the active site area sequence of the 2-methylenebornane (2-MB) synthase from Pseudomonas fluorescens is compared to the sequence of two other bacterial class I terpene synthases, the Streptomyces coelicolor 2-methylisoborneol (2-MIB) synthase and the Streptomyces pristinaspiralis selinadiene synthase (SDS), structure-function relationships, overview. The residues at the effector position of the C11-terpene synthases differ
noncanonical terpenes with 11 carbon atoms are synthesized via a GPP-C2-methyltransferase and the subsequent conversion of 2-methyl-GPP by certain terpene synthases into mainly 2-methylisoborneol and 2-methylenebornane. Many other C11-terpenes are reported as side products, but they are synthesized only in minor amounts by the bacterial C11-terpene biosynthesis pathway. 2-Methyl-GPP is converted to the C11-compound 2-MIB (2-methylisoborneol) by a terpene synthase (EC 4.2.3.118). Related 2-methyl-GPP-accepting terpene synthases in other bacteria are demonstrated to synthesize mainly the corresponding hydrocarbon 2-MB (2-methylenebornane)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in open and closed (ligand-bound) conformation. An induced-fit mechanism depends on an effector triad comprising the diphosphate sensor Arg178, the linker Asp181, and the effector Gly182-O. This structural motif is strictly conserved in class I terpene cyclases
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