Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.34 4-methyl-DL-tryptophan a competitive substrate inhibitor Claviceps purpurea
2.5.1.34 4-methyltryptophan 4-methyltryptophan is a competitive dead-end analogue of tryptophan used in kinetic studies of 4-DMATS Claviceps purpurea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.34 additional information
-
 additional information Michaelis-Menten kinetics for tryptophan and its 4-substituted analogues Claviceps purpurea
2.5.1.34 0.017
-
 4-amino-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 0.02
-
 L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 0.089
-
 4-methyl-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 0.25
-
 4-methoxy-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.34 Mg2+ required Claviceps purpurea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.34 dimethylallyl diphosphate + L-tryptophan Claviceps purpurea
-
 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 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
-
 ?
2.5.1.34 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

EC Number Organism UniProt Comment Textmining
2.5.1.34 Claviceps purpurea
-
-
-
2.5.1.34 Claviceps purpurea M1WA41
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.34 dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan catalytic reaction mechanism, overview Claviceps purpurea
a
2.5.1.34 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.34 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 ?
2.5.1.34 dimethylallyl diphosphate + 4-amino-L-tryptophan
-
 Claviceps purpurea diphosphate + 4-amino-5-(3-methylbut-2-en-1-yl)-L-tryptophan
-
 ?
2.5.1.34 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 ?
2.5.1.34 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
-
 ?
2.5.1.34 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 ?
2.5.1.34 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
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan
-
 Claviceps purpurea diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 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
-
 ?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan L-tryptophan is the preferred substrate Claviceps purpurea diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.34 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 ?
-
 ?
2.5.1.34 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 ?
-
 ?
2.5.1.34 additional information 4-methyltryptophan is an alternate substrate for 4-DMATS Claviceps purpurea ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.34 4-DMATS
-
 Claviceps purpurea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.34 30
-
 assay at Claviceps purpurea

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.34 0.42
-
 4-amino-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 0.75
-
 4-methyl-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 1.3
-
 4-methoxy-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 60
-
 L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.34 8
-
 assay at Claviceps purpurea

General Information

EC Number General Information Comment Organism
2.5.1.34 evolution all of the members of the structurally related dimethylallyltryptophan synthase family show a common mechanism for prenylation of tryptophan Claviceps purpurea
2.5.1.34 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
2.5.1.34 metabolism 4-DMATS catalyzes the normal prenylation of tryptophan at C4 by DMAPP as the first committed step in ergot alkaloid biosynthesis Claviceps purpurea
2.5.1.34 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.34 5.1
-
 4-methoxy-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 8.5
-
 4-methyl-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 25
-
 4-amino-L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea
2.5.1.34 3100
-
 L-tryptophan pH 8.0, 30°C, recombinant His-tagged 4-DMATS Claviceps purpurea