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Literature summary for 4.2.1.10 extracted from

  • Euverink, G.J.W.; Hessels, G.I.; Vrijbloed, J.W.; Coggins, J.R.; Dijkhuizen, L.
    Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica (1992), J. Gen. Microbiol., 138, 2449-2457.
    View publication on PubMed
Search for more literature for 4.2.1.10

Inhibitors

Inhibitors Comment Organism Structure
NaBH4
-
 Amycolatopsis methanolica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.121
-
 3-dehydroquinate
-
 Amycolatopsis methanolica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
10000
-
 10 * 10000, SDS-PAGE Amycolatopsis methanolica
135000
-
 gel filtration Amycolatopsis methanolica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydroquinate Amycolatopsis methanolica the enzyme is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids ?
-
 ?

Organism

Organism UniProt Comment Textmining
Amycolatopsis methanolica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Amycolatopsis methanolica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydroquinate
-
 Amycolatopsis methanolica 3-dehydroshikimate + H2O
-
 ?
3-dehydroquinate the enzyme is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids Amycolatopsis methanolica ?
-
 ?

Subunits

Subunits Comment Organism
dodecamer 10 * 10000, SDS-PAGE Amycolatopsis methanolica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
76
-
-
 Amycolatopsis methanolica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Amycolatopsis methanolica