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153-94-6

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153-94-6 Usage

Description

Different sources of media describe the Description of 153-94-6 differently. You can refer to the following data:
1. D(+)-tryptophan is the D-form (non-proteinogenic form) of the amino acid tryptophan. It can be used for Human embryonic kidney cell (HEK-293, ATCC: CRL-1573) culture. It is also a sweetener used to study the release of incretins from enteroendocrine cells triggered by sugar but not by sweeteners.
2. D-tryptophan (Full name D (+)-Tryptophan) is a white to pale yellow or white crystalline powder at room temperature, odorless or slight odor, slightly sweet taste. Solubility in water is 1.14 g (25 ℃), soluble in dilute acid and alkali, stable in alkali, decomposed in strong acid, slightly soluble in ethanol, not soluble in chloroform, ethyl ether. It plays an important role for human and animal growth and development, metabolism, known as the second essential amino acids. They are almost identical with L-type and physical and chemical properties, and only the optical activity is opposite. But their distribution, function and coenzyme have diversity. Its melting point is very high, generally above 200 degrees. It can dissolve in water, and in the near UV region it has the ability to absorb light. Tryptophan is one of the 20 standard amino acids, as well as an essential amino acid in the human diet. It is encoded in the standard genetic code as the codon UGG. the D-stereoisomer is occasionally found in naturally produced peptides (for example, the marine venom peptide contryphan). The distinguishing structural characteristic of tryptophan is that it contains an indole functional group. It is an essential amino acid as defined by its growth effects on rats.

Characteristics and Functions

D-tryptophan amino acid, as a non-reactive protein, has special physiological properties. It can be used as a non-nutritive sweeteners, feed additive, plant growth agents in food feed industry and agriculture. In the pharmaceutical industry, it mainly used for the synthesis of various polypeptides, instead of L-tryptophan peptide drug for half-life extending and reduce the side effects, but it will not resistant to the front body, and it will become important enzyme inhibitor. It can also improve the body's immunity, delayed allergic reactions. Most peptide antibiotic can resistant gram-positive bacteria, Gram-negative bacteria and some, such as Pseudomonas aeruginosa, mycobacteria, fungi, bacteria, pathogens and tumor cells, which have better inhibit and kill ability. D-tryptophan can be used for the synthetic of semi-synthetic antibiotics, for which pharmacological plays an important role for the side chain. The peptide bond is difficult to be β-lactam enzyme action, thus high stability, and has broad antibacterial spectrum, toxicity, hypoallergenic, rapid absorption, high blood concentrations of the drug long duration.

Project Standards

Appearance? white or slightly yellow crystalline powder Content 99.0%~101.0% Specific rotation [α] D20 + 30.5 °~+ 32.5 ° Transmittance ≥95.0% Acidity PH 5.5~6.4 Loss on drying ≤0.2% Residue on ignition ≤0.1% Chloride [Cl-] ≤0.02% Sulphate [SO42-] ≤0.02% Ammonium [NH4 +] ≤0.02% Heavy metals [Pb] ≤10ppm Ferric [Fe] ≤10ppm Arsenic salt [As2O3] ≤1ppm Other amino acids compliance

Application

An important nutrient, niacin is used as the control agent Medicine Production method: D-tryptophan as raw material, chloroacetic anhydride was added under cooling state after polishing sulfuric acid in ice water, filtered and recrystallized from water, and finally treatment with carboxypeptidase trypsin to remove L-type, acidified with acetic acid, ethanol recrystallization refining.

References

Different sources of media describe the References of 153-94-6 differently. You can refer to the following data:
1. https://pubchem.ncbi.nlm.nih.gov/compound/D-Tryptophan#section=Top
2. Fujita, Yukihiro, et al. "Incretin release from gut is acutely enhanced by sugar but not by sweeteners in vivo." American Journal of Physiology Endocrinology & Metabolism 296.3(2009):E473. Bacchus, W, W. Weber, and M. Fussenegger. "Increasing the dynamic control space of mammalian transcription devices by combinatorial assembly of homologous regulatory elements from different bacterial species." Metabolic Engineering 15.1(2013):144.

Chemical Properties

white powder

Uses

Different sources of media describe the Uses of 153-94-6 differently. You can refer to the following data:
1. An essential amino acid found in naturally produced pedtides. Unlike its stereoisomer, L-tryptophan, it is not used in structural or enzyme proteins.
2. An essential amino acid found in naturally produced peptides. Unlike its stereoisomer, L-tryptophan, it is not used in structural or enzyme proteins.
3. D-Tryptophan is used for human embryonic kidney cell (HEK-293, ATCC: CRL-1573) culture. The product is a sweetener used to study the release of incretins from enteroendocrine cells triggered by sugar but not by sweeteners.

Definition

ChEBI: The D-enantiomer of tryptophan.

General Description

White solid.

Air & Water Reactions

Slightly soluble in water.

Reactivity Profile

Amines are chemical bases. They neutralize acids to form salts plus water. These acid-base reactions are exothermic. The amount of heat that is evolved per mole of amine in a neutralization is largely independent of the strength of the amine as a base. Amines may be incompatible with isocyanates, halogenated organics, peroxides, phenols (acidic), epoxides, anhydrides, and acid halides. Flammable gaseous hydrogen is generated by amines in combination with strong reducing agents, such as hydrides.

Fire Hazard

Flash point data are not available for D(+)-Tryptophan, but D(+)-Tryptophan is probably combustible.

Biochem/physiol Actions

Low level of D-tryptophan is capable of preventing the growth of an?L-tryptophan-requiring mutant of the?E. coli.

Check Digit Verification of cas no

The CAS Registry Mumber 153-94-6 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 1,5 and 3 respectively; the second part has 2 digits, 9 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 153-94:
(5*1)+(4*5)+(3*3)+(2*9)+(1*4)=56
56 % 10 = 6
So 153-94-6 is a valid CAS Registry Number.
InChI:InChI:1S/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)

153-94-6 Well-known Company Product Price

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  • TCI America

  • (T0539)  D-Tryptophan  >98.0%(HPLC)(T)

  • 153-94-6

  • 5g

  • 320.00CNY

  • Detail
  • TCI America

  • (T0539)  D-Tryptophan  >98.0%(HPLC)(T)

  • 153-94-6

  • 25g

  • 990.00CNY

  • Detail
  • Alfa Aesar

  • (A18426)  D-Tryptophan, 99%   

  • 153-94-6

  • 5g

  • 235.0CNY

  • Detail
  • Alfa Aesar

  • (A18426)  D-Tryptophan, 99%   

  • 153-94-6

  • 25g

  • 1038.0CNY

  • Detail
  • Alfa Aesar

  • (A18426)  D-Tryptophan, 99%   

  • 153-94-6

  • 100g

  • 3126.0CNY

  • Detail
  • Sigma

  • (T9753)  D-Tryptophan  ≥98.0% (HPLC)

  • 153-94-6

  • T9753-5G

  • 475.02CNY

  • Detail
  • Sigma

  • (T9753)  D-Tryptophan  ≥98.0% (HPLC)

  • 153-94-6

  • T9753-25G

  • 1,818.18CNY

  • Detail
  • Sigma

  • (T9753)  D-Tryptophan  ≥98.0% (HPLC)

  • 153-94-6

  • T9753-100G

  • 5,053.23CNY

  • Detail

153-94-6SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 11, 2017

Revision Date: Aug 11, 2017

1.Identification

1.1 GHS Product identifier

Product name D-tryptophan

1.2 Other means of identification

Product number -
Other names (2R)-2-amino-3-(1H-indol-3-yl)propanoic acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:153-94-6 SDS

153-94-6Synthetic route

C15H15N3*C18H14Cl2N2O3

C15H15N3*C18H14Cl2N2O3

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With benzylamine hydrochloride In water; isopropyl alcohol at 20℃; for 1h;95%
Indole-3-pyruvic acid
392-12-1

Indole-3-pyruvic acid

A

L-Tryptophan
73-22-3

L-Tryptophan

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With CC10H14NOSCH2CH2CH3N(CH3)2 (5); zinc diacetate In methanol at 30℃; Product distribution; pH 4.00;A 6%
B 94%
With 5-((3-(dimethylamino)propyl)thio)-4-(aminomethyl)-3-hydroxyl-5,6,7,8-tetraquinoline In methanol at 30℃; Product distribution; stereoselective transaminations at pH=4.00, various reagents;A 6 % Chromat.
B 94 % Chromat.
With phosphate buffer; 6A-monoimidazolyl-6B-(5'-thiopyridoxaminyl)-β-D-cyclodextrin In water at 25℃; Product distribution; other reragents, various pH;
indole
120-72-9

indole

L-serin
56-45-1

L-serin

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
Stage #1: indole; L-serin With Salmonella enterica tryptophan synthase In methanol; aq. phosphate buffer at 37℃; pH=8.0; Enzymatic reaction;
Stage #2: With (2R)-aspartic acid In methanol; aq. phosphate buffer pH=8.0;
Stage #3: In aq. phosphate buffer; deuteromethanol at 37℃; pH=8.0; Enzymatic reaction; stereoselective reaction;
69%
β-(3-indolyl)-α-ketopropanoic acid sodium salt
66872-76-2

β-(3-indolyl)-α-ketopropanoic acid sodium salt

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With zinc(II) perchlorate; (S)-15-amino-methyl-14-hydroxy-5,5-dimethyl-2,8-dithia<9>(2,5)pyridinophane In methanol for 24h; Ambient temperature;62%
D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With sodium hydroxide; oxygen; 2-amino-2-hydroxymethyl-1,3-propanediol In water at 30℃; for 8h; pH=7.3; Resolution of racemate; Enzymatic reaction; enantioselective reaction;48%

A

L-Tryptophan
73-22-3

L-Tryptophan

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With Bis(2-ethylhexyl)phosphoric acid; sodium dodecyl-sulfate; O,O'-dibenzoyl-L-tartaric acid In octanol; water at 20℃; for 4h; Reflux; Resolution of racemate; optical yield given as %ee; enantioselective reaction;A n/a
B 18.59%
With (2R,3R,11R,12R)-(+)-18-crown-6-2,3,11,12-tetracarbonic acid In acetonitrile at 25℃; pH=3; Electrochemical reaction;
With teicoplanin In methanol; water Product distribution; Further Variations:; Reagents; pH-values; Solvents;
D-Tryptophan methyl ester
4299-70-1, 7303-49-3, 22032-65-1

D-Tryptophan methyl ester

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With barium dihydroxide; water
With methanol; barium dihydroxide
With Streptomyces spp. 82F2 D-aminopeptidase In dimethyl sulfoxide at 20℃; for 0.0833333h; pH=6.5; aq. buffer; Enzymatic reaction;
N-acetyl-D-tryptophan
2280-01-5

N-acetyl-D-tryptophan

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With hydrogenchloride; water
With sulfuric acid; water
With barium dihydroxide; water
With D-aminoacylase; cobalt(II) chloride hexahydrate at 36 - 37℃; pH=7.4; aq. phosphate buffer; Enzymatic reaction;
Nα-chloroacetyl-D-tryptophan
742100-62-5

Nα-chloroacetyl-D-tryptophan

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With sulfuric acid; water
N-(benzyloxycarbonyl)-D-tryptophan
2279-15-4

N-(benzyloxycarbonyl)-D-tryptophan

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With methanol; palladium; acetic acid Hydrogenation;
indole
120-72-9

indole

L-serin
56-45-1

L-serin

A

2-oxo-propionic acid
127-17-3

2-oxo-propionic acid

B

L-Tryptophan
73-22-3

L-Tryptophan

C

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
N+C5Ala2C16; PL+C2N2C16; copper(II) perchlorate In water at 30℃; for 200h; Product distribution; aq. acetate buffer (pH 5.0, KCl), other catalysts, also with D-serine and DL-serine;
(3-indolylmethyl)trimethylammonium iodide
5457-31-8

(3-indolylmethyl)trimethylammonium iodide

glycine
56-40-6

glycine

A

L-Tryptophan
73-22-3

L-Tryptophan

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
Yield given. Multistep reaction;
With hydrogenchloride; sodium hydroxide; S-2-N-(N'-benzylprolyl)aminibenzophenone; sodium methylate 1.) methanol, 2.) acetonitrile, 20 deg C, 3 h, 3.) methanol, reflux; Yield given. Multistep reaction. Yields of byproduct given. Title compound not separated from byproducts;
DL-5-indolylmethylhydantoin

DL-5-indolylmethylhydantoin

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With potassium phosphate buffer; Pseudomonas sp. AJ-11220 In various solvent(s) at 30℃; for 2h;
With potassium phosphate buffer; Pseudomonas sp. AJ-11220 In various solvent(s) at 30℃; for 2h; pH 8.0; enzymatic reaction;
N-carbamyl-D-tryptophan
54896-75-2

N-carbamyl-D-tryptophan

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With potassium phosphate buffer; Pseudomonas sp. AJ-11220 In various solvent(s) at 30℃; for 2h;
With potassium phosphate buffer; Pseudomonas sp. AJ-11220 In various solvent(s) at 30℃; for 2h; pH 7.5; enzymatic reaction;
(S)-2-{(N-benzyl-2-pyrrolidinyl)carbonylamino}benzaldehyde
82704-14-1

(S)-2-{(N-benzyl-2-pyrrolidinyl)carbonylamino}benzaldehyde

A

L-Tryptophan
73-22-3

L-Tryptophan

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With hydrogenchloride; sodium methylate; nickel(II) nitrate Product distribution; 1.) MeOH, 40 deg C, 24 h, 2.) reflux;
H-Arg-D-Trp-NmePhe-D-Trp-Leu-Met-NH2

H-Arg-D-Trp-NmePhe-D-Trp-Leu-Met-NH2

A

L-arginine
74-79-3

L-arginine

B

N-Methyl-L-phenylalanine
2566-30-5

N-Methyl-L-phenylalanine

C

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With base In water Product distribution; other reagent;
D-tryptophan-ethyl ester

D-tryptophan-ethyl ester

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With sodium hydroxide; ethanol; water
D-tryptophan-isopropyl ester

D-tryptophan-isopropyl ester

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With hydrogenchloride; water
6A-(2-(2-(2-aminoethylamino)ethylamino)ethylamino)-6A-deoxy-β-cyclodextrin (R)-tryptophan complex

6A-(2-(2-(2-aminoethylamino)ethylamino)ethylamino)-6A-deoxy-β-cyclodextrin (R)-tryptophan complex

A

D-tryptophan
153-94-6

D-tryptophan

B

6A-(2-(2-(2-aminoethylamino)ethylamino)ethylamino)-6A-deoxy-β-cyclodextrin

6A-(2-(2-(2-aminoethylamino)ethylamino)ethylamino)-6A-deoxy-β-cyclodextrin

Conditions
ConditionsYield
With sodium perchlorate In water at 25.05℃; Equilibrium constant; Further Variations:; pH-values; decomplexation;
6A-deoxy-6A-(1,4,7,10-tetraazacyclododecan-1-yl)-β-cyclodextrin (R)-tryptophan complex

6A-deoxy-6A-(1,4,7,10-tetraazacyclododecan-1-yl)-β-cyclodextrin (R)-tryptophan complex

A

D-tryptophan
153-94-6

D-tryptophan

B

6A-deoxy-6A-(1,4,7,10-tetraazacyclododecan-1-yl)-β-cyclodextrin

6A-deoxy-6A-(1,4,7,10-tetraazacyclododecan-1-yl)-β-cyclodextrin

Conditions
ConditionsYield
With sodium perchlorate In water at 25.05℃; Equilibrium constant; Further Variations:; pH-values; decomplexation;
D-Tryptophan methyl ester
4299-70-1, 7303-49-3, 22032-65-1

D-Tryptophan methyl ester

A

methanol
67-56-1

methanol

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With 2-(di(2-hydroxyethyl)amino)ethanesulfonic acid; lipase from Bacillus thermocatenulanatus In water at 40℃; pH=7.20; Enzyme kinetics;
DL-tryptophan methyl ester
7303-49-3

DL-tryptophan methyl ester

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
Multi-step reaction with 2 steps
1: di-O-benzoyl-Lg-tartaric acid
2: Ba(OH)2; water
View Scheme
Multi-step reaction with 2 steps
1: beim Behandeln mit Pankreas-Enzym in wss. Loesung
2: Ba(OH)2; methanol
View Scheme
N-acetyl-DL-tryptophan
1218-34-4, 87-32-1

N-acetyl-DL-tryptophan

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
Multi-step reaction with 2 steps
1: beim Behandeln mit Hilfe von Amidase aus Aspergillus oryzae oder Penicillium vinaceum
2: H2SO4; water
View Scheme
Multi-step reaction with 2 steps
1: quinine
2: H2SO4; water
View Scheme
Multi-step reaction with 2 steps
1: brucine
2: HCl; water
View Scheme
N2-(chloroacetyl)-DL-tryptophan
79189-76-7

N2-(chloroacetyl)-DL-tryptophan

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
Multi-step reaction with 2 steps
1: pancreas-enzyme / arbeiten in wss. Loesung bei pH 7.6
2: H2SO4; water
View Scheme
(PPh3)2 PdCl2

(PPh3)2 PdCl2

1-acetamido-2-(3-indolyl)ethene

1-acetamido-2-(3-indolyl)ethene

2-(2-isopropyl-5-methylcyclohexyloxy)ethanol

2-(2-isopropyl-5-methylcyclohexyloxy)ethanol

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With CO In tetrahydrofuran; hydrogenchloride
1-acetamido-2-(3-indolyl)ethene

1-acetamido-2-(3-indolyl)ethene

2-(2-isopropyl-5-methylcyclohexyloxy)ethanol

2-(2-isopropyl-5-methylcyclohexyloxy)ethanol

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With CO; (PPh3)2PdCl2 In tetrahydrofuran; hydrogenchloride
trans-cyclo-(D-tryptophanyl-L-tyrosyl)
107911-05-7

trans-cyclo-(D-tryptophanyl-L-tyrosyl)

A

L-tyrosine
60-18-4

L-tyrosine

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With hydrogenchloride; water at 110℃; for 16h;
D-Alanine
338-69-2

D-Alanine

Indole-3-pyruvic acid
392-12-1

Indole-3-pyruvic acid

A

2-oxo-propionic acid
127-17-3

2-oxo-propionic acid

B

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With pyridoxal 5'-phosphate; recombinant Lactobacillus salivarius UCC118 D-amino acid aminotransferase In aq. phosphate buffer at 30℃; for 0.0166667h; pH=7.5; Enzymatic reaction;
methanol
67-56-1

methanol

D-tryptophan
153-94-6

D-tryptophan

Conditions
ConditionsYield
With thionyl chloride for 4h; Heating;100%
With thionyl chloride at 0 - 40℃; for 6h;98%
With thionyl chloride at 40℃; for 4h;97%
D-tryptophan
153-94-6

D-tryptophan

(R)-6-bromotryptophan
496930-10-0

(R)-6-bromotryptophan

Conditions
ConditionsYield
With oxygen; FAD-dependent tryptophan halogenase Thal; sodium bromide In isopropyl alcohol at 25℃; pH=7.4; Enzymatic reaction; chemoselective reaction;100%
With sodium hypophosphate; recombinant phosphite dehydrogenase; recombinant tryptophan C-6 flavin-dependent halogenase tar14 from Streptomyces coelicolor CH999; recombinant tryptophan C-6 flavin-dependent reductase tar15 from Escherichia coli; nicotinamide adenine dinucleotide phosphate; flavin adenine dinucleotide; sodium chloride In aq. buffer at 30℃; pH=7.6; Enzymatic reaction; regiospecific reaction;
With alcohol dehydrogenase from Rhodococcus spp; flavin reductase PrnF from Pseudomonas fluorescens; tryptophan 6-halogenase Thal fromStreptomyces albogriseolus; NAD; oxygen; flavin adenine dinucleotide; sodium bromide In aq. phosphate buffer; isopropyl alcohol at 25℃; pH=7.4; Reagent/catalyst; Enzymatic reaction;
trifluoroacetic acid
76-05-1

trifluoroacetic acid

D-tryptophan
153-94-6

D-tryptophan

C11H11BrN2O2*C2HF3O2

C11H11BrN2O2*C2HF3O2

Conditions
ConditionsYield
Stage #1: D-tryptophan With flavin adenine dinucleotide fully reduced neutral; NAD; oxygen; isopropyl alcohol; sodium bromide In aq. phosphate buffer at 25℃; pH=7.4; Enzymatic reaction;
Stage #2: trifluoroacetic acid In acetonitrile
100%
piperonal
120-57-0

piperonal

D-tryptophan
153-94-6

D-tryptophan

C19H18N2O5

C19H18N2O5

Conditions
ConditionsYield
In acetonitrile at 20℃; Product distribution / selectivity; Inert atmosphere of nitrogen;99.8%
methanol
67-56-1

methanol

D-tryptophan
153-94-6

D-tryptophan

D-Tryptophan methyl ester
4299-70-1, 7303-49-3, 22032-65-1

D-Tryptophan methyl ester

Conditions
ConditionsYield
With sulfuric acid for 2h; Time; Reflux; Large scale;99.4%
Stage #1: methanol; D-tryptophan With thionyl chloride for 18h; Reflux;
Stage #2: With sodium carbonate
93%
With thionyl chloride at 10 - 45℃; for 2h; Large scale;93.6%
D-tryptophan
153-94-6

D-tryptophan

trimellitic Anhydride
552-30-7

trimellitic Anhydride

(R)-2-(1-carboxy-2-(1H-indol-3-yl)ethyl)-1,3-dioxoisoindoline-5-carboxylic acid

(R)-2-(1-carboxy-2-(1H-indol-3-yl)ethyl)-1,3-dioxoisoindoline-5-carboxylic acid

Conditions
ConditionsYield
In diethylene glycol dimethyl ether at 200℃; for 0.166667h; microwave irradiation;99%
D-tryptophan
153-94-6

D-tryptophan

(2R)-2-amino-3-(1H-indol-3-yl)propan-1-ol
154-09-6, 526-53-4, 2899-29-8, 52485-52-6

(2R)-2-amino-3-(1H-indol-3-yl)propan-1-ol

Conditions
ConditionsYield
With lithium aluminium tetrahydride In tetrahydrofuran for 15h; Inert atmosphere; Reflux;98%
With lithium aluminium tetrahydride In tetrahydrofuran at 0℃; Reflux;98%
With dimethyl sulfide borane In tetrahydrofuran Reflux;92%
(R)-1-benzotriazol-1-yl-3,3,3-trifluoro-2-methoxy-2-phenylpropan-1-one
942130-82-7

(R)-1-benzotriazol-1-yl-3,3,3-trifluoro-2-methoxy-2-phenylpropan-1-one

D-tryptophan
153-94-6

D-tryptophan

(R)-3-(1H-indol-3-yl)-2-((R)-3,3,3-trifluoro-2-methoxy-2-phenylpropionylamino)propionic acid

(R)-3-(1H-indol-3-yl)-2-((R)-3,3,3-trifluoro-2-methoxy-2-phenylpropionylamino)propionic acid

Conditions
ConditionsYield
With triethylamine In water; acetonitrile at 20℃; for 12h;98%
succinic acid anhydride
108-30-5

succinic acid anhydride

D-tryptophan
153-94-6

D-tryptophan

(R)-N-[1-carboxy-2-(1H-indol-3-yl)ethyl]succinamic acid

(R)-N-[1-carboxy-2-(1H-indol-3-yl)ethyl]succinamic acid

Conditions
ConditionsYield
In tetrahydrofuran for 40h; Heating;96%
pentan-3-one
96-22-0

pentan-3-one

D-tryptophan
153-94-6

D-tryptophan

1,1-diethyl-2,3,4,9-tetrahydro-1H-β-carboline-3-carboxylic acid

1,1-diethyl-2,3,4,9-tetrahydro-1H-β-carboline-3-carboxylic acid

Conditions
ConditionsYield
With trifluoroacetic acid In dichloromethane at 20℃; Pictet-Spengler reaction;96%
benzaldehyde
100-52-7

benzaldehyde

D-tryptophan
153-94-6

D-tryptophan

N-benzyl-D-tryptophan
888009-83-4

N-benzyl-D-tryptophan

Conditions
ConditionsYield
With sodium cyanoborohydride In methanol95%
With sodium cyanoborohydride In methanol at 20℃; for 24h;
Stage #1: benzaldehyde; D-tryptophan In methanol at 23℃; for 2h;
Stage #2: With sodium cyanoborohydride In methanol at 0℃; for 15h;
benzyl chloroformate
501-53-1

benzyl chloroformate

D-tryptophan
153-94-6

D-tryptophan

N-(benzyloxycarbonyl)-D-tryptophan
2279-15-4

N-(benzyloxycarbonyl)-D-tryptophan

Conditions
ConditionsYield
With sodium hydrogencarbonate; potassium carbonate In water; acetone at 30℃; for 3h; pH=8 - 10; Cooling with ice;94%
With sodium hydroxide88%
With sodium hydroxide74%
With sodium hydroxide In water at 0 - 20℃;
Stage #1: D-tryptophan With sodium hydrogencarbonate; sodium carbonate In water; acetonitrile at 0℃; for 0.25h; pH=10 - Ca. 11; Cooling with ice;
Stage #2: benzyl chloroformate In water; acetonitrile at 0 - 20℃; for 3h;
methanol
67-56-1

methanol

toluene-4-sulfonic acid
104-15-4

toluene-4-sulfonic acid

D-tryptophan
153-94-6

D-tryptophan

(R)-2-Amino-3-(1H-indol-3-yl)-propionic acid methyl ester; compound with toluene-4-sulfonic acid

(R)-2-Amino-3-(1H-indol-3-yl)-propionic acid methyl ester; compound with toluene-4-sulfonic acid

Conditions
ConditionsYield
With p-toluenesulfonyl chloride at 75℃; for 4h;94%
With p-toluenesulfonyl chloride for 20h; Heating;
1,4,5,8-naphthalenetetracarboxylic dianhydride
81-30-1

1,4,5,8-naphthalenetetracarboxylic dianhydride

D-tryptophan
153-94-6

D-tryptophan

(R)-2-{7-[1-carboxy-2-(1H-indol-3-yl)ethyl]-1,3,6,8-tetraoxo-3,6,7,8-tetrahydro-1H-benzo[lmn][3,8]phenanthrolin-2-yl}-3-(1H-indol-3-yl)propionic acid

(R)-2-{7-[1-carboxy-2-(1H-indol-3-yl)ethyl]-1,3,6,8-tetraoxo-3,6,7,8-tetrahydro-1H-benzo[lmn][3,8]phenanthrolin-2-yl}-3-(1H-indol-3-yl)propionic acid

Conditions
ConditionsYield
With pyridine for 12h; Heating;94%
carbonic acid dimethyl ester
616-38-6

carbonic acid dimethyl ester

D-tryptophan
153-94-6

D-tryptophan

D-Tryptophan methyl ester
4299-70-1, 7303-49-3, 22032-65-1

D-Tryptophan methyl ester

Conditions
ConditionsYield
With sulfuric acid at 92℃; for 18h;94%
S-benzoyl-3-mercaptopropanoyl chloride
67714-30-1

S-benzoyl-3-mercaptopropanoyl chloride

D-tryptophan
153-94-6

D-tryptophan

N2-(S-benzoyl-3-mercaptopropanoyl)-D-tryptophan
78818-49-2

N2-(S-benzoyl-3-mercaptopropanoyl)-D-tryptophan

Conditions
ConditionsYield
With potassium carbonate In water93%
1,2-Cyclohexanedicarboxylic acid-anhydride
85-42-7

1,2-Cyclohexanedicarboxylic acid-anhydride

D-tryptophan
153-94-6

D-tryptophan

(R)-2-(1,3-dioxooctahydroisoindol-2-yl)-3-(1H-indol-3-yl)propionic acid

(R)-2-(1,3-dioxooctahydroisoindol-2-yl)-3-(1H-indol-3-yl)propionic acid

Conditions
ConditionsYield
With pyridine for 12h; Heating;92%
2-nitrobenzyl chloride
610-14-0

2-nitrobenzyl chloride

D-tryptophan
153-94-6

D-tryptophan

(R)-3-(1H-indol-3-yl)-2-(2-nitrobenzamido)propanoic acid
1173180-35-2

(R)-3-(1H-indol-3-yl)-2-(2-nitrobenzamido)propanoic acid

Conditions
ConditionsYield
With sodium hydroxide In tetrahydrofuran; water at 0℃; Ionic liquid;91%
With sodium hydroxide In tetrahydrofuran; water at 0℃; for 2h; Reagent/catalyst;90%
With sodium hydroxide In tetrahydrofuran at 0℃; for 2h;1.59 g
(methylamino)acetonitrile
5616-32-0

(methylamino)acetonitrile

D-tryptophan
153-94-6

D-tryptophan

C14H16N4O

C14H16N4O

Conditions
ConditionsYield
With dmap; 1-ethyl-(3-(3-dimethylamino)propyl)-carbodiimide hydrochloride In tetrahydrofuran at 20℃; for 5h; Solvent; Temperature;91%
allyl alcohol
107-18-6

allyl alcohol

D-tryptophan
153-94-6

D-tryptophan

H-D-Trp-OAll

H-D-Trp-OAll

Conditions
ConditionsYield
With toluene-4-sulfonic acid In toluene at 25 - 95℃;90.3%
With toluene-4-sulfonic acid In toluene at 25 - 95℃;90%
With toluene-4-sulfonic acid In toluene at 25 - 95℃;90.2%
trifluoroacetic anhydride
407-25-0

trifluoroacetic anhydride

D-tryptophan
153-94-6

D-tryptophan

4-(3-indolylmethyl)-2-trifluoromethyl-5(4H)-oxazolone
126689-19-8

4-(3-indolylmethyl)-2-trifluoromethyl-5(4H)-oxazolone

Conditions
ConditionsYield
In diethyl ether at 30℃; for 0.166667h;90%
α-ethyl D-N-carbobenzoxyglutamate
97996-97-9

α-ethyl D-N-carbobenzoxyglutamate

D-tryptophan
153-94-6

D-tryptophan

Cbz-D-Glu(D-Trp-OH)-O-Et
1382326-14-8

Cbz-D-Glu(D-Trp-OH)-O-Et

Conditions
ConditionsYield
Stage #1: α-ethyl D-N-carbobenzoxyglutamate With 1-hydroxy-pyrrolidine-2,5-dione; 1-ethyl-(3-(3-dimethylamino)propyl)-carbodiimide hydrochloride In N,N-dimethyl-formamide at 20℃; Cooling with ice-water;
Stage #2: D-tryptophan In N,N-dimethyl-formamide at 20℃; Cooling with ice-water;
Stage #3: With hydrogenchloride In water; N,N-dimethyl-formamide Cooling with ice;
90%
benzyl chloride
100-44-7

benzyl chloride

D-tryptophan
153-94-6

D-tryptophan

D-tryptophan benzyl ester
141595-98-4

D-tryptophan benzyl ester

Conditions
ConditionsYield
With Iron(III) nitrate nonahydrate; ammonia; sodium Reflux;89%
piperonal
120-57-0

piperonal

D-tryptophan
153-94-6

D-tryptophan

(1R,3R)-1,2,3,4-tetrahydro-1-(3,4-methylenedioxyphenyl)-9H-pyrido[3,4-b]indole-3-carboxylic acid
406938-39-4

(1R,3R)-1,2,3,4-tetrahydro-1-(3,4-methylenedioxyphenyl)-9H-pyrido[3,4-b]indole-3-carboxylic acid

Conditions
ConditionsYield
Stage #1: piperonal; D-tryptophan With trifluoroacetic acid at 30 - 40℃; for 25h; Inert atmosphere;
Stage #2: With hydrogenchloride In water at 40 - 50℃; for 17h; Temperature; Inert atmosphere;
88.5%
1-benzyl N-carbobenzoxy-L-glutamate
65706-99-2

1-benzyl N-carbobenzoxy-L-glutamate

D-tryptophan
153-94-6

D-tryptophan

Cbz-D-Glu(D-Trp-OH)-O-Bzl
1382326-04-6

Cbz-D-Glu(D-Trp-OH)-O-Bzl

Conditions
ConditionsYield
Stage #1: 1-benzyl N-carbobenzoxy-L-glutamate With 1-hydroxy-pyrrolidine-2,5-dione; 1-ethyl-(3-(3-dimethylamino)propyl)-carbodiimide hydrochloride In N,N-dimethyl-formamide at 20℃; Cooling with ice-water;
Stage #2: D-tryptophan In N,N-dimethyl-formamide at 20℃; for 6h; Cooling with ice-water;
Stage #3: With hydrogenchloride In water; N,N-dimethyl-formamide Product distribution / selectivity; Cooling with ice;
88%
1,8-Naphthalic anhydride
81-84-5

1,8-Naphthalic anhydride

D-tryptophan
153-94-6

D-tryptophan

2-(1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)-3-(1H-indol-3-yl)-propionic acid

2-(1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)-3-(1H-indol-3-yl)-propionic acid

Conditions
ConditionsYield
In dimethyl sulfoxide at 150℃; for 0.5h;87%
2-Phenyl-iso-propyloxycarbonylfluorid
73167-00-7

2-Phenyl-iso-propyloxycarbonylfluorid

D-tryptophan
153-94-6

D-tryptophan

Ppoc-D-Trp
116246-59-4

Ppoc-D-Trp

Conditions
ConditionsYield
With sodium hydroxide; sodium hydrogencarbonate In tetrahydrofuran; diethyl ether at 0℃; for 2h;86%
di-tert-butyl dicarbonate
24424-99-5

di-tert-butyl dicarbonate

D-tryptophan
153-94-6

D-tryptophan

Boc-D-Trp-OH
5241-64-5

Boc-D-Trp-OH

Conditions
ConditionsYield
With triethylamine In methanol Inert atmosphere;86%
With sodium hydroxide In tetrahydrofuran; water at 0℃;

153-94-6Relevant articles and documents

A facile enantioseparation for amino acids enantiomers using β-cyclodextrins functionalized Fe3O4 nanospheres

Chen, Xin,Rao, Jinan,Wang, Jin,Gooding, J. Justin,Zou, Gang,Zhang, Qijin

, p. 10317 - 10319 (2011)

Herein is presented a strategy for the enantioseparation of amino acids enantiomers using β-CD functionalized Fe3O4 nanospheres, in which β-CD provides the ability to chirally discriminate amino acids enantiomers, while the Fe3O4 nanoparticles serve as magnetic separators.

Amino acid ionic liquids as chiral ligands in ligand-exchange chiral separations

Liu, Qian,Wu, Kangkang,Tang, Fei,Yao, Lihua,Yang, Fei,Nie, Zhou,Yao, Shouzhuo

, p. 9889 - 9896 (2009)

Recently, amino acid ionic liquids (AAILs) have attracted much research interest. In this paper, we present the first application of AAILs in chiral separation based on the chiral ligand exchange principle. By using 1alkyl-3-methylimidazolium L-proline (L-Pro) as a chiral ligand coordinated with copper(II), four pairs of underivatized amino acid enantiomers - DLphenylalanine (DL-Phe), DL-histidine (DL-His), DL-tryptophane (DL-Trp), and DL-tyrosine (DL-Tyr) - were successfully separated in two major chiral separation techniques, HPLC and capillary electrophoresis (CE), with higher enantioselectivity than conventionally used amino acid ligands (resolution (Rs) = 3.26-10.81 for HPLC; Rs = 1.34-4.27 for CE). Interestingly, increasing the alkyl chain length of the AAIL cation remarkably enhanced the enantioselectivity. It was inferred that the alkylmethylimidazolium cations and L-Pro form ion pairs on the surface of the sta-tionary phase or on the inner surface of the capillary. The ternary copper complexes with L-Pro are consequently attached to the support surface, thus inducing an ion-exchange type of retention for the DL-enantiomers. Therefore, the AAIL cation plays an essential role in the separation. This work demonstrates that AAILs are good alternatives to conventional amino acid ligands for ligand-exchange-based chiral separation. It also reveals the tremendous application potential of this new type of task-specific ILs.

Structure elucidation of a new natural diketopiperazine from a Microbispora aerata strain isolated from Livingston Island, Antarctica

Ivanova, Veneta,Laatsch, Hartmut,Kolarova, Mariana,Aleksieva, Krasja

, p. 164 - 170 (2013)

A new natural diketopiperazine (1) was obtained from the culture broth of Microbispora aerata strain imbas-11A, isolated from penguin excrements collected on the Antarctic Livingston Island. Compound 1 was purified consecutively by solvent extraction, silica gel column chromatography and preparative HPLC. The structure of the compound was elucidated by 1D and 2D NMR experiments and mass spectrometric investigations. The absolute configuration of compound 1 was determined by amino acid analysis and NOESY correlations. A low antiproliferative and cytotoxic effect of trans-cyclo-(D-tryptophanyl-L-tyrosyl) (1) was determined with L-929 mouse fibroblast cells, K-562 human leukemia cells and HeLa human cervix carcinoma. Trans-cyclo-(D-tryptophanyl-L-tyrosyl) (1) did not show antimicrobial activity at a concentration of 50 μg per disc against Bacillus subtilis, Staphylococcus aureus, Streptomyces viridochromogenes, Escherichia coli, Candida albicans and Mucor miehei.

Targeted Isolation of Asperheptatides from a Coral-Derived Fungus Using LC-MS/MS-Based Molecular Networking and Antitubercular Activities of Modified Cinnamate Derivatives

Chao, Rong,Hou, Xue-Mei,Xu, Wei-Feng,Hai, Yang,Wei, Mei-Yan,Wang, Chang-Yun,Gu, Yu-Cheng,Shao, Chang-Lun

, p. 11 - 19 (2021)

Under the guidance of MS/MS-based molecular networking, four new cycloheptapeptides, namely, asperheptatides A-D (1-4), were isolated together with three known analogues, asperversiamide A-C (5-7), from the coral-derived fungus Aspergillus versicolor. The planar structures of the two major compounds, asperheptatides A and B (1 and 2), were determined by comprehensive spectroscopic data analysis. The absolute configurations of the amino acid residues were determined by advanced Marfey's method. The two structurally related trace metabolites, asperheptatides C and D (3 and 4), were characterized by ESI-MS/MS fragmentation methods. A series of new derivatives (8-26) of asperversiamide A (5) were semisynthesized. The antitubercular activities of 1, 2, and 5-26 against Mycobacterium tuberculosis H37Ra were also evaluated. Compounds 9, 13, 23, and 24 showed moderate activities with MIC values of 12.5 μM, representing a potential new class of antitubercular agents.

Coordination properties of 3-functionalised β-cyclodextrins: Thermodynamic stereoselectivity of copper(II) complexes of the 3-histamine derivative and its exploitation in ligand-exchange capillary electrophoresis

Giuffrida, Alessandro,Cucinotta, Vincenzo,MacCarrone, Giuseppe,Messina, Marianna,Rizzarelli, Enrico,Vecchio, Graziella

, p. 377 - 383 (2014)

A histamine derivative of β-cyclodextrin functionalised at the secondary rim was synthesised and characterised by optical and NMR spectroscopy. Its binary systems both with proton and copper(II) were thermodynamically characterised through pH-metric potentiometry. In addition, the ternary systems with the enantiomers of tryptophan, phenylalanine and alanine were investigated. Thermodynamic stereoselectivity was observed for both the tryptophan and phenylalanine enantiomers. The properties of the synthesised cyclodextrin derivative as a chiral selector were verified in chiral ligand-exchange capillary electrophoresis (CLECE) towards the enantiomeric pairs of some amino acids. A β-cyclodextrin histamine-functionalised at the secondary rim was synthesised and characterised as a chiral selector of aromatic amino acids.

Reversal of optical induction in transamination by regioisomeric bifunctionalized cyclodextrins

Fasella, Elisabetta,Dong, Steven D.,Breslow, Ronald

, p. 709 - 714 (1999)

Two isomeric compounds have been synthesized carrying a pyridoxamine on C-6 of β-cyclodextrin and an imidazole unit on C-6 of the neighboring glucose residue. Each one stereoselectively transaminates phenylpyruvic acid to produce phenylalanine, and with opposite stereochemical preferences. Structure determinations by X-ray crystallography and NMR spectroscopy indicate that the imidazole units serve to block proton addition from their side, rather than acting to protonate the transamination intermediates. Related cyclodextrin-pyridoxamine compounds had been reported carrying ethylenediamine units instead of imidazoles, and high enantioselectivities in transamination were claimed. Our work indicates that these claims are incorrect, and that only poor selectivities are seen that are often unrelated to the position of the ethylenediamine units. Neither of these transaminating systems yet approaches the enantioselectivity seen with a pyridoxamine carrying a chirally mounted internal base group. Copyright (C) 1999 Elsevier Science Ltd.

Protein Engineering of d-Succinylase from Cupriavidus sp. for d-Amino Acid Synthesis and the Structural Implications

Azuma, Masayuki,Kumagai, Shinya,Nishiya, Yoshiaki,Sumida, Yosuke,Yamada, Toshihide,Yamasaki, Masayuki

, p. 4770 - 4778 (2021)

d-Amino acids are important chiral building blocks for pharmaceuticals and agrochemicals. Previously, we have used d-Succinylase (DSA) from Cupriavidus sp. P4-10-C and N-succinyl amino acid racemase (NSAR, EC.4.2.1.113) from Geobacillus stearothermophilus NCA1503 to produce d-amino acids via the dynamic kinetic resolution of N-succinyl-dl-amino acids. However, the use of this bioconversion system remains challenging for industrial application due to the insufficient enantioselectivity of DSA toward N-succinyl-d-amino acids. Therefore, we screened DSA mutants for improved enantioselectivity by directed evolution. Several mutants showed improved enantioseletivity compared to wild-type DSA. L182E mutant had superior enantioselectivity, and the thermal stability was also remarkably improved by this single mutation. We solved the crystal structure of the L182E mutant in complex with succinic acids at a resolution 2.0 ?. The mutated residues in all generated mutants that showed improved enantioselectivity (including the substituted Glu182 in the L182E mutant) are found very close to the active site. The solved crystal structure also provides some rationale to explain the higher thermostability of the L182E mutant compared to wild-type DSA. d-phenylalanine and d-tryptophan were produced in high conversion (approximately 90%) with 98.8% ee and 99.6% ee, respectively, using coupled L182E DSA and NSAR with the one-pot enzymatic method. These data suggested that L182E DSA may be a useful biocatalyst for industrial d-amino acids production. (Figure presented.).

Hydrogen Bond Assisted l to d Conversion of α-Amino Acids

Chin, Jik,Fu, Rui,Lough, Alan J.,So, Soon Mog

, p. 4335 - 4339 (2020)

l to d conversion of unactivated α-amino acids was achieved by solubility-induced diastereomer transformation (SIDT). Ternary complexes of an α-amino acid with 3,5-dichlorosalicylaldehyde and a chiral guanidine (derived from corresponding chiral vicinal diamine) were obtained in good yield as diastereomerically pure imino acid salt complexes and were hydrolysed to obtain enantiopure α-amino acids. A combination of DFT computation, NMR spectroscopy, and crystal structure provide detailed insight into how two types of strong hydrogen bonds assist in rapid epimerization of the complexes that is essential for SIDT.

Preparative separation of enantiomers based on functional nucleic acids modified gold nanoparticles

Huang, Rong,Wang, Daifang,Liu, Shuzhen,Guo, Longhua,Wang, Fangfang,Lin, Zhenyu,Qiu, Bin,Chen, Guonan

, p. 751 - 756 (2013)

The preparative-scale separation of chiral compounds is vitally important for the pharmaceutical industry and related fields. Herein we report a simple approach for rapid preparative separation of enantiomers using functional nucleic acids modified gold nanoparticles (AuNPs). The separation of DL-tryptophan (DL-Trp) is demonstrated as an example to show the feasibility of the approach. AuNPs modified with enantioselective aptamers were added into a racemic mixture of DL-Trp. The aptamer-specific enantiomer (L-Trp) binds to the AuNPs surface through aptamer-L-Trp interaction. The separation of DL-Trp is then simply accomplished by centrifugation: the precipitate containing L-Trp bounded AuNPs is separated from the solution, while the D-Trp remains in the supernatant. The precipitate is then redispersed in water. The aptamer is denatured under 95 °C and a second centrifugation is then performed, resulting in the separation of AuNPs and L-Trp. The supernatant is finally collected to obtain pure L-Trp in water. The results show that the racemic mixture of DL-Trp is completely separated into D-Trp and L-Trp, respectively, after 5 rounds of repeated addition of fresh aptamer-modified AuNPs to the DL-Trp mixture solution. Additionally, the aptamer-modified AuNPs can be repeatedly used for at least eight times without significant loss of its binding ability because the aptamer can be easily denatured and renatured in relatively mild conditions. The proposed approach could be scaled up and extended to the separation of other enantiomers by the adoption of other enantioselective aptamers. Chirality 25:751-756, 2013. 2013 Wiley Periodicals, Inc.

ASYMMETRIC SYNTHESIS OF α-AMINO ACIDS BY NONENZYMATIC TRANSAMINATION. VERSATILITY OF THE REACTION AND ENANTIOMERIC EXCESS OF THE PRODUCTS

Tachibana, Yoji,Ando, Makoto,Kuzuhara, Hiroyoshi

, p. 1765 - 1768 (1982)

Diverse α-keto acids were transformed into the corresponding α-amino acids enantiomeric excess ranging from 60 to 96percent by the reaction with chiral pyridoxamine analog, (R)- or (S)-15-aminomethyl-14-hydroxy-5,5-dimethyl-2,8-dithia(2,5)pyridinophane (4), and Zn2+ in the molar ratio of 2:1, in methanol.The use of the S enantiomer of 4 gave (R)-α-amino acids, and vice versa.

METHODS FOR PRODUCING D-TRYPTOPHAN AND SUBSTITUTED D-TRYPTOPHANS

-

Page/Page column 6; 10-11; 17, (2021/04/01)

Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism; and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. As disclosed herein, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted D-tryptophan analogs in high enantiomeric excess.

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