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Literature summary for 2.5.1.34 extracted from

  • Rudolf, J.D.; Wang, H.; Poulter, C.D.
    Multisite prenylation of 4-substituted tryptophans by dimethylallyltryptophan synthase (2013), J. Am. Chem. Soc., 135, 1895-1902.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.34

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged 4-DMATS in Escherichia coli strain BL21 Star (DE3) Claviceps purpurea
recombinant expression of the soluble enzyme in Escherichia coli strain BL21 Star™ (DE3) Claviceps purpurea

Inhibitors

Inhibitors Comment Organism Structure
4-methyl-DL-tryptophan a competitive substrate inhibitor Claviceps purpurea
4-methyltryptophan 4-methyltryptophan is a competitive dead-end analogue of tryptophan used in kinetic studies of 4-DMATS Claviceps purpurea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics for tryptophan and its 4-substituted analogues Claviceps purpurea
0.017
-
 4-amino-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
0.02
-
 L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
0.089
-
 4-methyl-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
0.25
-
 4-methoxy-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Claviceps purpurea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + L-tryptophan Claviceps purpurea
-
 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan Claviceps purpurea dimethylallyltryptophan synthase catalyzes both normal and reverse prenylation at C3 of the indole ring and normal prenylation of N1 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
additional information Claviceps purpurea 4-DMATS catalyzes normal prenylation at C4 of L-tryptophan. When C4 is blocked, 4-DMATS catalyzes alkylation at all of the activated positions, except weakly activated C6, depending on the electron-donating properties of the blocking substituent. In addition, both normal and reverse prenylation is seen at C3 for 4-methyltryptophan. The high regioselectivity for C4 alkylation with the normal substrates suggests that binding and catalysis of a single conformation has been optimized for synthesis of 4-dimethylallyltryptophan, but when alkylation at C4 is blocked, alkylation from other conformations becomes competitive ?
-
 ?

Organism

Organism UniProt Comment Textmining
Claviceps purpurea
-
-
-
Claviceps purpurea M1WA41
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged 4-DMATS from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography and dialysis Claviceps purpurea

Reaction

Reaction Comment Organism Reaction ID
dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan catalytic reaction mechanism, overview Claviceps purpurea
a
dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan ability of dimethylallyltryptophan synthase to prenylate at five different sites on the indole nucleus, with normal and reverse prenylation at one of the sites, is consistent with a dissociative electrophilic alkylation of the indole ring, where orientation of the substrates within the active site and substituent electronic effects determine the position and type of prenylation Claviceps purpurea
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + 4-amino-L-tryptophan an alternate substrate, giving normal prenylation at C5 and C7, shows 0.81% of the activity with L-tryptophan Claviceps purpurea diphosphate + ? the reaction with 4-methoxytryptophan gives five products, analysis, overview ?
dimethylallyl diphosphate + 4-amino-L-tryptophan
-
 Claviceps purpurea diphosphate + 4-amino-5-(3-methylbut-2-en-1-yl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + 4-methoxy-L-tryptophan an alternate substrate, giving normal prenylation at C5 as the major product, shows 0.17% of the activity with L-tryptophan Claviceps purpurea diphosphate + 5-(3-methylbut-2-enyl)4-methoxy-L-tryptophan the reaction with 4-methoxytryptophan gives four products, analysis, overview ?
dimethylallyl diphosphate + 4-methoxy-L-tryptophan
-
 Claviceps purpurea diphosphate + 4-methoxy-3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + 4-methoxy-3a-(3-methylbut-2-en-1-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + 4-methoxy-5-(3-methylbut-2-en-1-yl)-L-tryptophan + 4-methoxy-1-(3-methylbut-2-en-1-yl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + 4-methyl-L-tryptophan an alternate substrate and competitive inhibitor, shows 0.28% of the activity with L-tryptophan Claviceps purpurea diphosphate + ? the reaction with 4-methyltryptophan gives four products, analysis, overview ?
dimethylallyl diphosphate + 4-methyl-L-tryptophan
-
 Claviceps purpurea diphosphate + 4-methyl-3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + 4-methyl-3a-(3-methylbut-2-en-1-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid + 4-methyl-5-(3-methylbut-2-en-1-yl)-L-tryptophan + 4-methyl-1-(3-methylbut-2-en-1-yl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan
-
 Claviceps purpurea diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan dimethylallyltryptophan synthase catalyzes both normal and reverse prenylation at C3 of the indole ring and normal prenylation of N1 Claviceps purpurea diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan L-tryptophan is the preferred substrate Claviceps purpurea diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
additional information 4-DMATS catalyzes normal or reverse prenylation of tryptophan and C4-substituted analogues at five different sites on the indole ring, N1, C3, C4, C5, and C7, depending on the substituent Claviceps purpurea ?
-
 ?
additional information 4-DMATS catalyzes normal prenylation at C4 of L-tryptophan. When C4 is blocked, 4-DMATS catalyzes alkylation at all of the activated positions, except weakly activated C6, depending on the electron-donating properties of the blocking substituent. In addition, both normal and reverse prenylation is seen at C3 for 4-methyltryptophan. The high regioselectivity for C4 alkylation with the normal substrates suggests that binding and catalysis of a single conformation has been optimized for synthesis of 4-dimethylallyltryptophan, but when alkylation at C4 is blocked, alkylation from other conformations becomes competitive Claviceps purpurea ?
-
 ?
additional information 4-methyltryptophan is an alternate substrate for 4-DMATS Claviceps purpurea ?
-
 ?

Synonyms

Synonyms Comment Organism
4-DMATS
-
 Claviceps purpurea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Claviceps purpurea

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.42
-
 4-amino-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
0.75
-
 4-methyl-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
1.3
-
 4-methoxy-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
60
-
 L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Claviceps purpurea

General Information

General Information Comment Organism
evolution all of the members of the structurally related dimethylallyltryptophan synthase family show a common mechanism for prenylation of tryptophan Claviceps purpurea
evolution collectively a family of enzymes, the dimethylallyl tryptophan synthases (DMATS) catalyze alkylation of the indole ring in tryptophan or tryptophan-containing dipeptides at positions N1, C2, C3, C4, C5, C6, or C7 by dimethylallyl diphosphate (DMAPP) to give the different naturally occurring carbon skeletons. The dimethylallyl moiety can be attached at C1' (normal prenylation) or C3' (reverse prenylation), further increasing structural diversity Claviceps purpurea
metabolism 4-DMATS catalyzes the normal prenylation of tryptophan at C4 by DMAPP as the first committed step in ergot alkaloid biosynthesis Claviceps purpurea
physiological function the aromatic prenyltransferase dimethylallyltryptophan synthase in Claviceps purpurea catalyzes the normal prenylation of tryptophan at C4 of the indole nucleus in the first committed step of ergot alkaloid biosynthesis Claviceps purpurea

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1
-
 4-methoxy-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
8.5
-
 4-methyl-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
25
-
 4-amino-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
3100
-
 L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea