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Information on EC 2.4.1.16 - chitin synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P14180
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2.4.1.16 chitin synthaseIUBMB Comments
Converts UDP-N-acetyl-alpha-D-glucosamine into chitin and UDP.
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Word Map
- 2.4.1.16
- synthases
- candida
- albicans
- nikkomycins
- conidia
- hyphal
- septum
- colletotrichum
- chitinase
-
calcofluor
- cuticle
- polyoxins
- mycelial
- dextrose
-
molt
-
anthracnose
-
hyaline
-
peritrophic
-
weir
- integument
-
exoskeleton
-
echinocandins
- trichophyton
- gloeosporioides
- dermatophytes
- fructicola
- diflubenzuron
- siamense
-
re-isolated
- rouxii
- appressoria
-
rinsed
- caspofungin
-
acervuli
- conidiophore
- dermatitidis
- malassezia
- mentagrophytes
- arthroderma
-
single-spore
-
cottony
- exophiala
-
sunken
-
mother-bud
-
obtuse
- phycomyces
- naclo
-
tetranychus
- dermatophytosis
-
smooth-walled
- analysis
- agriculture
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
chitin synthase, chitin synthetase, chs3p, chitin synthase 1, chitin synthase iii, chitin synthase 2, csiii, chs4p, chs2p, chitin synthase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminyltransferase, chitin-uridine diphosphate
-
-
-
-
chitin synthase 2
chitin synthase III
chitin synthetase
-
-
-
-
chitin-UDP N-acetylglucosaminyltransferase
-
-
-
-
chitin-uridine diphosphate acetylglucosaminyltransferase
-
-
-
-
Chs1
-
-
-
-
Chs2
CHS2p
Chs3p
CSI
-
-
-
-
CSII
-
-
-
-
CSIII
trans-N-acetylglucosaminosylase
-
-
-
-
Chs2
-
-
-
-
CSIII
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + [(1->4)-N-acetyl-beta-D-glucosaminyl]n = UDP + [(1->4)-N-acetyl-beta-D-glucosaminyl]n+1
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9030-18-6
-
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
UDP-N-acetyl-alpha-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
-
-
?
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-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-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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
proper CSIII turnover is maintained through the endocytic internalization of Chs3p, overview
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
-
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
-
-
?
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
?
-
-
Chs4p is required for chitin synthase III activity and hence for chitin synthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Co2+
-
divalent cation required, chitin synthase 2 shows highest activity with chitin synthase 2
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+
Mg2+
-
the best divalent cation stimulator of chitin synthase 1 and 2
Mg2+
-
significant chitin synthase activity in the presence of Mg2+ or Mn2+, even without trypsin treatment
Mg2+
-
divalent cation required, chitin synthase 1 and 3 have a preference for Mg2+
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
Mn2+
-
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+
INHIBITOR
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-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetyl)pyrrolidine-2-carboxylic acid
-
75.5% inhibition at 0.3 mg/ml
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
-
-
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)-3-(4-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetoxy)phenyl)propanoic acid
-
65.3% inhibition at 0.3 mg/ml
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)-3-phenylpropanoic acid
-
-
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)-4-(methylthio)butanoic acid
-
-
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)acetic acid
-
-
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)butanoic acid
-
-
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)propanoic acid
-
-
3-(1H-imidazol-5-yl)-2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)propanoic acid
-
61.5% inhibition at 0.3 mg/ml
3-(1H-indol-3-yl)-2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)propanoic acid
-
-
3-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)propanoic acid
-
-
3-(2-hydroxy-3-(methyl(2-oxo-2-(piperidin-1-yl)ethyl)amino)propyl)-1-methylquinazoline-2,4(1H,3H)-dione
-
-
3-hydroxy-2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)propanoic acid
-
-
3-methyl-2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)butanoic acid
-
-
4-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)butanoic acid
-
68.2% inhibition at 0.3 mg/ml
4-methyl-2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)pentanoic acid
-
-
5'-(N-succinyl)-5'-amino-5'-deoxyuridine methyl ester
-
inhibits the yeast enzyme, and exhibits synergistic interaction with caspofungin against Candida albicans
-
5-(4-(2-hydroxy-3-((2-methoxyphenyl)amino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-((4-methoxyphenyl)amino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(1H-imidazol-1-yl)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(4H-1,2,4-triazol-4-yl)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(naphthalen-1-ylamino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(o-tolylamino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(p-tolylamino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(phenylamino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(piperazin-1-yl)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(piperidin-1-yl)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-(pyrrolidin-1-yl)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(2-hydroxy-3-morpholinopropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-((2,6-dimethylphenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-((2-chlorophenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-((4-bromophenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-((4-chlorobenzyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-((4-chlorophenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-(azepan-1-yl)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-(benzylamino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-(bis(2-hydroxyethyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-(butylamino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-(diethylamino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-(4-(3-(tert-butylamino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
-
-
5-[(6,6-dimethylhepta-2,4-diyn-1-yl)(methyl)amino]-3,4-dihydroquinolin-2(1H)-one
-
-
8-[(6,6-dimethylhepta-2,4-diyn-1-yl)(methyl)amino]-2H-1,4-benzoxazin-3(4H)-one
-
-
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-((2-hydroxy-3-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)propyl)(methyl)amino)acetamido)benzoate
-
-
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
-
-
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
[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
8,20-dihydroxy-9(11),13-abietadien-12-one
a diterpene compoud isolated from leaves of Chamaecyparis pisifera, inhibits Chs2p
Ni2+
-
inhibition of chitin synthase 1 and 2, no inhibition of chitin synthase 3
Nikkomycin
-
nikkomycin Z is more inhibitory to chitin synthetase 1 than for chitin synthetase 2
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
-
more inhibitory to chitin synthetase 1 than for chitin synthetase 2
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
-
no inhibition of chitin synthase 1 and 3 by methyllinderone, linderone, and kanakugiol from stem bark of Lindera erythrocarpa
-
additional information
the absence of Chs4p renders CSIII functionally inactive, independently of Chs3p accumulation at the plasma membrane
-
additional information
-
the absence of Chs4p renders CSIII functionally inactive, independently of Chs3p accumulation at the plasma membrane
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
lysophosphatidylserine
-
required, phosphatidylserine and lysophosphatidylserine are the best activators
phosphatidylserine
-
required, phosphatidylserine and lysophosphatidylserine are the best activators
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
-
additional information
blockade of endocytosis, independent of Chs4p function, stops Chs3p internalization, triggering a significant increase in chitin synthesis, overview
-
additional information
-
blockade of endocytosis, independent of Chs4p function, stops Chs3p internalization, triggering a significant increase in chitin synthesis, overview
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
N-acetyl-D-glucosamine
-
reaction with UDP-N-acetyl-D-glucosamine
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
0.005
O-methyl pisiferic acid
versus UDP-N-acetyl-beta-D-glucosamine
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
0.18
1-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetyl)pyrrolidine-2-carboxylic acid
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
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
-
-
0.166
2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)-3-(4-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetoxy)phenyl)propanoic acid
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.3
3-(1H-imidazol-5-yl)-2-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)propanoic acid
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.3
4-(2-(1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)acetamido)butanoic acid
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.8
5'-(N-succinyl)-5'-amino-5'-deoxyuridine methyl ester
Saccharomyces cerevisiae
-
pH 7.5, 25°C
-
0.1
5-(4-(2-hydroxy-3-((4-methoxyphenyl)amino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.47
5-(4-(2-hydroxy-3-(1H-imidazol-1-yl)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.15
5-(4-(2-hydroxy-3-(phenylamino)propyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.47
5-(4-(3-((2-chlorophenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.38
5-(4-(3-((4-bromophenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.36
5-(4-(3-((4-chlorophenyl)amino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 37°C
0.37
5-(4-(3-(butylamino)-2-hydroxypropyl)piperazin-1-yl)-2-oxo-1,2,3,4-tetrahydroquinoline hydrochloride
Saccharomyces cerevisiae
-
at pH 7.5 and 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
inhibition of Chs2p
0.44
8,20-dihydroxy-9(11),13-abietadien-12-one
Saccharomyces cerevisiae
inhibition of Chs1p
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Chs3p and Chs4p appear to co-localize at the neck region of the budding yeast
additional information
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
membrane-bound vesicle, Chs3p is present in an active form
additional information
-
the culture medium affects the relative abundance of chitin synthase 1 in chitosomes and plasma membrane populations
-
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
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
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
in SDS-PAGE, the purified enzyme shows a major band of 63000 Da and a weaker band at 74000 Da
additional information
the C-terminal region of Chs4p is required for its association with plasma membrane but not for biological function
additional information
-
the C-terminal region of Chs4p is required for its association with plasma membrane but not for biological function
additional information
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
proteolytic modification
side-chain modification
prenylation of CSIII components is involved in proper subcellular localization of the enzyme, overview
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
-
enzyme is present in the cell in a zymogen form
proteolytic modification
-
chitin synthetase zymogen is activated by proteinase B
proteolytic modification
-
chitin synthetase I exists as zymogen and is only measurable after trypsin treatment
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
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
-
chitin synthetase 2 is not activated by proteolysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V377I
-
enhanced emzymic activity in vitro. Mutation suppresses mutations in the C2 domain of INN1 protein, which is required for ingression
additional information
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
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high sensitivity of chitosomal chitin synthase 2 to high centrifugal forces
-
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of recombinant Chs2 from Pichia pastoris membranes by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of Chs4p-GFP and Chs3p-GFP in CRM233 and CRM103 strains, respectively
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
-
overexpression of CHS isozymes in Saccharomyces cerevisiae strains
-
overexpression of CHS2p isozyme in Saccharomyces cerevisiae strains
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
enzyme inhibitors can be useful as potential pesticidal agents
analysis
the chs3 gene encoding the chitin synthase 3 is used for synthetically lethality screening for mutation determination, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sburlati, A.; Cabib, E.
Chitin synthetase 2, a presumptive participant in septum formation in Saccharomyces cerevisiae
J. Biol. Chem.
261
15147-15152
1986
Saccharomyces cerevisiae
Cabib, E.; Kang, M.S.; Au-Young, J.
Chitin synthase from Saccharomyces cerevisiae
Methods Enzymol.
138
643-649
1987
Saccharomyces cerevisiae
Cabib, E.
Differential inhibition of chitin synthetases 1 and 2 from Saccharomyces cerevisiae by polyoxin D and nikkomycins
Antimicrob. Agents Chemother.
35
170-173
1991
Saccharomyces cerevisiae
Faehnrich, M.; Ahlers, J.
Improved assay and mechanism of the reaction catalyzed by the chitin synthase from Saccharomyces cerevisiae
Eur. J. Biochem.
121
113-118
1981
Saccharomyces cerevisiae
Ulane, R.E.; Cabib, E.
The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of the activating factor
J. Biol. Chem.
251
3367-3374
1976
Saccharomyces cerevisiae
Duran, A.; Cabib, E.
Solubilization and partial purification of yeast chitin synthetase. Confirmation of the zymogenic nature of the enzyme
J. Biol. Chem.
253
4419-4425
1978
Aspergillus flavus, Saccharomyces cerevisiae
Orlean, P.
Two chitin synthases in Saccharomyces cerevisiae
J. Biol. Chem.
262
5732-5739
1987
Saccharomyces cerevisiae
Kang, M.S.; Elango, N.; Mattia, E.; Au-Young, J.; Robbins, P.W.; Cabib, E.
Isolation of chitin synthetase from Saccharomyces cerevisiae. Purification of an enzyme by entrapment in the reaction product
J. Biol. Chem.
259
14966-14972
1984
Saccharomyces cerevisiae
Valdivieso, M.H.; Duran, A.; Roncero, C.
Chitin synthases in yeast and fungi
EXS
87
55-69
1999
Aspergillus nidulans, Saccharomyces cerevisiae, Candida albicans, Rhizopus microsporus var. oligosporus, Ustilago maydis
Uchida, Y.; Shimmi, O.; Sudoh, M.; Arisawa, M.; Yamada-Okabe, H.
Characterization of chitin synthase 2 of Saccharomyces cerevisiae II: Both full size and processed enzymes are active for chitin synthesis
J. Biochem.
119
659-666
1996
Saccharomyces cerevisiae
Lucero, H.A.; Kuranda, M.J.; Bulik, D.A.
A nonradioactive, high throughput assay for chitin synthase activity
Anal. Biochem.
305
97-105
2002
Saccharomyces cerevisiae
Leal-Morales, C.A.; Bracker, C.E.; Bartnicki-Garcia, S.
Subcellular localization, abundance and stability of chitin synthetases 1 and 2 from Saccharomyces cerevisiae
Microbiology
140
2207-2216
1994
Saccharomyces cerevisiae
-
Nagahashi, S.; Sudoh, M.; Ono, N.; Sawada, R.; Yamaguchi, E.; Uchida, Y.; Mio, T.; Takagi, M.; Arisawa, M.; Yamada-Okabe, H.
Characterization of chitin synthase 2 of Saccharomyces cerevisiae. Implication of two highly conserved domains as possible catalytic sites
J. Biol. Chem.
270
13961-13967
1995
Saccharomyces cerevisiae
Bulik, D.A.; Olczak, M.; Lucero, H.A.; Osmond, B.C.; Robbins, P.W.; Specht, C.A.
Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress
Eukaryot. Cell
2
886-900
2003
Saccharomyces cerevisiae
Cabib, E.; Schmidt, M.
Chitin synthase III activity, but not the chitin ring, is required for remedial septa formation in budding yeast
FEMS Microbiol. Lett.
224
299-305
2003
Saccharomyces cerevisiae (P29465), Saccharomyces cerevisiae
Yeager, A.R.; Finney, N.S.
The first direct evaluation of the two-active site mechanism for chitin synthase
J. Org. Chem.
69
613-618
2004
Saccharomyces cerevisiae
Grabinska, K.A.; Magnelli, P.; Robbins, P.W.
Prenylation of Saccharomyces cerevisiae Chs4p affects chitin synthase III activity and chitin chain length
Eukaryot. Cell
6
328-336
2007
Saccharomyces cerevisiae
Gautier-Lefebvre, I.; Behr, J.B.; Guillerm, G.; Muzard, M.
Iminosugars as glycosyltransferase inhibitors: synthesis of polyhydroxypyrrolidines and their evaluation on chitin synthase activity
Eur. J. Med. Chem.
40
1255-1261
2005
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180
Martinez-Rucobo, F.W.; Eckhardt-Strelau, L.; Terwisscha van Scheltinga, A.C.
Yeast chitin synthase 2 activity is modulated by proteolysis and phosphorylation
Biochem. J.
417
547-554
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae Y3437
Kang, T.H.; Hwang, E.I.; Yun, B.S.; Shin, C.S.; Kim, S.U.
Chitin synthase 2 inhibitory activity of O-methyl pisiferic acid and 8,20-dihydroxy-9(11),13-abietadien-12-one, isolated from Chamaecyparis pisifera
Biol. Pharm. Bull.
31
755-759
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae (A6ZKY2), Candida albicans (P23316), Candida albicans
Schmidt, M.; Drgon, T.; Bowers, B.; Cabib, E.
Hyperpolarized growth of Saccharomyces cerevisiae cak1P212S and cla4 mutants weakens cell walls and renders cells dependent on chitin synthase 3
FEMS Yeast Res.
8
362-373
2008
Saccharomyces cerevisiae (P29465), Saccharomyces cerevisiae
Reyes, A.; Sanz, M.; Duran, A.; Roncero, C.
Chitin synthase III requires Chs4p-dependent translocation of Chs3p into the plasma membrane
J. Cell Sci.
120
1998-2009
2007
Saccharomyces cerevisiae (P29465), Saccharomyces cerevisiae
Plant, A.; Thompson, P.; Williams, D.M.
Stereoselective synthesis of novel uracil polyoxin C conjugates as substrate analogues of chitin synthase
J. Org. Chem.
73
3714-3724
2008
Saccharomyces cerevisiae, Candida albicans
Hwang, E.I.; Lee, Y.M.; Lee, S.M.; Yeo, W.H.; Moon, J.S.; Kang, T.H.; Park, K.D.; Kim, S.U.
Inhibition of chitin synthase 2 and antifungal activity of lignans from the stem bark of Lindera erythrocarpa
Planta Med.
73
679-682
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH499
Ke, S.; Liu, F.; Wang, N.; Yang, Q.; Qian, X.
1,3,4-Oxadiazoline derivatives as novel potential inhibitors targeting chitin biosynthesis: Design, synthesis and biological evaluation
Bioorg. Med. Chem. Lett.
19
332-335
2009
Saccharomyces cerevisiae
Devrekanli, A.; Foltman, M.; Roncero, C.; Sanchez-Diaz, A.; Labib, K.
Inn1 and Cyk3 regulate chitin synthase during cytokinesis in budding yeasts
J. Cell Sci.
125
5453-5466
2012
Saccharomyces cerevisiae
Kral, K.; Bieg, T.; Nawrot, U.; W?odarczyk, K.; Lalik, A.; Hahn, P.; Wandzik, I.
New monomeric and dimeric uridinyl derivatives as inhibitors of chitin synthase
Bioorg. Chem.
61
13-20
2015
Saccharomyces cerevisiae
Ji, Q.; Yang, D.; Wang, X.; Chen, C.; Deng, Q.; Ge, Z.; Yuan, L.; Yang, X.; Liao, F.
Design, synthesis and evaluation of novel quinazoline-2,4-dione derivatives as chitin synthase inhibitors and antifungal agents
Bioorg. Med. Chem.
22
3405-3413
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae CGMCC 2.145
Gyore, J.; Parameswar, A.R.; Hebbard, C.F.; Oh, Y.; Bi, E.; Demchenko, A.V.; Price, N.P.; Orlean, P.
2-Acylamido analogues of N-acetylglucosamine prime formation of chitin oligosaccharides by yeast chitin synthase 2
J. Biol. Chem.
289
12835-12841
2014
Saccharomyces cerevisiae (P14180), Saccharomyces cerevisiae
Noureldin, N.A.; Kothayer, H.; Lashine, E.M.; Baraka, M.M.; Huang, Y.; Li, B.; Ji, Q.
Design, synthesis and biological evaluation of novel quinazoline-2,4-diones conjugated with different amino acids as potential chitin synthase inhibitors
Eur. J. Med. Chem.
152
560-569
2018
Saccharomyces cerevisiae, Saccharomyces cerevisiae CGMCC2.145
Ji, Q.; Deng, Q.; Li, B.; Li, B.; Shen, Y.
Design, synthesis and biological evaluation of novel 5-(piperazin-1-yl)quinolin-2(1H)-one derivatives as potential chitin synthase inhibitors and antifungal agents
Eur. J. Med. Chem.
180
204-212
2019
Saccharomyces cerevisiae, Saccharomyces cerevisiae CGMCC 2.145
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