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Information on EC 2.4.1.16 - chitin synthase and Organism(s) Ustilago maydis and UniProt Accession O13394

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.16 chitin synthase
IUBMB Comments
Converts UDP-N-acetyl-alpha-D-glucosamine into chitin and UDP.
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This record set is specific for:
Ustilago maydis
UNIPROT: O13394
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Word Map
The taxonomic range for the selected organisms is: Ustilago maydis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
chitin synthase, chitin synthetase, chs3p, chitin synthase 1, chitin synthase iii, chitin synthase 2, csiii, chs4p, chs2p, chitin synthase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chitin synthase 5
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chitin-UDP acetyl-glucosaminyl transferase 5
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acetylglucosaminyltransferase, chitin-uridine diphosphate
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chitin synthase 1
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chitin synthase 2
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chitin synthase 3
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chitin synthase 4
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chitin synthase 6
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chitin synthase 7
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chitin synthetase
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chitin-UDP acetyl-glucosaminyl transferase 1
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chitin-UDP acetyl-glucosaminyl transferase 2
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chitin-UDP acetyl-glucosaminyl transferase 3
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chitin-UDP acetyl-glucosaminyl transferase 4
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chitin-UDP acetyl-glucosaminyl transferase 6
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chitin-UDP acetyl-glucosaminyl transferase 7
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chitin-UDP N-acetylglucosaminyltransferase
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chitin-uridine diphosphate acetylglucosaminyltransferase
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CSI
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CSII
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CSIII
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trans-N-acetylglucosaminosylase
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UmCHS3
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UmCHS6
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-18-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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-
?
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
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?
additional information
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
Manually annotated by BRENDA team
CHS5 is localized at the septum of yeast-like cells and hyphae
Manually annotated by BRENDA team
CHS5 is localized at the growing bud and hyphal tips, indicating that they participate in tip growth
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
CHS5 is localized at the septum of yeast-like cells and hyphae
Manually annotated by BRENDA team
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transmembrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Ruiz-Herrera, J.; Xoconostle-Cazares, B.; Reynaga-Pena, C.G.; Leon-Ramirez, C.; Carabez-Trejo, A.
Immunolocalization of chitin synthases in the phytopathogenic dimorphic fungus Ustilago maydis
FEMS Yeast Res.
6
999-1009
2006
Ustilago maydis
Manually annotated by BRENDA team
Weber, I.; Assmann, D.; Thines, E.; Steinberg, G.
Polar localizing class V myosin chitin synthases are essential during early plant infection in the plant pathogenic fungus Ustilago maydis
Plant Cell
18
225-242
2006
Ustilago maydis (O13394), Ustilago maydis (O13395), Ustilago maydis (P30598), Ustilago maydis (P30599), Ustilago maydis (Q4P333), Ustilago maydis (Q99126), Ustilago maydis (Q99127), Ustilago maydis
Manually annotated by BRENDA team
Treitschke, S.; Doehlemann, G.; Schuster, M.; Steinberg, G.
The myosin motor domain of fungal chitin synthase V is dispensable for vesicle motility but required for virulence of the maize pathogen Ustilago maydis
Plant Cell
22
2476-2494
2010
Ustilago maydis (Q4P9K9), Ustilago maydis
Manually annotated by BRENDA team
Fernandes, C.; Gow, N.; Goncalves, T.
The importance of subclasses of chitin synthase enzymes with myosin-like domains for the fitness of fungi
Fungal Biol. Rev.
30
1-14
2016
Aspergillus fumigatus, Aspergillus nidulans, Aspergillus oryzae, Botrytis cinerea, Yarrowia lipolytica, Colletotrichum graminicola, Cryptococcus neoformans, Fusarium oxysporum, Fusarium verticillioides, Fusarium graminearum, Neurospora crassa, Pyricularia oryzae, Ustilago maydis, Exophiala dermatitidis, Penicillium digitatum
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Manually annotated by BRENDA team