Biochemical Characterization of Indole Prenyltransferases

Yu, Xia; Liu, Yan; Xie, Xiulan; Zheng, Xiaodong; Li, Shu-Ming

doi:10.1074/jbc.m111.317982

Cited by 76 publications

(72 citation statements)

References 55 publications

(77 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The 1 H NMR spectra of 1 b-3 b clearly differed from those of the enzyme products of 5-DMATS with 1 a-3 a (coupling pattern and chemical shifts), [11] thus indicating prenylation at C-6. Furthermore, the 1 H NMR spectra of 1 b and 2 b corresponded well to those of the enzyme products of IptA with 1 a and 2 a.…”

Section: Confirmation Of the Prenylation Position Of The Enzyme Productsmentioning

confidence: 93%

“…To confirm prenylation and determine the prenylation position, seven enzyme products (1 b-7 b) were isolated by HPLC from incubation mixtures of SAML0654 with 1 a-7 a in the presence of DMAPP and subjected to MS and NMR analyses (Tables S3-S4 ) confirmed the attachment of a regular dimethylallyl moiety to a C atom. [9,11,16,17] Comparison of the NMR spectra of 1 b-7 b with those of 1 a-7 a revealed the disappearance of signals for one aromatic proton, thus proving the attachment of the prenyl moiety at the indole ring. The singlet at d H = 7.08-7.15 ppm for H-2 in all the spectra indicated that prenylation did not take place at C-2.…”

Section: Confirmation Of the Prenylation Position Of The Enzyme Productsmentioning

confidence: 94%

“…[9,11,13,15] In contrast, they show high promiscuity for the aromatic substrate and accept a large number of tryptophan derivatives. [9,11,16,17] FgaPT2 and 7-DMATS even used hydroxynaphthalenes as prenyl acceptors; [18] these are natural substrates of prenyltransferases of the CloQ/NphB group, from both bacteria and fungi. [19,20] The acceptance of hydroxynaphthalenes by FgaPT2 and 7-DMATS encouraged us to compare the biochemical properties and substrate specificities of DMATSs from bacteria and fungi.…”

Section: Introductionmentioning

confidence: 91%

“…They were shown to catalyze prenylation of l-tryptophan at C-4, C-5, and C-7, respectively. [11][12][13] Three bacterial DMATSs have shown prenylation at positions N1, C-5, and C-6: CymD (Salinispora arenicola), SCO7467 (Streptomyces coelicolor), and IptA (Streptomyces sp. SN-593), respectively.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Biochemical Investigations of Two 6‐DMATS Enzymes from Streptomyces Reveal New Features of L‐Tryptophan Prenyltransferases

Winkelblech

2014

ChemBioChem

Self Cite

View full text Add to dashboard Cite

Two putative prenyltransferase genes, SAML0654 and Strvi8510, were identified in Streptomyces ambofaciens and Streptomyces violaceusniger, respectively. Their deduced products share 63% sequence identity. Biochemical investigations with recombinant proteins demonstrated that L-tryptophan and derivatives, including D-tryptophan, 4-, 5-, 6- and 7-methyl-dl-tryptophan, were well accepted by both enzymes in the presence of DMAPP. Structural elucidation of the isolated products revealed regiospecific prenylation at C-6 of the indole ring and proved unequivocally the identification of two very similar 6-dimethylallyltryptophan synthases (6-DMATS). Detailed biochemical investigations with SAML0654 proved L-tryptophan to be the best substrate (K(m) 18 μm, turnover 0.3 s(-1)). Incubation with different prenyl donors showed that they also accepted GPP and catalyzed the same specific prenylation. Utilizing GPP as a prenyl donor has not been reported for tryptophan prenyltransferases previously. Both enzymes also catalyzed prenylation of some hydroxynaphthalenes; this has not previously been described for bacterial indole prenyltransferases. Interestingly, SAML0654 transferred prenyl moieties onto the unsubstituted ring of hydroxynaphthalenes.

show abstract

Section: Confirmation Of the Prenylation Position Of The Enzyme Productsmentioning

confidence: 93%

Section: Confirmation Of the Prenylation Position Of The Enzyme Productsmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Biochemical Investigations of Two 6‐DMATS Enzymes from Streptomyces Reveal New Features of L‐Tryptophan Prenyltransferases

Winkelblech

2014

ChemBioChem

Self Cite

View full text Add to dashboard Cite

show abstract

“…The order of the signals for the four protons of the indole ring of 1 b-6 b (that is, the two singlets between the two doublets) corresponds very well to that of the known C6-, but clearly differs from that of C5-prenylated or alkylated indole derivatives. [19][20][21] This unequivocally proves C6-geranylation of the b-series products (1 b-6 b).…”

Section: Acceptance Of Gpp By Anaptmentioning

confidence: 68%

Geranylation of Cyclic Dipeptides by the Dimethylallyl Transferase AnaPT Resulting in a Shift of Prenylation Position on the Indole Ring

Pockrandt

2013

ChemBioChem

Self Cite

View full text Add to dashboard Cite

The dimethylallyl transferase AnaPT from Neosartorya fischeri is involved in the biosynthesis of acetylaszonalenin and catalyses the regioselective and stereospecific C3α-prenylation of (R)-benzodiazepinedione in the presence of dimethylallyl diphosphate. This enzyme also converts several tryptophan-containing cyclic dipeptides to C3α-prenylated indolines. In this study, we demonstrate the geranylation of (R)-benzodiazepinedione and five other cyclic dipeptides by AnaPT in the presence of geranyl diphosphate (GPP). Interestingly, structure elucidation by NMR and MS analyses revealed that, with GPP, the geranyl moiety is attached to C-6 or C-7 rather than C-3 of the indole ring of the enzyme products. For (R)-benzodiazepinedione, one dominant C6-geranylated derivative was obtained, whereas the other five substrates yielded both C6- and C7-geranylated products. Neither acceptance of GPP by a dimethylallyl transferase from the dimethylallyltryptophan synthase superfamily, nor the alkylation shift from C-3 to the benzene ring of the indole nucleus has been reported previously.

show abstract

One Substrate – Seven Products with Different Prenylation Positions in One‐Step Reactions: Prenyltransferases Make it Possible

Fan

2013

Adv Synth Catal

View full text Add to dashboard Cite

Prenylated indole alkaloids derived from L‐tryptophan are widely distributed in nature and show diverse biological and pharmacological activities, usually distinct from their non‐prenylated precursors. Prenyltransferases catalyze the transfer reactions of prenyl moieties onto the indole nucleus and contribute largely to the structural diversity of these compounds. In this study, we demonstrate the acceptance of cyclo‐L‐homotryptophan‐D‐valine, an unnatural cyclic dipeptide, by eight prenyltransferases of the dimethylallyltryptophan synthase superfamily. Seven products with one prenyl moiety at each position of the indole nucleus and one diprenylated derivative were isolated from enzyme assays of cyclo‐L‐homotryptophan‐D‐valine with dimethylallyl diphosphate. To the best of our knowledge, this is the first report for production of seven monoprenylated products from one substrate by one‐step reactions.magnified image

show abstract

Biochemical Characterization of Indole Prenyltransferases

Cited by 76 publications

References 55 publications

Biochemical Investigations of Two 6‐DMATS Enzymes from Streptomyces Reveal New Features of L‐Tryptophan Prenyltransferases

Biochemical Investigations of Two 6‐DMATS Enzymes from Streptomyces Reveal New Features of L‐Tryptophan Prenyltransferases

Geranylation of Cyclic Dipeptides by the Dimethylallyl Transferase AnaPT Resulting in a Shift of Prenylation Position on the Indole Ring

One Substrate – Seven Products with Different Prenylation Positions in One‐Step Reactions: Prenyltransferases Make it Possible

Contact Info

Product

Resources

About