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Literature summary extracted from

  • Valdivieso, M.H.; Duran, A.; Roncero, C.
    Chitin synthases in yeast and fungi (1999), EXS, 87, 55-69.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.16
-
 Aspergillus nidulans
2.4.1.16
-
 Candida albicans
2.4.1.16
-
 Mycosarcoma maydis
2.4.1.16
-
 Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.16 Ni2+ inhibition of chitin synthase 1 and 2, no inhibition of chitin synthase 3 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.16 chitosome
-
 Saccharomyces cerevisiae 45009
-
2.4.1.16 plasma membrane
-
 Saccharomyces cerevisiae 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.16 Co2+ divalent cation required, chitin synthase 2 shows highest activity with chitin synthase 2 Saccharomyces cerevisiae
2.4.1.16 Mg2+
-
 Aspergillus nidulans
2.4.1.16 Mg2+ divalent cation required, chitin synthase 1 and 3 have a preference for Mg2+ Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n Saccharomyces cerevisiae
-
 UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n Aspergillus nidulans 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 + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.16 Aspergillus nidulans
-
-
-
2.4.1.16 Candida albicans
-
-
-
2.4.1.16 Mycosarcoma maydis
-
-
-
2.4.1.16 Rhizopus microsporus var. oligosporus
-
-
-
2.4.1.16 Saccharomyces cerevisiae
-
 chitin synthase 1, 2 and 3
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.16 proteolytic modification
-
 Candida albicans
2.4.1.16 proteolytic modification
-
 Aspergillus nidulans
2.4.1.16 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 Saccharomyces cerevisiae

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.16 additional information level of chitin synthase 1 remains constant during vegetative growth in synchronised cells Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
-
 Saccharomyces cerevisiae UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
-
 Aspergillus nidulans UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
-
 Candida albicans UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
-
 Mycosarcoma maydis UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n
-
 Rhizopus microsporus var. oligosporus UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?
2.4.1.16 UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n 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 Aspergillus nidulans UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1
-
 ?