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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O - Streptomyces sp. cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O - Streptomyces melanosporofaciens cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O the enzyme is involved in biosynthesis of cyclooctatin Streptomyces melanosporofaciens cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O when bound to the enzyme, geranylgeranyl dithiophosphate (GGSPP) is folded in the active site pocket into a unique S-shaped conformation. A Mg2+ ion is coordinated in an octahedral manner by the Asn220, Ser224, and Glu228 side chains of the NSE motif, as well as by a water molecule and the diphosphate group of GGSPP. Compared to the apoform, the side chain of Asn220 is rotated and oriented to allow Mg2+ binding. The diphosphate group of GGSPP is also recognized by Arg177, Arg227, and the basic motif residues Arg294 and Tyr295. Active site docking model for the complex of CotB2 and reaction product (2R,3R,6R,7S,11R,14R)-cyclooctat-9-en-7-ol Streptomyces melanosporofaciens cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O - Streptomyces melanosporofaciens MI614-43F2 cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O when bound to the enzyme, geranylgeranyl dithiophosphate (GGSPP) is folded in the active site pocket into a unique S-shaped conformation. A Mg2+ ion is coordinated in an octahedral manner by the Asn220, Ser224, and Glu228 side chains of the NSE motif, as well as by a water molecule and the diphosphate group of GGSPP. Compared to the apoform, the side chain of Asn220 is rotated and oriented to allow Mg2+ binding. The diphosphate group of GGSPP is also recognized by Arg177, Arg227, and the basic motif residues Arg294 and Tyr295. Active site docking model for the complex of CotB2 and reaction product (2R,3R,6R,7S,11R,14R)-cyclooctat-9-en-7-ol Streptomyces melanosporofaciens MI614-43F2 cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O the enzyme is involved in biosynthesis of cyclooctatin Streptomyces melanosporofaciens MI614-43F2 cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O - Streptomyces sp. LZ35 cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O - Streptomyces melanosporofaciens M1614-43f2 cyclooctat-9-en-7-ol + diphosphate - ?
Show all pathways known for 4.2.3.146Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.146geranylgeranyl diphosphate + H2O the enzyme is involved in biosynthesis of cyclooctatin Streptomyces melanosporofaciens M1614-43f2 cyclooctat-9-en-7-ol + diphosphate - ?
Results 1 - 10 of 14 > >>
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