Literature summary for 2.5.1.106 extracted from

Jost, M.; Zocher, G.; Tarcz, S.; Matuschek, M.; Xie, X.; Li, S.M.; Stehle, T.
Structure-function analysis of an enzymatic prenyl transfer reaction identifies a reaction chamber with modifiable specificity (2010), J. Am. Chem. Soc., 132, 17849-17858.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Aspergillus fumigatus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of unliganded enzyme FtmPT1 to 2.5 A resolution as well as of a ternary complex of FtmPT1 bound to brevianamide F and an analogue of its isoprenoid substrate dimethylallyl diphosphate. FtmPT1 assumes a rare alpha/beta-barrel fold, consisting of 10 circularly arranged -strands surrounded by alpha-helices. Catalysis is performed in a hydrophobic reaction chamber at the center of the barrel	Aspergillus fumigatus

Crystallization (Comment)

Organism

crystal structures of unliganded enzyme FtmPT1 to 2.5 A resolution as well as of a ternary complex of FtmPT1 bound to brevianamide F and an analogue of its isoprenoid substrate dimethylallyl diphosphate. FtmPT1 assumes a rare alpha/beta-barrel fold, consisting of 10 circularly arranged -strands surrounded by alpha-helices. Catalysis is performed in a hydrophobic reaction chamber at the center of the barrel

Aspergillus fumigatus

Protein Variants

Protein Variants	Comment	Organism
E102Q	mutation reduces the production of tryprostatin B to undetectable amounts	Aspergillus fumigatus
G115A	no change in prenylation position of product	Aspergillus fumigatus
G115I	complete loss of activity	Aspergillus fumigatus
G115L	formation of tryprostatin B is abolished, formation of a new product occurs	Aspergillus fumigatus
G115T	0.4% of wild-type activity in formation of trytrostatin B. Mutant catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus	Aspergillus fumigatus
H279F	70% of wild-type activity	Aspergillus fumigatus

Organism

Organism	UniProt	Comment	Textmining
Aspergillus fumigatus	Q4WAW7	-	-
Aspergillus fumigatus Af293	Q4WAW7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
dimethylallyl diphosphate + brevianamide F	-	Aspergillus fumigatus	diphosphate + tryprostatin B	mutant G115T catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus	?
dimethylallyl diphosphate + brevianamide F	-	Aspergillus fumigatus Af293	diphosphate + tryprostatin B	mutant G115T catalyzes the formation of a different product that carries a reverse prenyl moiety at the C-3 of the indole nucleus	?
additional information	the reaction is most likely initiated by hydrolysis of the phosphoric acid ester bond to form the dimethylallylic cation and a diphosphate group. The resulting carbocation would be stabilized from two sides by cation-pi interactions with aromatic ring systems, one from the substrate brevianamide F and one from the side chain of Y382. The stabilized cation can then undergo a nucleophilic attack from an aromatic nucleus such as that of the indole. The reactivity of the indole is likely enhanced by a hydrogen bond from its N-1 nitrogen to the side chain carboxylate of E102	Aspergillus fumigatus	?	-	?
additional information	the reaction is most likely initiated by hydrolysis of the phosphoric acid ester bond to form the dimethylallylic cation and a diphosphate group. The resulting carbocation would be stabilized from two sides by cation-pi interactions with aromatic ring systems, one from the substrate brevianamide F and one from the side chain of Y382. The stabilized cation can then undergo a nucleophilic attack from an aromatic nucleus such as that of the indole. The reactivity of the indole is likely enhanced by a hydrogen bond from its N-1 nitrogen to the side chain carboxylate of E102	Aspergillus fumigatus Af293	?	-	?