154-08-5

Basic information

• Product Name: 5-FLUORO-DL-TRYPTOPHAN
• Synonyms: H-DL-TRP(5-F)-OH;H-5-FLUORO-DL-TRP-OH;DL-5-FLUOROTRYPTOPHAN;DL-2-AMINO-3-(5-FLUOROINDOLYL)PROPIONIC ACID;2-AMINO-3-(5-FLUORO-1H-INDOL-3-YL)PROPANOIC ACID;5-FLUORO-DL-TRYPTOPHAN;TIMTEC-BB SBB003340;5-fluorotryptophan
• CAS NO: 154-08-5
• Molecular Formula: C₁₁H₁₁FN₂O₂
• Molecular Weight: 222.22
• EINECS: 205-822-5
• Product Categories: Indoles and derivatives;Amino Acids 13C, 2H, 15N;Amino Acids & Derivatives;FA - FLPeptide Synthesis;Alphabetic;F;A - HPeptide Synthesis;Amino Acids;Modified Amino Acids;Tryptophan Derivatives;Unnatural Amino Acid Derivatives
• Mol File: 154-08-5.mol
• Article Data: 1

Chemical Properties

• Melting Point: 265 °C (dec.)(lit.)
• Boiling Point: 450.71 °C at 760 mmHg
• Flash Point: 226.382 °C
• Appearance: white/powder
• Density: 1.2556 (estimate)
• Vapor Pressure: 6.54E-09mmHg at 25°C
• Refractive Index: 1.673
• Storage Temp.: 2-8°C
• PKA: 2.21±0.10(Predicted)
• BRN: 22753
• CAS DataBase Reference: 5-FLUORO-DL-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: 5-FLUORO-DL-TRYPTOPHAN(154-08-5)
• EPA Substance Registry System: 5-FLUORO-DL-TRYPTOPHAN(154-08-5)

Safety Data

• Hazard Codes: Xi
• Statements: 36/38
• Safety Statements: 22-24/25
• WGK Germany: 3
• RTECS: YN6825000
• Hazardous Substances Data: 154-08-5(Hazardous Substances Data)

Usage

Chemical Properties

light beige powder

Uses

A metabolic antagonist of tryptophan

Definition

ChEBI: A non-proteinogenic alpha-amino acid that is tryptophan in which the hydrogen at position 5 on the indole ring is replaced by a fluoro group.

Purification Methods

Recrystallise it from EtOH, aqueous EtOH or AcOH. Also purify it by passage through a Dowex AG1x2 (acetate form) column and recrystallise the L-enantiomer (from enzymic enrichment) from H2O/EtOH, m 158-163o(dec), [] D -8.3o (c 2.5, N NaOH). [Coy et al. Biochemistry 13 3550 1974, Beilstein 22/14 V 116.]

InChI:InChI=1/C11H11FN2O2/c12-7-1-2-10-8(4-7)6(5-14-10)3-9(13)11(15)16/h1-2,4-5,9,14H,3,13H2,(H,15,16)/t9-/m1/s1

Upstream product

• 154170-01-1 ethyl 2-amino-3-(5-fluoro-1H-indol-3-yl)propanoate 
• 1017683-44-1 (5-fluoro-3-indolylmethyl)trimethylammonium iodide 
• 399-52-0 5-fluoro-1H-indole 
• 343-90-8 3-dimethylaminomethyl-5-fluoroindole 
• 427-87-2 acetylamino-[3-(4-fluoro-phenylhydrazono)-propyl]-malonic acid diethyl ester 
• 428-79-5 acetylamino-(5-fluoro-indol-3-ylmethyl)-malonic acid diethyl ester 
• 363-37-1 acetylamino-(5-fluoro-indol-3-ylmethyl)-malonic acid 

Downstream Products

• 576-16-9 5-fluorotryptamine 
• 7730-20-3 DL-6-fluorotryptophan 
• 343-91-9 D-5-fluorotryptophan 
• 67337-05-7 2-((tert-butoxycarbonyl)amino)-3-(5-fluoro-1H-indol-3-yl)propanoic acid 
• 1422431-05-7 C₃₇H₃₃FN₆O₇ 
• 1422430-97-4 C₃₆H₃₁FN₆O₇ 
• 1403850-91-8 (2S)-N-((3S,6S)-3-(tert-butyl)-1⁹-fluoro-2⁴-(4-(hydroxymethyl)oxazol-2-yl)-5-oxo-1^5a,1^10bdihydro-1⁶H-4-aza-1(10b,2)-benzofuro[2,3-b]indola-2(5,2)-oxazolacycloheptaphane-6-yl)-2-hydroxy-3-methylbutanamide 
• 1403851-24-0 C₃₈H₃₄FN₅O₈ 
• 1403851-23-9 C₃₈H₃₈FN₅O₉ 
• 1403851-22-8 C₃₄H₃₁FN₄O₇ 
• 1403851-21-7 C₃₅H₃₃FN₄O₇ 
• 1403851-19-3 C₃₅H₃₅FN₄O₇ 
• 1422430-43-0 C₂₆H₂₆FN₃O₅ 
• 1403851-18-2 C₂₆H₃₀FN₃O₅ 

Relevant articles and documents

Biosynthesis of violacein, structure and function of L-tryptophan oxidase VioA from chromobacterium violaceum

Violacein is a natural purple pigment of Chromobacterium violaceum with potential medical applications as antimicrobial, antiviral, and anticancer drugs. The initial step of violacein biosynthesis is the oxidative conversion of L-tryptophan into the corresponding α-imine catalyzed by the flavoenzyme L-tryptophan oxidase (VioA). A substrate-related (3-(1H-indol-3-yl)-2-methylpropanoic acid) and a product-related (2-(1H-indol-3-ylmethyl)prop-2-enoic acid) competitive VioA inhibitor was synthesized for subsequent kinetic and x-ray crystallographic investigations. Structures of the binary VioA?FADH2 and of the ternary VioA?FADH2 ?2-(1H-indol-3-ylmethyl)prop-2-enoic acid complex were resolved. VioA forms a "loosely associated" homodimer as indicated by small-angle x-ray scattering experiments. VioA belongs to the glutathione reductase family 2 of FAD-dependent oxidoreductases according to the structurally conserved cofactor binding domain. The substrate-binding domain of VioA is mainly responsible for the specific recognition of L-tryptophan. Other canonical amino acids were efficiently discriminated with a minor conversion of L-phenylalanine. Furthermore, 7-aza-tryptophan, 1-methyl-tryptophan, 5-methyl-tryptophan, and 5-fluoro-tryptophan were efficient substrates of VioA. The ternary product-related VioA structure indicated involvement of protein domain movement during enzyme catalysis. Extensive structure-based mutagenesis in combination with enzyme kinetics (using L-tryptophan and substrate analogs) identified Arg64 , Lys269 , and Tyr309 as key catalytic residues of VioA. An increased enzyme activity of protein variant H163A in the presence of L-phenylalanine indicated a functional role of His163 in substrate binding. The combined structural and mutational analyses lead to the detailed understanding of VioA substrate recognition. Related strategies for the in vivo synthesis of novel violacein derivatives are discussed.