192315-36-9

Basic information

• Product Name: BOC-3-CHLORO-L-TYROSINE
• Synonyms: BOC-3-CHLORO-L-TYR-OH;BOC-3-CHLORO-L-TYROSINE;BOC-L-3-CHLOROTYROSINE;(S)-2-(tert-butoxycarbonylamino)-3-(3-chloro-4-hydroxyphenyl)propanoic acid;Boc-3-chloro-L-Tyr-OH·DCHA;Boc-Tyr(3-Cl)-OH.DCHA;Boc-3-chloro-L-tyrosine dicyclohexylammonium salt;3-Chloro-N-[(1,1-dimethylethoxy)carbonyl]-L-tyrosine
• CAS NO: 192315-36-9
• Molecular Formula: C₁₄H₁₈ClNO₅
• Molecular Weight: 315.75
• Product Categories: Amino Acid Derivatives
• Mol File: 192315-36-9.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: Store at 0-5°C
• CAS DataBase Reference: BOC-3-CHLORO-L-TYROSINE(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-3-CHLORO-L-TYROSINE(192315-36-9)
• EPA Substance Registry System: BOC-3-CHLORO-L-TYROSINE(192315-36-9)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 192315-36-9(Hazardous Substances Data)

Usage

General Description

BOC-3-CHLORO-L-TYROSINE is a chemical compound that belongs to the class of tyrosine derivatives and is commonly used in the field of organic chemistry. It is formed by the addition of a BOC (tert-butyloxycarbonyl) protecting group to the amino group of L-tyrosine and a chlorine atom attached to the benzene ring. BOC-3-CHLORO-L-TYROSINE is often utilized as a building block in the synthesis of various pharmaceuticals, agrochemicals, and other fine chemicals due to its unique properties and reactivity. BOC-3-CHLORO-L-TYROSINE plays a crucial role in the development of novel drug candidates and in the advancement of chemical research.

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 7423-93-0 (S)-2-amino-3-(3-chloro-4-hydroxyphenyl)propanoic acid 

Downstream Products

• 1609638-43-8 (S)-2-((tert-butoxycarbonyl)amino)-3-(4-((tert-butyldiphenylsilyl)oxy)-3-chlorophenyl)propanoic acid 
• 1447710-51-1 (S)-3-(4-(allyloxy)-3-chlorophenyl)-2-(tert-butoxycarbonylamino)propanoic acid 

Relevant articles and documents

Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site

Hydrogen bonds are ubiquitous in enzyme active sites, providing binding interactions and stabilizing charge rearrangements on substrate groups over the course of a reaction. But understanding the origin and magnitude of their catalytic contributions relative to hydrogen bonds made in aqueous solution remains difficult, in part because of complexities encountered in energetic interpretation of traditional site-directed mutagenesis experiments. It has been proposed for ketosteroid isomerase and other enzymes that active site hydrogen bonding groups provide energetic stabilization via "short, strong" or "low-barrier" hydrogen bonds that are formed due to matching of their pKa or proton affinity to that of the transition state. It has also been proposed that the ketosteroid isomerase and other enzyme active sites provide electrostatic environments that result in larger energetic responses (i.e., greater "sensitivity") to ground-state to transition-state charge rearrangement, relative to aqueous solution, thereby providing catalysis relative to the corresponding reaction in water. To test these models, we substituted tyrosine with fluorotyrosines (F-Tyr's) in the ketosteroid isomerase (KSI) oxyanion hole to systematically vary the proton affinity of an active site hydrogen bond donor while minimizing steric or structural effects. We found that a 40-fold increase in intrinsic F-Tyr acidity caused no significant change in activity for reactions with three different substrates. F-Tyr substitution did not change the solvent or primary kinetic isotope effect for proton abstraction, consistent with no change in mechanism arising from these substitutions. The observed shallow dependence of activity on the pKa of the substituted Tyr residues suggests that the KSI oxyanion hole does not provide catalysis by forming an energetically exceptional pKa-matched hydrogen bond. In addition, the shallow dependence provides no indication of an active site electrostatic environment that greatly enhances the energetic response to charge accumulation, consistent with prior experimental results.