51887-89-9

Basic information

• Product Name: 3-CHLORO-L-ALANINE HYDROCHLORIDE
• Synonyms: H-ALA(3-CL)-OH HCL;H-BETA-CHLORO-ALA-OH HCL;(R)-2-AMINO-3-CHLOROPROPIONIC ACID HYDROCHLORIDE;B-CHLORO-L-ALANINE HYDROCHLORIDE;3-Chloro-L-alanineHCl;β-chloro-l-alanine hydrochloride;3-CHLORO-L-ALANINE HYDROCHLORIDE 98+%;H-b-Chloro-Ala-OH·HCl
• CAS NO: 51887-89-9
• Molecular Formula: C₃H₆ClNO₂*ClH
• Molecular Weight: 160
• EINECS: 200-528-9
• Product Categories: Carboxylic Acids (Chiral);Chiral Building Blocks;Synthetic Organic Chemistry;A;AA to ALCertified Reference Materials (CRMs);Alphabetic;Application CRMs;Clinical Chemistry CRM;Alanine aminotransferase;Alanine aminotransferasePeptides for Cell Biology;A to;Enzyme Inhibitors;Enzyme Inhibitors by Enzyme
• Mol File: 51887-89-9.mol

Chemical Properties

• Melting Point: 205 °C (dec.)(lit.)
• Boiling Point: 243.6 °C at 760 mmHg
• Flash Point: 101.1 °C
• Appearance: /
• Density: 1.401 g/cm³
• Vapor Pressure: 0.0105mmHg at 25°C
• Storage Temp.: −20°C
• CAS DataBase Reference: 3-CHLORO-L-ALANINE HYDROCHLORIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 3-CHLORO-L-ALANINE HYDROCHLORIDE(51887-89-9)
• EPA Substance Registry System: 3-CHLORO-L-ALANINE HYDROCHLORIDE(51887-89-9)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36
• WGK Germany: 3
• Hazardous Substances Data: 51887-89-9(Hazardous Substances Data)

Usage

Uses

Used in Enzyme Kinetics Studies:
3-CHLORO-L-ALANINE HYDROCHLORIDE is used as a substrate for screening tyrosine phenol lyase steady state kinetics. This application is crucial in understanding the enzyme's activity and its role in various biochemical processes.
Used in Cellular and Molecular Biology Research:
In the inhibition of serine palmitoyltransferase and cytotoxicity studies in lymphocyte Ly-1 cells, 3-CHLORO-L-ALANINE HYDROCHLORIDE serves as a valuable tool. This application aids in investigating the enzyme's function and its impact on cell viability and function.
Used in Protein Synthesis Systems:
3-CHLORO-L-ALANINE HYDROCHLORIDE is used as an inhibitor of alanine transaminase in wheat germ cell-free protein synthesis systems. This application is essential for studying the regulation of protein synthesis and the role of alanine transaminase in this process.

Biochem/physiol Actions

β-Chloro-L-alanine hydrochloride is an inhibitor of alanine aminotransferase (ALAT). Inhibition of ALAT leads to suppression of tumor progression in lung carcinoma.

InChI:InChI=1/C3H6ClNO2.ClH/c4-1-2(5)3(6)7;/h2H,1,5H2,(H,6,7);1H/t2-;/m0./s1

Upstream product

• 112839-92-6 O-(trifluoroacetyl)-L-serine p-toluenesulfonic acid salt 
• 17136-54-8 Methyl (2R)-2-amino-3-chloropropionate hydrochloride 
• 16428-75-4 D,L-serine hydrochloride 
• 56-45-1 L-serin 

Downstream Products

• 7625-65-2 L-carbobenzyloxy-β-chloroalanine 
• 96099-72-8 (2R)-S-cysteine 
• 96150-12-8 (2S,3R)-3-((R)-2-Amino-2-carboxy-ethylsulfanyl)-2-benzyloxycarbonylamino-butyric acid 
• 212651-52-0 (2R)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-chloropropionic acid 
• 1464-43-3 seleno-L-cystine 
• 56-88-2 L-cystathionine 
• 2731-73-9 2-amino-3-chloropropanoic acid 

Relevant articles and documents

Method for synthesizing L -selenium - methylselenocysteine

The invention provides a method for synthesizing L -selenium - methylselenocysteine, and relates to the reaction of a compound of formula II or a salt thereof with dimethyl diselenoate, and the method comprises MBH. 4 The method comprises the following steps: directly synthesizing L - selenium - methylselenocysteine through a one-pot reaction under the action of alkali or synthesizing L - selenium - methylselenocysteine, and hydrolyzing to obtain L - selenium - methylselenocysteine. The synthesis method has the advantages of simple reaction. The method has the advantages of convenient operation, high product yield, good quality, low cost and suitability for industrialization.

Reactivity of Selenocystine and Tellurocystine: Structure and Antioxidant Activity of the Derivatives

l-Selenocystine (5) and l-tellurocystine (6) have been prepared and the reactivity of these amino acids, i.e., oxidation of 5 and 6, has been performed at various pH values. Hydrogen peroxide was used as an oxidant and it was treated with 5 and 6 in excess in acidic and basic media. Compound 5, upon oxidation, afforded SeIV and SeVI products. Selenocysteic acid [HO3SeCH2CH(NH2)COOH] 9, a novel SeVI compound, was isolated and characterised by single-crystal X-ray diffraction studies. In contrast, l-tellurocystine, upon oxidation with H2O2, afforded TeII and TeIV products. Zwitterionic organotellurolate(IV), [TeCl3CH2CH(NH3)COOH] 13, was isolated and characterised by NMR and IR spectroscopy, mass spectrometry and elemental analysis. Compound 13 crystallizes in an orthorhombic space group. l-Tellurocystine, when reduced with NaBH4, produced the desired tellurolate intermediate, which was trapped with bromoacetic acid. Furthermore, l- and d-tellurocysteine derivatives, [(RTeCH2CH(NH2)COOH) R=phenyl, substituted phenyl and naphthyl (24–39)] were synthesised and evaluated for their glutathione peroxidase (GPx)-like activities. The results show that l-tellurocysteine derivatives have higher activity than their D-tellurocysteine analogues. DFT calculations for l-tellurocysteine derivatives provided information about the bond lengths and bond angles. This study reveals that the introduction of naphthyl substituents (35–38) leads to twisted conformation of the amino acid derivatives.

Preparation method for L-selenocysteine

The invention belongs to the field of chemical synthesis, and concretely relates to a synthetic method for L-selenocysteine. The method comprises the following steps: a, chloridizing L-serine hydrochloride to obtain 3-chloro-L-alanine hydrochloride; b, performing seleno-reaction of 3-chloro-L-alanine hydrochloride prepared by step a under alkaline condition to obtain L-selenocystine; and c, performing reduction reaction of L-selenocystine to obtain L-selenocysteine. The method has simple steps, high yield, low cost, and good application prospect.

Processes for producing β-halogeno-α-amino-carboxylic acids and phenylcysteine derivatives and intermediates thereof

An industrially advantageous method of producing β-halogeno-α-aminocarboxylic acids is provided. Methods are also provided of producing optically active N-protected-S-phenylcysteines having high optical purity and of intermediates thereof, respectively, in which the above production method is utilized. A method of producing β-halogeno-α-aminocarboxylic acids or salts thereof is disclosed which comprises halogenating the hydroxyl group of a β-hydroxy-α-aminocarboxylic acid (in which the basicity of the amino group in α-position is not masked by the presence of a substituent on said amino group) or a salt thereof with an acid with a halogenating agent. A method of producing optically active N-protected-S-phenylcysteines represented by the general formula (3) or salts thereof is further disclosed which comprises applying the above production method to optically active serine or a salt thereof and then carrying out treatment with an amino-protecting agent and reaction with thiophenol under a basic condition.

Direct synthesis of Fmoc-protected amino acids using organozinc chemistry: Application to polymethoxylated phenylalanines and 4-oxoamino acids

The newN-Fmoc 3-iodoalaninetert-butyl ester derived organozinc reagent1, obtained in 7 steps from optically pure 3-serine, was coupled to a range of electrophiles under palladium catalysis to give substituted phenylalanines and 4-oxoamino acids in variabl