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108391-82-8

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108391-82-8 Usage

General Description

6-fluoro-D-tryptophan is a chemical compound that is a derivative of the amino acid tryptophan, with a fluorine atom replacing one of the hydrogen atoms on the 6th position of the indole ring. It is a synthetic analog of tryptophan and has been used in research to study the interactions and functions of tryptophan-containing proteins. The fluorine substitution can alter the properties of the compound, affecting its binding affinity and metabolic pathways. This makes 6-fluoro-D-tryptophan a valuable tool for investigating the role of tryptophan in biological processes and for the development of potential therapeutic applications.

Check Digit Verification of cas no

The CAS Registry Mumber 108391-82-8 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,8,3,9 and 1 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 108391-82:
(8*1)+(7*0)+(6*8)+(5*3)+(4*9)+(3*1)+(2*8)+(1*2)=128
128 % 10 = 8
So 108391-82-8 is a valid CAS Registry Number.

108391-82-8Relevant articles and documents

Complete Stereoinversion of l -Tryptophan by a Fungal Single-Module Nonribosomal Peptide Synthetase

Hai, Yang,Jenner, Matthew,Tang, Yi

, p. 16222 - 16226 (2019)

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. Here, 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.

Regioselective enzymatic halogenation of substituted tryptophan derivatives using the FAD-dependent halogenase RebH

Frese, Marcel,Guzowska, Paulina H.,Voss, Hauke,Sewald, Norbert

, p. 1270 - 1276 (2014)

Regioselective methods to establish carbon-halide bonds are still rare, although halogenation is considered as a commonly used methodology for the functionalization of organic compounds. The incorporation of halogen substituents by organic synthesis usually requires hazardous conditions, shows poor regioselectivity and results in the formation of unwanted byproducts. In addition, halogenation by electrophilic aromatic substitution (SEAr) obeys distinct rules depending on electron-withdrawing or -donating groups already present in the aromatic ring. We employed the tryptophan-7-halogenase RebH for regioselective enzymatic halogenation to overcome these limitations. In combination with a tryptophan synthase, an array of C5- and C6-substituted tryptophan derivatives was synthesized and halogenated by RebH. The halogenase is able override these directing effects and halogenates at the electronically unfavored C7-meta-position, even in presence of ortho/para-directing groups. No business as usual: The tryptophan halogenase RebH from Lechevalieria aerocolonigenes is able to halogenate at the electronically unfavored C7-meta-position of C5-substituted tryptophan derivatives, even in presence of deactivating ortho/para-directing groups.

Deracemization and stereoinversion to aromatic d-amino acid derivatives with ancestral l-amino acid oxidase

Nakano, Shogo,Minamino, Yuki,Hasebe, Fumihito,Ito, Sohei

, p. 10152 - 10158 (2019/10/19)

Enantiomerically pure amino acid derivatives could be foundational compounds for peptide drugs. Deracemization of racemates to l-amino acid derivatives can be achieved through the reaction of evolved d-amino acid oxidase and chemical reductants, whereas deracemization to d-amino acid derivatives has not progressed due to the difficulty associated with the heterologous expression of l-amino acid oxidase (LAAO). In this study, we succeeded in developing an ancestral LAAO (AncLAAO) bearing broad substrate selectivity (13 l-amino acids) and high productivity through an Escherichia coli expression system (50.7 mg/L). AncLAAO can be applied to perform deracemization to d-amino acids in a similar way to deracemization to l-amino acids. In fact, full conversion (>99% ee, d-form) could be achieved for 16 racemates, including nine d,l-Phe derivatives, six d,l-Trp derivatives, and a d,l-phenylglycine. Taken together, we believe that AncLAAO could be a key enzyme to obtain optically pure d-amino acid derivatives in the future.

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