice variant 8b is required only for the latter
-
-
-
additional information
?
-
chitin, synthesized by chitin synthase, is essential for the structural integrity of the exoskeletal cuticle and midgut peritrophic membrane of insects
-
-
-
additional information
?
-
chitin, synthesized by chitin synthase, is essential for the structural integrity of the exoskeletal cuticle and midgut peritrophic membrane of insects
-
-
-
additional information
?
-
CHS catalyzes the synthesis of chitin, the beta-1,4-linked polymer of N-acetylglucosamine
-
-
-
additional information
?
-
CHS catalyzes the synthesis of chitin, the beta-1,4-linked polymer of N-acetylglucosamine
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
R4I3H8
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
R4I3H8
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
P14180
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
key enzyme in chitin biosynthesis
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase B is essential for hyphal growth
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase 1 is involved in repair functions at the end of cytokinesis, chitin synthase 2 is responsible for the synthesis of the primary septum that separates mother and daughter cells, chitin synthase 3 is responsible for the formation of the ring where most of the cell wall chitin is located
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
P78611
deletion of chsE causes a significant decrease in the chitin content of the cell wall during early sexual development. Expression of chsE is increased by substituting glucose with lactose or by addition of 0.6 M KCl or NaCl, but affected little by substituting glucose with sodium acetate. ChsE has a mode of expression distinct from those of the other chitin synthase genes, chsA, chsB and chsC
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
subapical branching may be regulated though an interplay between chitinolytic enzymes and chitin synthases, chitin synthase B may represent the main chitin synthase activity involved in apical hyphal extension
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Q9GQC3
the enzyme is likely to be essential to oogenesis and embryonic development
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase III from Candida albicans plays an important role in maintaining cell wall integrity, being essential when invading surrounding tissues. Candida albicans strains deficient in CHS7, a key regulator of chitin synthase III, exhibit morphogenetic alterations and attenuated virulence
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
Chlorovirus CVK2
-
chlorovirus CVK2 encodes a chitin synthase gene and produces hairy chitin polysaccharides on the infected cell surface
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthase activity is required for normal development of nematodes and removal of this activity delays emergency of juveniles in Meloidogyne artiellia
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
existence of a unique secretory pathway based on chitosome microvesicles as the main conveyors of chitin synthetase to the cell surface
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthetase 2 is responsible for chitin synthesis in vivo, chitin synthase 1 is not essential
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthetase 2 is the physiological agent for chitin deposition in strains with a disrupted CHS1 gene
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
chitin synthetase 2 is essential for primary septum formation, chitin synthetase 1 is a repair enzyme
-
-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
P29465
chitin synthase III activity is required for remedial septa formation in Saccharomyces cerevisiae
-
-
?
additional information
?
-
P30583
ChsA and ChsC share overlapping roles in septum formation
-
-
-
additional information
?
-
O13281
CsmA and CsmB play compensatory roles that are essential for normal tip growth
-
-
-
additional information
?
-
Q2L6A0
CsmA and CsmB play compensatory roles that are essential for normal tip growth
-
-
-
additional information
?
-
-
chs-1 is critical for eggshell production. Complete loss of function in a chs-1 deletion results in embryos that lack chitin in their eggshells and fail to divide
-
-
-
additional information
?
-
-
knocking down chs-2 by RNAi causes a defect in the pharynx and leads to L1 larval arrest, indicating that chitin is involved in the development and function of the pharynx
-
-
-
additional information
?
-
-
chitin synthesis and hydrolysis are not coupled, but both are regulated during yeast - hyphe morphogenesis in Candida albicans
-
-
-
additional information
?
-
-
class II CaChs1p is involved in septum formation in both the yeast and hyphal forms and for cell integrity
-
-
-
additional information
?
-
-
the hyphal-specific chitin synthase gene CHS2 is not essential for growth, dimorphism, or virulence. The class I CaChs2p enzyme is responsible for part of the hyphal chitin
-
-
-
additional information
?
-
P23316
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
P30572
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
P30573
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
Q5A7T2
shape and integrity of fungal cells is dependent on the skeletal polysaccharides in their cell walls of which beta-1,3-glucan and chitin are of principle importance, individual chitin synthase enzymes synthesize microfibrils of differing structure at specific locations in the Candida albicans cell wall, overview
-
-
-
additional information
?
-
-
the chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola, overview
-
-
-
additional information
?
-
Q8TFN5
the chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola, overview
-
-
-
additional information
?
-
Q8TFN6
the chitin synthase with a myosin-like motor domain is essential for hyphal growth, appressorium differentiation, and pathogenicity of the maize anthracnose fungus Colletotrichum graminicola, overview
-
-
-
additional information
?
-
-
CHS3 is the most important chitin synthase for vegetative growth. Deletion of chs3 gene leads to cell death at 37°C
-
-
-
additional information
?
-
Q5KCU4
CHS3 is the most important chitin synthase for vegetative growth. Deletion of chs3 gene leads to cell death at 37°C
-
-
-
additional information
?
-
-
insect development is dependent on the precisely tuned expression of chitin synthase genes. Ecdysterone has a regulatory role on CHS-1 (DmeChSB) and CHS-2
-
-
-
additional information
?
-
P30600
WdChs1p is more responsible than WdChs2p for normal yeast cell reproductive growth because strains with defects in the latter exhibited no morphological abnormalities, whereas those with defects in WdChs1p are frequently impaired in one or more yeast developmental processes
-
-
-
additional information
?
-
Q8TGV2
class V chitin synthase is required for sustained cell growth at the temperature of infection, 37°C, with increased WdCHS5 mRNA synthesis being the major factor responsible for the increased WdCHS5 transcript
-
-
-
additional information
?
-
Q5YCX0
class VII chitin synthase involved in septation is critical for pathogenicity in Fusarium oxysporum, gene chsVb is likely to function in polarized growth and confirm the critical importance of cell wall integrity in the complex infection process of this fungus, overview
-
-
-
additional information
?
-
-
MsCHS1 appears to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
-
-
-
additional information
?
-
Q530Z6
MsCHS1 appears to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
-
-
-
additional information
?
-
Q8T4U2
MsCHS1 appears to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
-
-
-
additional information
?
-
Q530Z6
chitin synthesis is controlled by an intestinal proteolytic signalling cascade linking chitin synthase activity to the nutritional state of the larvae, overview
-
-
-
additional information
?
-
-
Chs4p (Cal2/Csd4/Skt5) is a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Abolition of Chs4p prenylation causes about 60% decrease in CSIII activity, which is correlated with about 30% decrease in chitin content. Lack of Chs4p prenylation decreases the average chain length of the chitin polymer
-
-
-
additional information
?
-
A6ZKY2
Chs2 synthesizes the primary septum after mitosis is completed. It is essential for proper cell separation and expected to be highly regulated. Chs2 is hyperactivated by a soluble yeast protease, which is expressed during logarithmic growth phase, when budding cells require Chs2 activity
-
-
-
additional information
?
-
-
Chs4p is required for chitin synthase III activity and hence for chitin synthesis
-
-
-
additional information
?
-
A6ZKY2
Chs2 synthesizes the primary septum after mitosis is completed. It is essential for proper cell separation and expected to be highly regulated. Chs2 is hyperactivated by a soluble yeast protease, which is expressed during logarithmic growth phase, when budding cells require Chs2 activity
-
-
-
additional information
?
-
Q06BR7
chitin synthase B is very important in midgut formation and development
-
-
-
additional information
?
-
Q3I5Q4
the enzyme is involved in larval development, and is important for the growth and development of cuticles and trachea in the beet armyworm, Spodoptera exigua, overview
-
-
-
additional information
?
-
-
the enzyme is involved in larval development, and is important for the growth and development of cuticles and trachea in the beet armyworm, Spodoptera exigua, overview
-
-
-
additional information
?
-
Q6WD22
RNAi-mediated down-regulation of TcCHS2, but not TcCHS1, leads to cessation of feeding, a dramatic shrinkage in larval size and reduced chitin content in the midgut
-
-
-
additional information
?
-
-
RNAi-mediated down-regulation of TcCHS2, but not TcCHS1, leads to cessation of feeding, a dramatic shrinkage in larval size and reduced chitin content in the midgut
-
-
-
additional information
?
-
Q6WD22
splice variant 8a of TcCHS1 is required for both the larval-pupal and pupal-adult moults, whereas splice variant 8b is required only for the latter
-
-
-
additional information
?
-
-
splice variant 8a of TcCHS1 is required for both the larval-pupal and pupal-adult moults, whereas splice variant 8b is required only for the latter
-
-
-
additional information
?
-
Q6WD22
chitin, synthesized by chitin synthase, is essential for the structural integrity of the exoskeletal cuticle and midgut peritrophic membrane of insects
-
-
-
additional information
?
-
Q6WD23
chitin, synthesized by chitin synthase, is essential for the structural integrity of the exoskeletal cuticle and midgut peritrophic membrane of insects
-
-
-
additional information
?
-
O13394
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
O13395
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
P30598
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
P30599
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
Q4P333
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
Q99126
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
Q99127
CHS1 supports the tip growth of yeastlike cells
-
-
-
additional information
?
-
O13394
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
O13395
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
P30598
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
P30599
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q4P333
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q99126
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q99127
CHS2 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
O13394
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
O13395
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
P30598
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
P30599
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q4P333
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q99126
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q99127
CHS3 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
O13394
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
O13395
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
P30598
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
P30599
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q4P333
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q99126
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
Q99127
CHS4 plays a minor role during infection process and becomes crucial when the plant grows under optimal conditions
-
-
-
additional information
?
-
O13394
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
O13395
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
P30598
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
P30599
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q4P333
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q99126
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q99127
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs5 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
O13394
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
O13395
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
P30598
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
P30599
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q4P333
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q99126
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q99127
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs6 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
O13394
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
O13395
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
P30598
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
P30599
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q4P333
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q99126
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
additional information
?
-
Q99127
CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth. Chs7 is important for mating tube and dikaryotic hyphae formation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
Mg2+
Mn2+
Co2+
-
in stimulation of Chs2 Co2+ is twice as effective on an enzyme activated by trypsin
Co2+
-
absolute requirement for a divalent cation. Mg2+, Mn2+ or Co2+
Co2+
-
divalent cation required, chitin synthase 2 shows highest activity with chitin synthase 2
Mg2+
-
low concentration of Mg2+ at 1.0-4.0 mmol/l significantly increase CHS activity, whereas 10.0 mmol/l or higher significantly inhibit CHS enzyme activity
Mg2+
-
greatly stimulated by Mg2+, optimal concentration is 2.5 mM, half-maximal activity at 17 mM
Mg2+
-
divalent cation required for maximal activity, Mg2+ is most efficient
Mg2+
-
best stimulator of Chs1. Mg2+ and Mn2+ lead to similar maximal stimulation of Chs2
Mg2+
-
absolute requirement for a divalent cation. Mg2+, Mn2+ or Co2+. Optimum concentration for Mg2+ is 1-10 mM
Mg2+
-
the best divalent cation stimulator of chitin synthase 1 and 2
Mg2+
-
divalent cation required, chitin synthase 1 and 3 have a preference for Mg2+
Mg2+
-
significant chitin synthase activity in the presence of Mg2+ or Mn2+, even without trypsin treatment
Mn2+
-
absolute requirement for a divalent cation. Mg2+, Mn2+ or Co2+
Mn2+
-
significant chitin synthase activity in the presence of Mg2+ or Mn2+, even without trypsin treatment
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R,4R,5R)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine
-
IC50: 1.6 mM
(2R,3R,4R,5S)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine
-
IC50: 38 mM
(2S,3R,4R,5R)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine
-
IC50: 4.0 mM
1-(2,2-dibutyl-5-(3,5-dimethylphenyl)-1,3,4-oxadiazol-3(2H)-yl)ethanone
-
0.25 mM, about 30% residual activity
1-[2,2-dibutyl-5-(2-chlorophenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
-
0.25 mM, about 10% residual activity
1-[2,2-dibutyl-5-(4-chlorophenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
-
0.25 mM, about 30% residual activity
1-[2,2-dibutyl-N-[(2,6-difluorophenyl)carbonyl]-5-(3,5-dimethylphenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
-
0.25 mM, about 20% residual activity
1-[2,2-dibutyl-N-[(2-chlorophenyl)carbonyl]-5-(2,4-dichlorophenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
-
0.25 mM, about 15% residual activity
1-[2,2-dibutyl-N-[(2-chlorophenyl)carbonyl]-5-(3,5-dimethylphenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
-
0.25 mM, about 25% residual activity
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N,N-dipropylacetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-(2-nitrophenyl)acetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-(3-nitrophenyl)acetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-(4-(trifluoromethyl)phenyl)acetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-(4-methoxyphenyl)acetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-(4-nitrophenyl)acetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-(ptolyl)acetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-methyl-N-phenylacetamide
-
-
-
2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)-N-phenylacetamide
-
-
-
3-(2-hydroxy-3-(methyl(2-oxo-2-(piperidin-1-yl)ethyl)amino)propyl)-1-methylquinazoline-2,4(1H,3H)-dione
-
-
-
5'-(N-succinyl)-5'-amino-5'-deoxyuridine methyl ester
-
inhibits the yeast enzyme, and exhibits synergistic interaction with caspofungin against Candida albicans
-
bis(5'-amino-5'-deoxyuridine) 2,2'-[(1,4-dioxobutane-1,4-diyl)diazanediyl]diacetate
-
50% inhibition at 3 mM
-
bis(5'-amino-5'-deoxyuridine) 4-[(carboxymethyl)amino]-4-oxobutanoate
-
-
-
kanakugiol
-
inhibition of chitin synthase 2 and antifungal activity of the lignan from the stem bark of Lindera erythrocarpa, overview
linderone
-
inhibition of chitin synthase 2 and antifungal activity of the lignan from the stem bark of Lindera erythrocarpa, overview
methyl 2-((2-(methyl(2-oxo-2H-chromen-4-yl)amino)ethoxy) (phenoxy)phosphorylamino)-3-phenylpropanoate}
-
-
-
methyl 2-((2-(methyl(2-oxo-2H-chromen-4-yl)amino)ethoxy) (phenoxy)phosphorylamino)acetate}
-
-
-
methyl 2-((2-(methyl(2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)propanoate}
-
-
-
methyl 2-((2-(methyl(6-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-3-phenylpropanoate}
-
-
-
methyl 2-((2-(methyl(6-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)acetate}
-
-
-
methyl 2-((2-(methyl(6-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)propanoate}
-
-
-
methyl 2-((2-(methyl(6-tert-buty-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-3-phenylpropanoate
-
a noncompetitive inhibitor against chitin synthase
-
methyl 2-((2-(methyl(6-tert-buty-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)acetate}
-
-
-
methyl 2-((2-(methyl(6-tert-buty-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)propanoate}
-
-
-
methyl 2-((2-(methyl(7-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-3-phenylpropanoate}
-
-
-
methyl 2-((2-(methyl(7-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-acetate}
-
-
-
methyl 2-((2-(methyl(7-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)propanoate}
-
-
-
methyl 2-((2-(methyl(8-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-3-phenylpropanoate}
-
-
-
methyl 2-((2-(methyl(8-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-acetate}
-
-
-
methyl 2-((2-(methyl(8-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)propanoate}
-
-
-
methyl 2-(2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)acetamido)benzoate
-
-
-
methyl 3-methyl-2-((2-(methyl(2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)butanoate}
-
-
-
methyl 3-methyl-2-((2-(methyl(6-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)butanoate}
-
-
-
methyl 3-methyl-2-((2-(methyl(6-tert-buty-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)butanoate}
-
-
-
methyl 3-methyl-2-((2-(methyl(7-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)butanoate}
-
-
-
methyl 3-methyl-2-((2-(methyl(8-methyl-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)butanoate}
-
-
-
methyllinderone
-
inhibition of chitin synthase 2 and antifungal activity of the lignan from the stem bark of Lindera erythrocarpa, overview
N,N-dibenzyl-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl) (methyl) amino)acetamide
-
-
-
N,N-diethyl-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl) (methyl) amino)acetamide
-
-
-
N- benzyl-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl) amino)acetamide
-
-
-
N-(2-chlorophenyl)-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)acetamide
-
-
-
N-(4-(cyanomethyl)phenyl)-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)acetamide
-
-
-
N-(4-chlorobenzyl)-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)acetamide
-
-
-
N-(4-chlorophenyl)-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)acetamide
-
-
-
N-(tert-butyl)-2-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl) amino)acetamide
-
-
-
[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-carbamic acid 2-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethylcarbamoyloxy]-ethyl ester
-
1 mM, 32% inhibition, competitive. IC50: 2.2 mM
[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-carbamic acid 2-{2-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethylcarbamoyloxy]-ethoxy}-ethyl ester
-
1 mM 45% inhibition. IC50: 11.8 mM
8,20-dihydroxy-9(11),13-abietadien-12-one
a diterpene compoud isolated from leaves of Chamaecyparis pisifera, inhibits Chs1p; a diterpene compoud isolated from leaves of Chamaecyparis pisifera, inhibits Chs2p
Mg2+
-
low concentration of Mg2+ at 1.0-4.0 mmol/l significantly increase CHS activity, whereas 10.0 mmol/l or higher significantly inhibit CHS enzyme activity
Ni2+
-
inhibition of chitin synthase 1 and 2, no inhibition of chitin synthase 3
Nikkomycin
Kluyveromyces bulgaricus
-
0.015 for chitin synthetase III; IC50: 0.022 mM for chitin synthetase II; IC50: 0.032 mM for chitin synthetase I
Nikkomycin
-
competitive; competitive inhibitor of chitin synthetase 2; nikkomycin X and nikkomycin Z; nikkomycin Z is more inhibitory to chitin synthetase 1 than for chitin synthetase 2
nikkomycin Z
exposure to nikkomycin Z, a CHS inhibitor, reduces the amount of chitin in the peritrophic membrane of molted larvae
nikkomycin Z
a chitin synthase inhibitor that downregulates the expression of BmChsA and decreases the amount of epidermis chitin during the molting process
nikkomycin Z
competitive inhibition, presence of inhibitor leads to increased expression; competitive inhibition, presence of inhibitor leads to increased expression
O-methyl pisiferic acid
a diterpene compound isolated from leaves of Chamaecyparis pisifera, inhibition of chitin synthase 1
O-methyl pisiferic acid
; a diterpene compound isolated from leaves of Chamaecyparis pisifera, specifically inhibits Chs2p in a mixed competitive manner versus UDP-N-acetyl-beta-D-glucosamine
Polyoxin D
-
competitive inhibitor of chitin synthetase 2; more inhibitory to chitin synthetase 1 than for chitin synthetase 2
uracil polyoxin C methyl ester
-
stereoselective synthesis routes of both the natural (C5'-S) and unnatural (C5'-R) diastereoisomers of uracil polyoxin C methyl ester as specific substrate analogue-inhibitors of chirin synthase, conjugation of the methyl ester of uracil polyoxin C with activated isoxazole carboxylic acids, detailed overview
uracil polyoxin C methyl ester
-
stereoselective synthesis routes of both the natural (C5'-S) and unnatural (C5'-R) diastereoisomers of uracil polyoxin C methyl ester as specific substrate analogue-inhibitors of chirin synthase, conjugation of the methyl ester of uracil polyoxin C with activated isoxazole carboxylic acids, detailed overview
additional information
-
purification of a soluble protein inhibitor from cytoplasm of Mucor rouxii, which forms part of the regulatory mechanism of chitin synthesis in the cells
-
additional information
-
no in vitro inhibition by polyoxin D. Inhibition of chitin synthesis by the chemicals is not due to direct inhibition of chitin synthase in Anopheles gambiae
-
additional information
-
synthesis and biological evaluation of phosphoramidate derivatives of coumarin as chitin synthase inhibitors and antifungal agents, overview
-
additional information
-
synthesis and biological evaluation of novel 3-substituted amino-4-hydroxylcoumarin derivatives as chitin synthase inhibitors and antifungal agents, overview. Most of the compounds have good inhibitory activity against CHS, in which the best compound with IC50 of 0.10 mmol/l has stronger activity than that of polyoxin B As far as the antifungal activity is concerned, most of the compounds possessed moderate to excellent activity against some representative pathogenic fungi. The most potent agent against Cryptococcus neoformans has a minimal inhibitory concentration (MIC) of 0.004 mg/ml. The compounds have negligible actions to some tested bacteria and are promising to develop selective antifungal agents
-
additional information
-
no inhibition by BAY SIR 8514; no inhibition by diflubenzuron
-
additional information
-
(2S,3R,4R,5S)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine shows no inhibition at 8 mM. 2,5-dideoxy-2,5-imino-L-iditol shows no inhibition at 5 mM
-
additional information
-
the absence of Chs4p renders CSIII functionally inactive, independently of Chs3p accumulation at the plasma membrane
-
additional information
-
no inhibition of chitin synthase 1 and 3 by methyllinderone, linderone, and kanakugiol from stem bark of Lindera erythrocarpa
-
additional information
-
design, synthesis and evaluation of 1-methyl-3-substituted quinazoline-2,4-dione derivatives as chitin synthase inhibitors and antifungal agents, NMR and mass spectrometry structure analysis, overview
-
additional information
-
no inhibition by BAY SIR 8514; no inhibition by diflubenzuron
-
additional information
-
a pH-dependent, heat-stable inhibitor is present in the soluble cytoplasm from the mycelium
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lysophosphatidylserine
-
required, phosphatidylserine and lysophosphatidylserine are the best activators
N-acetyl-alpha-D-glucosamine
-
stimulates CHS activity at 2.5 mM but inhibits enzyme activity at higher concentrations
N-acetyl-D-glucosamine
GlcNAc and 2-acylamido analogues of GlcNAc stimulate formation of chitin oligosaccharides by yeast chitin synthase, and GlcNAc is transferred to the 2-acylamido analogues. Synthesis of chitin oligosaccharides is strongly dependent on inclusion of GlcNAc in chitin synthase incubations. Formation of both chitin oligosaccharides and insoluble chitin is also stimulated by GlcNAc2
N-butanoyl-D-glucosamine
stimulates formation of both chitin oligosaccharides and insoluble chitin from the 2-acylamido analogues of UDP-N-acetyl-alpha-D-glucosamine
N-Glycolyl-D-glucosamine
stimulates formation of both chitin oligosaccharides and insoluble chitin from the 2-acylamido analogues of UDP-N-acetyl-alpha-D-glucosamine
N-propanoyl-D-glucosamine
stimulates formation of both chitin oligosaccharides and insoluble chitin from the 2-acylamido analogues of UDP-N-acetyl-alpha-D-glucosamine
-
Phospholipid
-
required, phosphatidylserine and lysophosphatidylserine are the best activators
proteinase B
-
from Saccharomyces cerevisiae, stimulates Chs1, no effect on Chs2
-
Staphylococcus V8 protease
-
best activator of Chs2 in presence of Co2+, elicits little Mg2+-stimulatable activity
-
ATP
-
0.25 mM activates by 33%, concentrations up to 0.5 mM stimulate
Digitonin
-
chitin synthase 2 is maximally stimulated at the sharply defined digitonin to protein ratio of 0.042. Chitin synthase I is maximally active at a digitonin to protein ratio of 0.3-0.75
Digitonin
-
stimulates, both membrane-bound and dissociated chitin synthase show little activity in the absence of digitonin
phosphatidylserine
-
required, phosphatidylserine and lysophosphatidylserine are the best activators
additional information
Chs2 is hyperactivated by a soluble yeast protease, addition of leupeptin, a serine and cysteine protease inhibitor, almost completely abolishes the stimulatory effect, while it does not affect the activity of Chs2 or Chs2DELTAN222 by itself
-
additional information
-
blockade of endocytosis, independent of Chs4p function, stops Chs3p internalization, triggering a significant increase in chitin synthesis, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
N-acetyl-D-glucosamine
-
reaction with UDP-N-acetyl-D-glucosamine
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
5-((2-amino-5-O-(aminocarbonyl)-2-deoxy-L-xylonoyl)amino)-1-(5-carboxy-3,4-dihydro-2,4-dioxo-1(2H)-pyrimidinyl)-1,5-dideoxy-beta-D-allofuranuronic acid
-
chitin synthetase 1
0.096
methyl 2-((2-(methyl(6-tert-buty-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-3-phenylpropanoate
-
pH 7.5, 37°C
-
0.005
O-methyl pisiferic acid
versus UDP-N-acetyl-beta-D-glucosamine; versus UDP-N-acetyl-beta-D-glucosamine
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
(2R,3R,4R,5R)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine
Saccharomyces cerevisiae
-
IC50: 1.6 mM
38
(2R,3R,4R,5S)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine
Saccharomyces cerevisiae
-
IC50: 38 mM
4
(2S,3R,4R,5R)-2-[(1-ethylphosphonyl)-1,1-difluoromethyl]-3,4-dihydroxy-5-hydroxymethyl-pyrrolidine
Saccharomyces cerevisiae
-
IC50: 4.0 mM
0.0079
1-[2,2-dibutyl-5-(2-chlorophenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
Saccharomyces cerevisiae
-
-
0.0056
1-[2,2-dibutyl-N-[(2-chlorophenyl)carbonyl]-5-(2,4-dichlorophenyl)-1,3,4-oxadiazol-3(2H)-yl]ethanone
Saccharomyces cerevisiae
-
-
0.8
5'-(N-succinyl)-5'-amino-5'-deoxyuridine methyl ester
Saccharomyces cerevisiae
-
pH 7.5, 25°C
-
0.08
methyl 2-((2-(methyl(6-tert-buty-2-oxo-2H-chromen-4-yl)amino)ethoxy)(phenoxy)phosphorylamino)-3-phenylpropanoate
Candida tropicalis
-
pH 7.5, 37°C
-
2.2
[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-carbamic acid 2-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethylcarbamoyloxy]-ethyl ester
Saccharomyces cerevisiae
-
1 mM, 32% inhibition, competitive. IC50: 2.2 mM
11.8
[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl]-carbamic acid 2-{2-[5-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethylcarbamoyloxy]-ethoxy}-ethyl ester
Saccharomyces cerevisiae
-
1 mM 45% inhibition. IC50: 11.8 mM
0.2264
8,20-dihydroxy-9(11),13-abietadien-12-one
Saccharomyces cerevisiae
A6ZKY2
inhibition of Chs2p
0.44
8,20-dihydroxy-9(11),13-abietadien-12-one
Saccharomyces cerevisiae
A6ZKY2
inhibition of Chs1p
0.18
Polyoxin B
Cryptococcus neoformans
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0025
Kluyveromyces bulgaricus
-
chitin synthetase III, activity at the end of exponential growth phase
0.0028
Kluyveromyces bulgaricus
-
chitin synthetase II, activity at the end of exponential growth phase
0.008
Kluyveromyces bulgaricus
-
chitin synthetase I, activity at the end of exponential growth phase
additional information
additional information
recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells
additional information
recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells
additional information
recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells
additional information
Q5A7T2
recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells; recombinant YFP-tagged isozymes in BWP17 cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
6.5
7.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
pH 6.5: about 85% of maximal activity, pH 8.5: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
28
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20°C: about 80% of maximal activity, 40°C: about 55% of maximal activity
25 - 50
-
25°C: about 60% of maximal activity, 50°C: about 90% of maximal activity, chitin synthase 1
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.04
6.4
8.05
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
-
substantial amounts of CHS-1 and CHS-2 RNA are present 4 to 8 hours after induction of cyst formation by glucose deprivation. In contrast to CHS-1 RNA, expression of CHS-2 RNA is more transient and no plateau is observed between 8 and 16 hours of encystation. Both CHS RNAs are no longer detectable after 48 hours when most of the cells are transformed into mature cysts
-
synthesis of chitin continues to take place in nematode eggs within the egg sac in the parasitic nematode. The removal of the activity affects egg development
early embryos contain large amounts of Bm-chs-1 transcripts, later stage embryos within the maternal uterus show little or no Bm-chs-1 transcripts
isoform IIIb appears to be involved exclusively in cell wall construction during haustorium development
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
Chlorovirus CVK2
-
the chitin synthase gene from chlorovirus CVK2 is expressed 10 min postinfection in Chlorella cells
-
enzyme predominantly localizes at polarized growth sites and between vesicles and metulae, between metulae and phialides, and between phalides and conidia in asexual development
-
enzyme predominantly localizes at polarized growth sites and between vesicles and metulae, between metulae and phialides, and between phalides and conidia in asexual development
additional information
-
Chs3p and Chs4p appear to co-localize at the neck region of the budding yeast
-
of midgut. The enzyme is restricted to the apical tips of microvilli
-
ChsA is localized in the plasma membrane of growing apices of hyphal branches, conidiophores, and falcate and oval conidia
-
enzyme predominantly localizes at polarized growth sites and between vesicles and metulae, between metulae and phialides, and between phalides and conidia in asexual development
-
ChsA is localized in the plasma membrane of growing apices of hyphal branches, conidiophores, and falcate and oval conidia
gene BmChsA is an epidermis-specific expressed gene during the molting stage, BmChsA gene in the epidermis of the head
-
CHS-A gene is exclusively expressed in the epidermis and related ectodermal cells such as tracheal cells
presence of alternative exons CHSA-2a and CHSA-2b. Transcripts of both exons are preferentially expressed in epidermis. During growth and development of Ostrinia furnacalis, CHSA-2a is mainly expressed during larval-larval molting and larval-pupal transformation, as well as in newly-laid eggs, while CHSA-2b is expressed only during the larval-larval molting
-
CHS-A gene is exclusively expressed in the epidermis and related ectodermal cells such as tracheal cells
chsB is ubiquitously expressed throughout the fungal body and quite indenpendently of the change in status of the cell
isoform IIIa is restricted to fungal infection structures growing on the surface of the plant, such as germ tubes and, predominantly, appressoria and may be involved in cell wall construction during germ tube and, particularly, appressoria development
-
expression of CHS-B gene is restricted to gut epithelial cells that produce chitin in the formation of the peritrophic matrix
-
expression of CHS-B gene is restricted to gut epithelial cells that produce chitin in the formation of the peritrophic matrix
CsmA is concentrated at hyphal tips and forming septa; CsmB is concentrated at hyphal tips and forming septa
-
localization to hyphal tips and forming septa during hyphal growth
-
ChsA is localized in the plasma membrane of growing apices of hyphal branches, conidiophores, and falcate and oval conidia
hyphal apex, septa, and Spitzenkoerper; hyphal apex, septa, and Spitzenkoerper
-
hyphal apex, septa, and Spitzenkoerper; hyphal apex, septa, and Spitzenkoerper
-
CHS2 is localized at the septum of yeast-like cells and hyphae; CHS3 is localized at the septum of yeast-like cells and hyphae; CHS4 is localized at the septum of yeast-like cells and hyphae; CHS5 is localized at the septum of yeast-like cells and hyphae; CHS6 is localized at the septum of yeast-like cells and hyphae; CHS7 is localized at the septum of yeast-like cells and hyphae
CHS is localized in the underlying epidermal cells of the integument and tracheal cells
gene BmChsA is an epidermis-specific expressed gene during the molting stage
distribution of CTLP1 and CHS2 in cryosections of the anterior midgut from fifth instar larvae, overview
larval, expression of MsCHS1 and MsCHS2. MsCHS1 appeared to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut; larval, expression of MsCHS1 and MsCHS2. MsCHS1 appeared to be inversely regulated because its mRNA is detectable only during the molt at the time when tracheal growth occurs at the basal site of the midgut
specific expression of chitin synthase B, constitutively in the midgut from the 3rd instar larval stage to prepupae reaching highest expression on the first day of the fifth instar larval stage, overview
chsC is moderately expressed in young vegetative mycelia, weak expression of chsC in old vegetative mycelium
-
the transcriptional level of gene Pochs1 in mycelia increases significantly by the temperature-downshift treatment, which is one of the important factors for inducing the onset of fruit-body formation
-
both two CHS genes, AgCHS1 and AgCHS2, are highly expressed in the pupal stage
-
CHS-A gene is exclusively expressed in the epidermis and related ectodermal cells such as tracheal cells
class A CHS is localized in the trachea and the underlying epidermal cells of the tracheal cells
-
CHS-A gene is exclusively expressed in the epidermis and related ectodermal cells such as tracheal cells
additional information
little expression in mature sexual structures
additional information
chsA is expressed specifically during asexual differentiation
additional information
chsA is expressed specifically during asexual differentiation
additional information
-
enzyme predominantly localizes at polarized growth sites and between vesicles and metulae, between metulae and phialides, and between phalides and conidia in asexual development
additional information
gene BmChsB expression profiles in the midgut during molting and the mulberry-leaf ingestion processes
additional information
semiquantitative RT-PCR expression analysis and expression pattern, overview
additional information
-
enzyme is transcribed in adult females, independent of their fertilization status, but is also expressed in males and microfilariae
additional information
enzyme is transcribed in adult females, independent of their fertilization status, but is also expressed in males and microfilariae
additional information
-
total specific activity is higher in hyphal form than in yeast form
additional information
the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis
additional information
the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis
additional information
the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis
additional information
Q5A7T2
the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis; the architecture of the chitin skeleton of Candida albicans is shaped by the action of more than one chitin synthase at the site of cell wall synthesis
additional information
-
chitin synthase expression during vegetative and pathogenic growth; chitin synthase expression during vegetative and pathogenic growth; chitin synthase isozymes of different classes are all expressed during vegetative and pathogenic growth
additional information
chitin synthase expression during vegetative and pathogenic growth; chitin synthase expression during vegetative and pathogenic growth; chitin synthase isozymes of different classes are all expressed during vegetative and pathogenic growth
additional information
chitin synthase expression during vegetative and pathogenic growth; chitin synthase expression during vegetative and pathogenic growth; chitin synthase isozymes of different classes are all expressed during vegetative and pathogenic growth
additional information
-
stage-specific expression of the chitin synthase DmeChSA and DmeChSB genes during the onset of metamorphosis
additional information
-
genes corresponding to CHS-1 and CHS-2 are not expressed in Entamoeba trophozoites
additional information
-
genes corresponding to CHS-1 and CHS-2 are not expressed in Entamoeba trophozoites
additional information
-
genes corresponding to CHS-1 and CHS-2 are not expressed in Entamoeba trophozoites
additional information
Lucilia sp.
-
GlcNAc acceptors functioning as primers for chain assembly transcripts are detectable in all developmental stages of the fly
additional information
-
suncellular localization study of CHS-3, CHS proteins are delivered to the cell surface via an alternative route distinct from the classical ER-Golgi body secretory pathway, overview; suncellular localization study of CHS-6, CHS proteins are delivered to the cell surface via an alternative route distinct from the classical ER-Golgi body secretory pathway, overview
additional information
suncellular localization study of CHS-3, CHS proteins are delivered to the cell surface via an alternative route distinct from the classical ER-Golgi body secretory pathway, overview; suncellular localization study of CHS-6, CHS proteins are delivered to the cell surface via an alternative route distinct from the classical ER-Golgi body secretory pathway, overview
additional information
-
suncellular localization study of CHS-3, CHS proteins are delivered to the cell surface via an alternative route distinct from the classical ER-Golgi body secretory pathway, overview; suncellular localization study of CHS-6, CHS proteins are delivered to the cell surface via an alternative route distinct from the classical ER-Golgi body secretory pathway, overview
-
additional information
-
growth and conidia production of wild-type and disruption mutant strains, and relative expression of chs genes in Penicillium digitatum strain CECT20796 under different growth conditions, overview
additional information
growth and conidia production of wild-type and disruption mutant strains, and relative expression of chs genes in Penicillium digitatum strain CECT20796 under different growth conditions, overview
additional information
-
growth and conidia production of wild-type and disruption mutant strains, and relative expression of chs genes in Penicillium digitatum strain CECT20796 under different growth conditions, overview
-
additional information
-
the transcriptional level of Pochs1 is higher in the stage of immature fruit body than in the stages of mycelia and mature fruit body
additional information
-
chitin synthase II shows highest specific activities in extracts from logarithmically growing cultures. Chitin synthetase I, whether from growing cultures or stationary phase cultures, is only measurable after trypsin treatment, and levels of zymogen do not change
additional information
-
level of chitin synthase 1 remains constant during vegetative growth in synchronised cells
additional information
expression, localization and degradation of Chs2 are cell cycle dependent
additional information
-
expression, localization and degradation of Chs2 are cell cycle dependent
-
additional information
CHSB is not expressed in the cuticle, fat body, tracheae, and the Malpighian tubules, CHSB tissue distribution and developmental expression, overview
additional information
developmental expression and tissue distribution of CHSA, CHSA mRNA is highly expressed in the early and late stages of each larval instar, and consistently expressed in high level during the pupal stage, CHS is further localized in the underlying epidermal cells of the integument and tracheal cells, but not in the fat body or Malpighian tubules, overview
additional information
gene TcCHS-A expression during embryonic and adult development, overview; gene TcCHS-B expression during embryonic and adult development, overview
additional information
gene TcCHS-A expression during embryonic and adult development, overview; gene TcCHS-B expression during embryonic and adult development, overview
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
additional information
CHS6 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth; CHS7 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
CsmA tagged with 9*HA epitopes is localized near actin structures at the hyphal tips and septation sites. Its myosin motor-like domain is able to bind to actin. Interaction between the myosin motor-like domain and actin is not only necessary for the proper localization of CsmA, but also for CsmA function
-
the enzyme is restricted to the apical tips of microvilli from columnar cells
additional information
-
ChsA is localized in nascent septa, and during septum conversion to an end wall after hyphal breakage
; developing septa; developing septa; developing septa; developing septa; developing septa
-
; developing septa; developing septa; developing septa; developing septa; developing septa
-
CHS2 is localized at the septum of yeast-like cells and hyphae; CHS3 is localized at the septum of yeast-like cells and hyphae; CHS4 is localized at the septum of yeast-like cells and hyphae; CHS5 is localized at the septum of yeast-like cells and hyphae; CHS6 is localized at the septum of yeast-like cells and hyphae; CHS7 is localized at the septum of yeast-like cells and hyphae
ChsA and ChsC transiently exist at the septation sites during and shortly after septum formation. Their localizations are not identical but partly overlapp at the septation sites; ChsA and ChsC transiently exist at the septation sites during and shortly after septum formation. Their localizations are not identical but partly overlapp at the septation sites
-
ChsA is localized in nascent septa, and during septum conversion to an end wall after hyphal breakage
localizes in regions of cell wall growth in an actin dependent fashion. In unbudded, stationary-phase cells incubated at 37°C Chs5 is found in a punctuate fashion just under the cell wall surface. In contrast in yeast cells with smaller buds, Chs5 is mostly localized at the bud apex, whereas in cells with larger buds Chs5 is spread more widely toward the mother cell and less infrequently localized to a septal region in the mother-bud neck when both are approximately equal size, presumably just before or concomitantly with cytokinesis
-
chitin synthase 1 and 2; the culture medium affects the relative abundance of chitin synthase 1 in chitosomes and plasma membrane populations
expression of recombinant protein leads to puncta structures co-localized with the Golgi marker
-
membrane-bound vesicle, Chs3p is present in an active form
-
transmembrane protein, the insect chitin synthase contains multiple transmembrane helices reflecting their association with either the plasma membrane or intracellular vesicles such as chitosomes
assembly mechanism of the chitin synthase Ar-CS1 via its extracellular domain ArCS1_E22
transmembrane CHS2 with an extracellular C-terminal domain
integral, analysis of the transmembrane helices of CHSA
-
ChsA is localized in the plasma membrane of growing apices of hyphal branches, conidiophores, and falcate and oval conidia
-
chitin synthase 1 and 2; the culture medium affects the relative abundance of chitin synthase 1 in chitosomes and plasma membrane populations
-
chitin synthase III requires Chs4p-dependent translocation of Chs3p into the plasma membrane, Chs4p thus promotes Chs3p translocation into the plasma membrane in a stable and active form. In the absence of Chs4p, Chs3p is delivered to the plasma membrane but fails to accumulate there because it is rapidly endocytosed and accumulates in intracellular vesicles. The C-terminal region of Chs4p is required for its association with plasma membrane but not for biological function
core; core; core; core; core; core, isozyme CHS-2-GFP seems to occupy a smaller area at the Spk than the rest of the CHS isozymes
-
core; core; core; core; core; core, isozyme CHS-2-GFP seems to occupy a smaller area at the Spk than the rest of the CHS isozymes
-
additional information
-
the enzyme is mainly associated with the mixed membrane fraction
-
additional information
-
ChsA is localized in growing tips of multiple cell types
-
additional information
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
additional information
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
additional information
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
additional information
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
additional information
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
additional information
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
additional information
-
cellular distribution, analysis using fluorescent-labeled enzyme; cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and cell septa, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs, cellular distribution, analysis using fluorescent-labeled enzyme; isozymes CHS-5 and CHS-2 show a different pattern of localization than the other CHSs. Isozyme CHS-1 partially colocalizes with isozymes CHS-2 and CHS-5 at the spitzenkoerper and septa, cellular distribution, analysis using fluorescent-labeled enzyme
-
-
additional information
-
the enzyme is mainly associated with the mixed membrane fraction
-
additional information
-
the culture medium affects the relative abundance of chitin synthase 1 in chitosomes and plasma membrane populations
-
additional information
-
Chs4p is transported in vesicles in a polarized fashion independently of the other Chs proteins. Its association with membranes depends not only on prenylation, but also on its interaction with other proteins, mainly Chs3p, which is the catalytic subunit of CSIII and is able to properly direct Chs4p to the bud neck in the absence of prenylation
-
additional information
-
the enzyme sediments with membranous components of high specific gravity
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13500
x * 21500, recombinant transmembrane segment ArCS1_E22, x * 13500, recombinant transmembrane segment ArCS1_E22, SDS-PAGE
21500
x * 21500, recombinant transmembrane segment ArCS1_E22, x * 13500, recombinant transmembrane segment ArCS1_E22, SDS-PAGE
67000
-
x * 67000, reversible aggregation into large multimolecular units, SDS-PAGE
73000
114000
additional information
size analysis of proteins purified at pH 4.7, pH 6.5, and pH 7.5 by using gel filtration, native PAGE, and dynamic light scattering
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
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x * 174500, calculated, x * 190000 + x * 119000 + x * 60000, SDS-PAGE
polymer
additional information
?
x * 21500, recombinant transmembrane segment ArCS1_E22, x * 13500, recombinant transmembrane segment ArCS1_E22, SDS-PAGE
polymer
-
x * 67000, reversible aggregation into large multimolecular units, SDS-PAGE
additional information
assembly mechanism of the chitin synthase Ar-CS1 via its extracellular domain ArCS1_E22. ArCS1_E22 forms regular nanostructures on cationic substrates, atomic force microscopy
additional information
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class V CHS isozyme contains an N-terminal myosin-like motor domain
additional information
class V CHS isozyme contains an N-terminal myosin-like motor domain
additional information
class V CHS isozyme contains an N-terminal myosin-like motor domain
additional information
LeChs1 contains a myosin motor-like domain, domain structure of LeChs1, overview
additional information
isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
additional information
isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
additional information
isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
additional information
isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
additional information
isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
additional information
isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
additional information
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isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview; isozyme chitin synthase 1 domain structure, overview
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additional information
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in SDS-PAGE, the purified enzyme shows a major band of 63000 Da and a weaker band at 74000 Da
additional information
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the C-terminal region of Chs4p is required for its association with plasma membrane but not for biological function
additional information
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INN1 protein, which is required for ingreesion, associates with isoform CHS2 in cell extracts, and interacts with the amino terminal part of isoform CHS2 carrying the catalytic domain
additional information
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SDS-PAGE results in 19 bands from 27000 Da to 125000 Da. Five of them show intensities that parallele the chitin synthase activity: 83000 Da, 72000 Da, 67000 Da, 36000 Da and 31000 Da
additional information
isoform Chs1 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis; isoform Chs2 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis
additional information
isoform Chs1 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis; isoform Chs2 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis
additional information
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isoform Chs1 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis; isoform Chs2 protein contains N-terminal microtubule interacting and trafficking domains involved in protein recycling by endocytosis
additional information
SeCHSB has an N-terminal domain with several membrane-spanning regions, a central domain that shares high sequence identity among different insects, and a C-terminal domain with additional transmembrane regions characteristic of glycosyltransferase family 2 enzymes
additional information
protein consists of a myosin motor domain fused to a membrane-spanning chitin synthase region. Both domains are required for fungal virulence. Fungi carrying mutations in the chitin synthase domain are rapidly recognized and killed by the plant, whereas fungi carrying a deletion of the motor domain show alterations in cell wall composition but can invade host tissue and cause a moderate plant response
additional information
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protein consists of a myosin motor domain fused to a membrane-spanning chitin synthase region. Both domains are required for fungal virulence. Fungi carrying mutations in the chitin synthase domain are rapidly recognized and killed by the plant, whereas fungi carrying a deletion of the motor domain show alterations in cell wall composition but can invade host tissue and cause a moderate plant response
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
proteolytic modification
side-chain modification
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prenylation of CSIII components is involved in proper subcellular localization of the enzyme, overview
glycoprotein
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purified chitin synthase complex can be stained with Calcofluor White suggesting that it is either glycosylated, or still associated with chitin fibrils
phosphoprotein
phosphorylation site mapping, Chs2 contains twelve phosphorylation sites, all in the N-terminal domain, phosphorylation of the N-terminal domain is important for Chs2 stability, these sites might play an important role in the cell cycle-dependent degradation of the enzyme, and thus in cell division
phosphoprotein
-
phosphorylation site mapping, Chs2 contains twelve phosphorylation sites, all in the N-terminal domain, phosphorylation of the N-terminal domain is important for Chs2 stability, these sites might play an important role in the cell cycle-dependent degradation of the enzyme, and thus in cell division
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proteolytic modification
-
activity increases up to 20times by digestion with trypsin
proteolytic modification
-
enzyme exists in the zymogenic form and requires proteolytic activation
proteolytic modification
-
activity can be increased 6fold by digestion of the enzyme preparation with trypsin
proteolytic modification
-
enzyme exists as a zymogen and requires proteolytic activation
proteolytic modification
-
preincubation with trypsin results in approximately 4fold increase in activity
proteolytic modification
-
enzyme exists chiefly in a zymogenic form. Endogenous activation of chitin synthase zymogen is observed over many days in preparations stored in glycerol, 33% w/v at -12°C and over many hours in preparations stored at 30°C The zymogen is preferentially retarded on the column matrices in comparison with the active enzyme
proteolytic modification
-
activated by acid proteases, slightly activated by trypsin, inhibited by neutral proteases; activated by all proteases
proteolytic modification
-
the activity of chitin synthase 3 is not potentated by controlled proteolysis
proteolytic modification
affinity-purified enzyme requires protease treatment to give rise to enzyme activity
proteolytic modification
-
following treatment with trypsin, the chitin synthase activity is increased by 6fold, indicating that most of the chitin synthase activity is zymogenic
proteolytic modification
-
pronase and proteinase K stimulates both Chs1 and Chs2. Proteinase B from Saccharomyces cerevisiae stimulates Chs1 and has no effect on Chs2, Staphylococcus V8 protease is the best activator of Chs2 in presence of Co2+, elicits little Mg2+-stimulatable activity
proteolytic modification
-
enzyme is present in the cell in a zymogen form
proteolytic modification
-
chitin synthetase zymogen is activated by proteinase B
proteolytic modification
-
chitin synthetase 2 is not activated by proteolysis; chitin synthetase I exists as zymogen and is only measurable after trypsin treatment
proteolytic modification
-
several proteases, including trypsin and chymotrypsin activate chitin synthase 1 and 2. Chitin synthase 3 requires the presence of substrate during protease treatment in order to be activated to some extent
proteolytic modification
-
chitin synthase 2 activity is independent of the N-terminal 193 amino acid truncation, because partially purified full length enzyme also exhibits the activity without trypsin treatment in the presence of appropriate cations
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Mortierella pusilla
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activity increases during low temperature storage
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high sensitivity of chitosomal chitin synthase 2 to high centrifugal forces
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treatment with digitonin causes an increase in specific activity and stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, digitonin-solubilized enzyme is stable for several months, purified enzyme is stable for at least a few weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
partial purification of recombinant Chs2 from Pichia pastoris membranes by nickel affinity chromatography
recombinant His-tagged enzyme fragment by nickel affinity chromatography
recombinant His-tagged transmembrane protein ArCS1_E22TM from Dictyostelium discoideum by nickel affinity chromatography, soluble recombinant ArCS1_E22 proteins can be purified as monomers only at basic pH of 9.0
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and expression of class I CHS isozyme; cloning and expression of class III CHS isozyme; cloning and expression of class IV and V CHS isozymes
cloning from anterior midguts of fifth instar larvae, expression in Saccharomyces cerevisiae AH109 cells and protein interaction analysis by yeast two hybrid screening, identifying a chymotrypsin-like protease CTLP1 that binds to the extracellular carboxyterminal domain of CHS2
comparative sequence analysis, cloning and expression of the enzyme's transmembrane segment ArCS1_E22TM, recombinant expression of the His-tagged domain in Dictyostelium discoideum, the corresponding transmembrane protein ArCS1_E22TM accumulates in membrane fractions of the expression host Dictyostelium discoideum, recombinant expression of clone EIIIab containing the ArCS1_E22 cDNA fragment in Escherichia coli strain BL21(DE3)
expressed in Saccharomyces cerevisiae using the GAL1 promoter in a multicopy plasmid
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expression in Escherichia coli
expression of a 12 kDa Myo12p epitope located in the C-terminal end of the N-terminal myosin motorlike domain with a P-loop and use for generation of antibodies
expression of Chs4p-GFP and Chs3p-GFP in CRM233 and CRM103 strains, respectively
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gene BcChs6, cloning in Escherichia coli strain DH5alpha, Agrobacterium-mediated transformation of Bortrytis cinerea spores for gene disruption
gene BmChsA, semiquantitative RT-PCR expression analysis, expression pattern
gene BmChsB, DNA and amino acid sequence determination and analysis, seqeunce comparisons, quantitative expression analysis and expression profile
gene chs-3, DNA and amino acid sequence determination and analysis, expression of GFP-labeled CHS-3 in hyphae and subcellular localization, overview; gene chs-6, DNA and amino acid sequence determination and analysis, expression of GFP-labeled CHS-6 in hyphae and subcellular localization, overview
gene CHS1, expression of YFP-tagged wild-type and mutant isozymes in strain BWP17, location of the YFP-tagged Chs proteins in yeast and hyphal cells, overview; gene CHS2, expression of YFP-tagged wild-type and mutant isozymes in strain BWP17, location of the YFP-tagged Chs proteins in yeast and hyphal cells, overview; gene CHS3, expression of YFP-tagged wild-type and mutant isozymes in strain BWP17, location of the YFP-tagged Chs proteins in yeast and hyphal cells, overview; gene CHS8, expression of YFP-tagged wild-type and mutant isozymes in strain BWP17, location of the YFP-tagged Chs proteins in yeast and hyphal cells, overview
gene chs2, DNA and amino acid sequence determination and analysis; gene chs2, DNA and amino acid sequence determination and analysis
gene CHSA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of a fragment comprising base pairs 2040-2495 as His-tagged protein
gene CHSB, DNA and amino acid sequence determination and analysis, genetic structure,phylogenetic analysis, expression analysis, sequence comparisons
gene chsVII, phylogenetic analysis, quantitative RT-PCR enzyme expression analyis
gene Lechs1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic structure, expression in Escherichia coli strain JM109
gene Pochs1, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative expression analysis
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genes CHS1-4, phylogenetic tree, expression of deeltion mutants, quantitative expression analysis by RT-PCR
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high level expression of wild-type Chs2 and a mutant Chs2DELTAN222 lacking the N-terminal region in Escherichia coli strain C41 and in Pichia pastoris strain SMD1163 membranes in an active form, the latter system results in higher enzyme activity, overview
myosin motor-like chitin synthase gene chsVb, DNA and amino acid sequence determination and analysis, expression analysis, phylogenetic tree and analysis
overexpression of CHS2p isozyme in Saccharomyces cerevisiae strains; overexpression of CHS isozymes in Saccharomyces cerevisiae strains
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since chitin synthase 2 can not expressed in bacterial cells or insect cells in an active form, Saccharomyces cerevisiae is used as the host for overexpression
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the entire region of csmB cDNA is cloned by 5' and 3' RACE methods
WdChs5p-myc protein has a differential expression feature that is similar to the differential transcription of the WdCHS5 gene, transcriptional regulation is the first and probably the most important control point of the expression ofWdCHS5, overview, expression of wild-type and myc-tagged enzyme in Escherichia coli strain DH5alpha, expression of WdChs5p-myc protein in Wangiella dermatitidis, expression patterns, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CHS7 transcription is strongly induced on germination of spores, and a tagged Chs7 protein is produced abundantly during infection-related morphogenesis
decrease in transcription under higher osmotic conditions, e.g., in the presence of 0.3 M KCl; decrease in transcription under higher osmotic conditions, e.g., in the presence of 0.3 M KCl; low glucose concentrations of 0.05% instead of 3% provoke a derepression of transcription. Oxidative stress due to mycelial growth in presence of 5 mM H2O2, induces higher transcription levels; low glucose concentrations of 0.05% instead of3% provoke a derepression of transcription. Oxidative stress due to mycelial growth in presence of 5 mM H2O2, induces higher transcription levels
exogenous 20-hydroxyecdysone and methoprene, a juvenile hormone analogue, significantly upregulate the expression of BmChsB when the levels of endogenous molting hormone are low and the levels of endogenous juvenile hormone are high immediately after molting. When levels of endogenous molting hormone are high and those of endogenous juvenile hormone are low during the molting stage, exogenous 20-hydroxyecdyson does not upregulate BmChsB expression and exogenous methoprene upregulates it negligibly. When the endogenous hormone levels are low during the mulberry-leaf intake process, BmChsB expression is upregulated by exogenous methoprene
exogenous hormones, 20-hydroxyecdysone and methoprene, significantly upregulate the expression of gene BmChsA at low levels of endogenous molting hormone and high levels of endogenous juvenile hormone immediately after molting. With low levels of endogenous hormones during the mulberry intake process, BmChsA is rarely upregulated by exogenous hormones. With high levels of endogenous molting hormone and low levels of endogenous juvenile hormone during the molting stage, upregulation of gene BmChsA by exogenous hormones is not detected
nikkomycin Z, a chitin synthase inhibitor, downregulates the expression of BmChsA and decreases the amount of epidermis chitin during the molting process
presence of alternative exons CHSA-2a and CHSA-2b. Transcripts of both exons are preferentially expressed in epidermis. During growth and development of Ostrinia furnacalis, CHSA-2a is mainly expressed during larval-larval molting and larval-pupal transformation, as well as in newly-laid eggs, while CHSA-2b is expressed only during the larval-larval molting
the transcription level is relatively constant at the 4th instar stage but decreases between the 4th and the 5th instar molting time, with gradually increase throughout the 5th instar. Transcription level drops dramatically when the feeding ceases at the 6th day of the 5th instar. At the larval-pupal molting time, only minor amounts of transcripts can be detected. During the pupal stages, the transcription level increases at the 3rd day and then drops at the 4th day, suggesting that the enzyme might be involved in tissue reconstruction during the pupa-adult metamorphosis
treatment of Candida albicans with low levels of echinocandins such as caspofungin, echinocandin B, cilofungin and anidulafungin stimulates chitin synthase gene expression, increases Chs activity, elevates chitin content and reduced efficacy of these drugs
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V377I
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enhanced emzymic activity in vitro. Mutation suppresses mutations in the C2 domain of INN1 protein, which is required for ingression
additional information
additional information
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expression of the central domain of chitin synthase isoform 3a, i.e. Spsa GntI Core, as inclusion bodies in Escherichia coli. The fragment does not show chitin synthase activity but shows specific binding for the substrate UDP-GlcNAc with a dissociation constant similar to the Michaelis constant, and a major contribution of the uracil moiety for recognition is confirmed
additional information
the gene is disrupted through Agrobacterium tumefaciens-mediated transformation
additional information
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the gene is disrupted through Agrobacterium tumefaciens-mediated transformation
-
additional information
construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview
additional information
construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview
additional information
construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview
additional information
Q5A7T2
construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview; construction of isozyme deficient mutant cells, analysis of chitin ghosts of chs mutant strains by shadow-cast transmission electron microscopy show that the long-chitin microfibrils are absent in chs8 mutants and the short-chitin rodlets are absent in chs3 mutants. The inferred site of chitin microfibril synthesis of these Chs enzymes is corroborated by their localization determined in Chsp-YFP-expressing strains, overview
additional information
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construction of null mutants of CHS V isozyme, which shows srongly impaired vegetative growth and pathogenicity, CHS class V mutants do not develop macroscopically visible anthracnose disease symptoms and are nonpathogenic, phenotype, overview; mutants of class III isozyme do not differ from the wild-type isozyme; mutants of class I isozyme do not differ from the wild-type isozyme
additional information
construction of null mutants of CHS V isozyme, which shows srongly impaired vegetative growth and pathogenicity, CHS class V mutants do not develop macroscopically visible anthracnose disease symptoms and are nonpathogenic, phenotype, overview; mutants of class III isozyme do not differ from the wild-type isozyme; mutants of class I isozyme do not differ from the wild-type isozyme
additional information
construction of null mutants of CHS V isozyme, which shows srongly impaired vegetative growth and pathogenicity, CHS class V mutants do not develop macroscopically visible anthracnose disease symptoms and are nonpathogenic, phenotype, overview; mutants of class III isozyme do not differ from the wild-type isozyme; mutants of class I isozyme do not differ from the wild-type isozyme
additional information
expression of a 12 kDa Myo12p epitope located in the C-terminal end of the N-terminal myosin motorlike domain with a P-loop, and use for generation of antibodies
additional information
targeted disrupted single DELTAchsVb and double DELTAchsVDELTAchsVb mutants are unable to infect and colonize tomato plants or grow invasively on tomato fruit tissue, the strains are hypersensitive to compounds that interfere with fungal cell wall assembly, produce lemon-like shaped conidia, and show swollen balloon-like structures in hyphal subapical regions, thickened walls, aberrant septa, and intrahyphal hyphae, phenotypes, overview
additional information
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
additional information
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
additional information
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
additional information
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
additional information
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
additional information
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
additional information
-
construction of a deletion mutant of isozyme CHS-1; construction of a deletion mutant of isozyme CHS-2; construction of a deletion mutant of isozyme CHS-3; construction of a deletion mutant of isozyme CHS-4; construction of a deletion mutant of isozyme CHS-5; construction of a deletion mutant of isozyme CHS-6
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additional information
determination and analysis of the polymorphism patterns of the class II chitin synthase gene chs2, sequence tree, detailed overview; determination and analysis of the polymorphism patterns of the class II chitin synthase gene chs2, sequence tree, detailed overview
additional information
determination and analysis of the polymorphism patterns of the class II chitin synthase gene chs2, sequence tree, detailed overview; determination and analysis of the polymorphism patterns of the class II chitin synthase gene chs2, sequence tree, detailed overview
additional information
functional expression in a Saccharomyces cerevisiae chs3 null mutant results in an increase in total chitin synthase activity and in chitin content in its cell wall
additional information
-
functional expression in a Saccharomyces cerevisiae chs3 null mutant results in an increase in total chitin synthase activity and in chitin content in its cell wall
additional information
-
disruption of the gene coding PdChsVII, which contains a short version of a myosin motor domain, has been achieved by using Agrobacterium tumefaciens strain AGL-1-mediated transformation, morphological changes and chitin content in Penicillium digitatum PdchsVII disruption strains, overview
additional information
disruption of the gene coding PdChsVII, which contains a short version of a myosin motor domain, has been achieved by using Agrobacterium tumefaciens strain AGL-1-mediated transformation, morphological changes and chitin content in Penicillium digitatum PdchsVII disruption strains, overview
additional information
-
disruption of the gene coding PdChsVII, which contains a short version of a myosin motor domain, has been achieved by using Agrobacterium tumefaciens strain AGL-1-mediated transformation, morphological changes and chitin content in Penicillium digitatum PdchsVII disruption strains, overview
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additional information
construction of a Chs2 mutant Chs2DELTAN222 lacking the N-terminal region
additional information
screening for mutations synthetically lethal with chs3 in the indicator strain ECY46-4-1B, the thin cell wall phenotype is caused by a mutation of the Cdc28-activating kinase CAK1 gene, phenotype, reduced or increased CSIII activity, overview
additional information
-
mutations in isoform CHS2 may suppress mutations in the C2 domain of INN1 protein, which is required for ingression. The dominant CHS2 alleles also suppress cytokinesis defects produced by lack of the Cyk3 protein
additional information
-
construction of a Chs2 mutant Chs2DELTAN222 lacking the N-terminal region
-
additional information
recombinant protein does not show in vitro activity
additional information
recombinant protein does not show in vitro activity
additional information
-
recombinant protein does not show in vitro activity
additional information
disruption of Spodoptera exigua larval development by silencing chitin synthase gene A with RNA interference, injection of synthesized dsRNA/siRNA into the 4th instar larvae, resulting in cuticles that are disordered and epithelial walls of larval trachea that do not expand uniformly in injected individuals, phenotype, overview
additional information
adults treated with dsRNA for TcCHS-B exhibit little or no chitin in their PM and die about 2 weeks after injection, none of the TcCHS-B-treated females oviposite, which is probably a secondary effect caused by starvation, overview; when dsRNA for gene TcCHS-A is injected into male or female pharate adults, all insects die 5-7 d after the adult molt, and the females fail to oviposit prior to death, when dsTcCHS-A is injected into young adults 1-2 d post-eclosion, a similar lethal phenotype is obtained after 5 d and no oviposition occurs, when dsTcCHS-A injections are delayed until after adult maturation 7-10 d post-eclosion, the treated females do oviposit and the resulting embryos appear to develop normally, however, the chitin content of the eggs is dramatically reduced, the embryos became twisted and enlarged, and the eggs do not hatch, overview
additional information
adults treated with dsRNA for TcCHS-B exhibit little or no chitin in their PM and die about 2 weeks after injection, none of the TcCHS-B-treated females oviposite, which is probably a secondary effect caused by starvation, overview; when dsRNA for gene TcCHS-A is injected into male or female pharate adults, all insects die 5-7 d after the adult molt, and the females fail to oviposit prior to death, when dsTcCHS-A is injected into young adults 1-2 d post-eclosion, a similar lethal phenotype is obtained after 5 d and no oviposition occurs, when dsTcCHS-A injections are delayed until after adult maturation 7-10 d post-eclosion, the treated females do oviposit and the resulting embryos appear to develop normally, however, the chitin content of the eggs is dramatically reduced, the embryos became twisted and enlarged, and the eggs do not hatch, overview
additional information
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construction of deletion mutants of the 4 isozymes CHS1-CHS4, phenotypes, overview
additional information
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construction of deletion mutants of the 4 isozymes CHS1-CHS4, phenotypes, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
the chs3 gene encoding the chitin synthase 3 is used for synthetically lethality screening for mutation determination, overview
agriculture
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enzyme inhibitors can be useful as potential pesticidal agents
agriculture
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enzyme inhibitors can be useful as potential pesticidal agents
agriculture
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gene disruption mutant is not significantly affected in either growth characteristics or pathogenicity on tomato leaves. Mutant exhibits a 31% increase in its chitin content and displays increased sensitivity to Caclofluor White and slightly enhanced tolerance to cell-wall disturbing substances and osmosis regulators
agriculture
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specific disruption of the CHS1 gene results in a 58% reduction of chitin synthase activity, accompanied by decreases of 35% in chitin content, 22% in conidiation, and 16% in macroconidium length. The mutant displays significantly reduced pathogenicity on wheat spikes and seedlings
agriculture
enzyme deletion mutants are unable to form appressoria on artificial surfaces, except following the application of the exogenous inducers 1,16-hexadecanediol and cyclic adenosine monophosphate. Mutants are significantly reduced in their ability to enter rice plants, but growth in planta is not affected
LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.16)
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