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Literature summary extracted from

  • Roszak, A.W.; Robinson, D.A.; Krell, T.; Hunter, I.S.; Fredrickson, M.; Abell, C.; Coggins, J.R.; Lapthorn, A.J.
    The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor (2002), Structure, 10, 493-503.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.10
-
 Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.10 R23A reduced catalytic activity, replacement of Arg23 results in Tyr28 adopting an alternative conformation, more favourable than the one required for catalysis Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.10 additional information Streptomyces coelicolor role in shikimate pathway ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.10 Streptomyces coelicolor P15474
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.10 3-dehydroquinate = 3-dehydroshikimate + H2O mechanism Streptomyces coelicolor
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.10 3-dehydroquinate
-
 Streptomyces coelicolor 3-dehydroshikimate + H2O
-
 ?
4.2.1.10 additional information role in shikimate pathway Streptomyces coelicolor ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.10 dodecamer
-
 Streptomyces coelicolor