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Literature summary for 4.2.1.19 extracted from

  • Sinha, S.C.; Chaudhuri, B.N.; Burgner, J.W.; Yakovleva, G.; Davisson, V.J.; Smith, J.L.
    Crystal structure of imidazole glycerol-phosphate dehydratase: Duplication of an unusual fold (2004), J. Biol. Chem., 279, 15491-15498.
    View publication on PubMed
Search for more literature for 4.2.1.19

Crystallization (Commentary)

Crystallization (Comment) Organism
trimeric form without Mn2+, hanging drop vapor diffusion method Cryptococcus neoformans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ metalloprotein, transition metals induce aggregation and are required for catalysis, 1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme Cryptococcus neoformans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Cryptococcus neoformans sixth step in histidine biosynthesis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Cryptococcus neoformans P0CO22
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Cryptococcus neoformans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate removal of a non-acidic hydrogen atom in the dehydration reaction Cryptococcus neoformans 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
 ?
additional information sixth step in histidine biosynthesis Cryptococcus neoformans ?
-
 ?

Subunits

Subunits Comment Organism
multimer 1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme Cryptococcus neoformans
trimer 1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme Cryptococcus neoformans