13567-14-1

Basic information

• Product Name: 6-hydroxy-L-tryptophan
• Synonyms: 6-hydroxy-L-tryptophan;L-Tryptophan, 6-hydroxy-;(S)-2-Amino-3-(6-hydroxy-1H-indol-3-yl)propanoic acid
• CAS NO: 13567-14-1
• Molecular Formula: C₁₁H₁₂N₂O₃
• Molecular Weight: 220.22458
• EINECS: -0
• Mol File: 13567-14-1.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• Storage Temp.: Keep in dark place,Inert atmosphere,Store in freezer, under -20°C
• CAS DataBase Reference: 6-hydroxy-L-tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 6-hydroxy-L-tryptophan(13567-14-1)
• EPA Substance Registry System: 6-hydroxy-L-tryptophan(13567-14-1)

Safety Data

• Hazardous Substances Data: 13567-14-1(Hazardous Substances Data)

Usage

General Description

6-hydroxy-L-tryptophan is a chemical compound derived from the amino acid tryptophan. It is a hydroxylated derivative of tryptophan, containing a hydroxyl group (-OH) attached to the sixth carbon atom of the tryptophan molecule. 6-hydroxy-L-tryptophan has been of interest in scientific research due to its potential biological activities, including antioxidant and anti-inflammatory properties. 6-hydroxy-L-tryptophan has also been studied for its potential role in the synthesis of neurotransmitters and its potential use in the pharmaceutical industry for the development of new drugs. Additionally, it has been found in some natural sources such as certain foods and plants.

Upstream product

• 73-22-3 L-Tryptophan 
• 2380-86-1 6-hydroxy-1H-indole 
• 56-45-1 L-serin 

Downstream Products

• 179669-87-5 N-Boc-6-hydroxy-L-tryptophan 

Relevant articles and documents

Isolation of 6-hydroxy-L-tryptophan from the fruiting body of Lyophyllum decastes for use as a tyrosinase inhibitor

Tyrosinase is the key enzyme that controls melanin formation. We found that a hot water extract of the lyophilized fruiting body of the fungus Lyophyllum decastes inhibited tyrosinase from Agaricus bisporus. The extract was fractionated by ODS column chromatography, and an active compound was obtained by purification through successive preparative HPLC using an ODS and a HILIC column. Using spectroscopic data, the compound was identified to be an uncommon amino acid, 6-hydroxytryptophan. 6-Hydroxy-L-tryptophan and 6-hydroxy-D-tryptophan were prepared through a Fenton reaction from L-tryptophan and D-tryptophan, respectively. The active compound was determined to be 6-hydroxy-L-tryptophan by comparison of their circular dichroism spectra and retention time on HPLC analysis of the Nα-(5-fluoro-2,4-dinitrophenyl)-L-leuciamide derivative with those of 6-hydroxy-L-tryptophan and 6-hydroxy-D-tryptophan. A Lineweaver-Burk plot of the enzyme reaction in the presence of 6-hydroxy-L-tryptophan indicated that this compound was a competitive inhibitor. The IC50 values of 6-hydroxy-L-tryptophan was 0.23 mM.

Directed evolution of the tryptophan synthase β-subunit for stand-alone function recapitulates allosteric activation

Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical reactions. Separating the subunits of such complexes, however, often severely attenuates their catalytic activities, because they can no longer be activated by their protein partners. We used directed evolution to explore allosteric regulation as a source of latent catalytic potential using the β-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB). As part of its native αββα complex, TrpB efficiently produces tryptophan and tryptophan analogs; activity drops considerably when it is used as a stand-alone catalyst without the α-subunit. Kinetic, spectroscopic, and X-ray crystallographic data show that this lost activity can be recovered by mutations that reproduce the effects of complexation with the α-subunit. The engineered PfTrpB is a powerful platform for production of Trp analogs and for further directed evolution to expand substrate and reaction scope.