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β-Chloro-L-alanine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

β-Chloro-L-alanine is an inhibitor of L-alanine aminotransferase (ALAT) and thus inhibits L-alanine production and impairs D-glucose uptake of LLC1 Lewis lung carcinoma cells.

Category

Inhibitors containing Unusual Amino Acids

Catalog number

BAT-007773

CAS number

2731-73-9

Molecular Formula

C3H6NO2Cl

Molecular Weight

123.54

IUPAC Name

(2R)-2-amino-3-chloropropanoic acid

Synonyms

β-Chloro-L-Ala-OH; 3-Chloro-L-alanine; (R)-2-Amino-3-chloropropanoic acid; Alanine, 3-chloro-; beta-Chloro-L-alanine; beta-Chloroalanine; 3-Chloro-DL-alanine; beta-Chloro-DL-alanine; H-Ala(Cl)-OH

Appearance

White solid

Purity

≥ 95% (HPLC)

Density

1.401 g/cm3

Melting Point

156 °C

Boiling Point

243.6 °C at 760 mmHg

Storage

Store at 2-8 °C

InChI

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

InChI Key

ASBJGPTTYPEMLP-REOHCLBHSA-N

Canonical SMILES

C(C(C(=O)O)N)Cl

β-Chloro-L-alanine, a synthetic amino acid with diverse applications, plays a crucial role in various research and industrial settings. Here are the key applications of β-Chloro-L-alanine, presented with high perplexity and burstiness:

Enzyme Inhibition Studies: As a potent irreversible inhibitor of pyridoxal phosphate-dependent enzymes like cysteine desulfhydrase and alanine racemase, β-Chloro-L-alanine binds covalently to active sites, offering invaluable insights into enzyme function and regulation. Understanding these intricate interactions is fundamental for the development of enzyme-targeted drugs and agricultural pesticides, shaping the landscape of biochemical research.

Neurochemistry Research: In neurochemistry, β-Chloro-L-alanine serves as a powerful tool for investigating the complex role of amino acids in neurotransmission. By disrupting normal amino acid metabolism, researchers can explore the effects on neurotransmitter levels and neuronal activity, shedding light on the pathophysiology of neurodegenerative conditions and psychiatric ailments in a nuanced and multifaceted manner.

Microbial Metabolism: Within the realm of microbial metabolism, β-Chloro-L-alanine acts as a key player in probing amino acid utilization in microorganisms. By selectively inhibiting metabolic enzymes, researchers unravel the intricate pathways utilized by diverse microbial species, offering valuable insights for industrial microbiology applications such as antibiotic synthesis and fermentation technology in a complex and dynamic ecosystem.

Chemical Synthesis: Serving as a pivotal building block in the synthesis of various chemical compounds, including pharmaceuticals and agrochemicals, β-Chloro-L-alanine's unique structural features enable the formation of complex molecules through a diverse array of chemical reactions. This versatility positions it as a prized intermediate in organic synthesis and drug development, playing a crucial role in advancing the frontiers of chemical innovation and scientific exploration.

1. 3-Chloro-D-alanine chloride-lyase (deaminating) of Pseudomonas putida CR 1.1. Purification and characterization of a novel enzyme occurring in 3-chloro-D-alanine-resistant pseudomonads

H Hosono, Y Tani, H Yamano, H Yamada, B Kawakami, T Nagasawa, H Ohkishi J Biol Chem . 1982 Nov 25;257(22):13749-56.

A novel enzyme catalyzing cleavage of 3-chloro-D-alanine to pyruvate, ammonia, and chloride ion is distributed in some pseudomonads which have a resistance to high concentrations of 3-chloro-D-alanine. Pseudomonas putida CR 1-1 (AKU 867) was found to have the highest activity of enzyme, which was inducibly formed by the addition of 3-chloro-D-alanine to the medium. The enzyme, tentatively called 3-chloro-D-alanine chloride-lyase, was purified from P.l putida CR 1-1 in seven steps. After the last step, the enzyme appeared to be homogeneous by the criteria of polyacrylamide gel electrophoresis, analytical ultracentrifuge, and double diffusion in agarose. The enzyme has a molecular weight of about 76,000 and consists of two subunits identical in molecular weight (approximately 38,000). The enzyme exhibits absorption maxima at 278 nm and 418 nm, which are independent of the pH (6.0-9.0), and contains 2 mol of pyridoxal 5'-phosphate/mol of the enzyme. The holoenzyme is resolved to the apoenzyme by incubation with phenylhydrazine and reconstituted by the addition of pyridoxal-P. The apoenzyme can be crystallized by adding ammonium sulfate. 3-Chloro-D-alanine chloride-lyase catalyzes an alpha, beta-elimination reaction of 3-chloro-D-alanine and also, but to a lesser extent, D-cysteine and D-cysteine. The enzyme also catalyzes a beta-replacement reaction of chlorine of 3-chloro-D-alanine with hydrosulfide to yield D-cysteine. The important role of this novel beta-lyase enzyme in the detoxication of e-chloro-D-alanine by P. putida CR 1-1 is also discussed.

2. The effect of beta-chloro D-alanine and L-cycloserine on the serine, phosphorus and palmitic acid uptake and metabolism of Tetrahymena lipids

P Kovács Acta Biol Hung . 1999;50(4):363-73.

The serine palmitoyltransferase inhibitors beta-chloro-D-alanine and L-cycloserine resulted in the uptake and metabolism of 3H-serine, 3H-palmitic acid and 32P significant alterations in the unicellular Tetrahymena pyriformis GL as compared to the untreated cells. In contrast with the higher eukariotic cells, by these treatments - except 5 mM L-cycloserine - the ceramide formation were not inhibited in Tetrahymena. L-cycloserine inhibited the conversion of phosphatidylserine (PS) to phosphatidyl-ethanolamine (PE) by decarboxylation, and the conversion of PE to phosphatidylcoline (PC) by methylation. The shorter L-cycloserine treatments caused lower, and the longer treatments higher label in glycerophospholipids. beta-chloro-D-alanine resulted in the glycerophospholids higher lipid precursor incorporation both in the shorter and longer treatments. Presumably beta-chloro-D-alanine treatments inhibit the transaminase activity, and the higher concentration (5 and 10 mM) proved to be toxic for Tetrahymena. We found differences between the metabolism of serine and palmitic acid labeled lipids in the beta-chloro-D-alanine and L-cycloserine treated groups. This phenomenon is probably due to a difference in the uptake of phospholipid head group component serine and hydrophobic tail precursor palmitic acid: the incorporation of palmitic acid in Tetrahymena is extremely quick, on the other hand, the uptake of serine is slower, a clear time dependence was measured.

3. 3-Chloro-DL-alanine resistance by L-methionine-alpha-deamino-gamma-mercaptomethane-lyase activity

Yoshio Nakano, Mamiko Yoshimura, Toshihiko Koga, Haruka Fukamachi FEBS Lett . 2002 Jul 17;523(1-3):119-22. doi: 10.1016/s0014-5793(02)02958-7.

The antibacterial agent 3-chloro-DL-alanine (3CA) is an inhibitor of peptidoglycan synthesis. Fusobacterium nucleatum and Porphyromonas gingivalis, the bacteria responsible for oral malodor, are shown to be resistant to 1 mM 3CA, whereas Streptococcus mutans and Escherichia coli are sensitive to this antibacterial agent at the same concentration. We isolated the 3CA resistance gene from F. nucleatum and showed that the gene encodes an L-methionine-alpha-deamino-gamma-mercaptomethane-lyase that catalyzes the alpha,gamma-elimination of L-methionine to produce methyl mercaptan. The enzyme also exhibits 3CA chloride-lyase (deaminating) activity. This antibacterial agent is expected to be useful for specific selection of malodorous oral bacteria producing high amounts of methyl mercaptan.