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β-cyano-L-alanine

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β-cyano-L-alanine is a reversible inhibitor of the H2S-synthesizing enzyme CSE. It blocks H2S synthesis in rat liver preparations with an IC50 value of 6.5 µM and increases blood pressure in anaesthetized rats induced with hemorrhagic shock by inhibiting endogenous H2S synthesis.

Category

L-Amino Acids

Catalog number

BAT-008142

CAS number

6232-19-5

Molecular Formula

C4H6N2O2

Molecular Weight

114.1

IUPAC Name

(2S)-2-amino-3-cyanopropanoic acid

Synonyms

BCA; beta-cyano-L-alanine; 3-Cyano-L-alanine; L-3-Cyanoalanine

Appearance

White to off-white powder

Purity

≥ 98% (TLC)

Density

1.317 g/cm3

Melting Point

>180°C (dec.)

Boiling Point

368.1°Cat 760 mmHg

Storage

Store at-20 °C

Solubility

Soluble in Water

InChI

InChI=1S/C4H6N2O2/c5-2-1-3(6)4(7)8/h3H,1,6H2,(H,7,8)/t3-/m0/s1

InChI Key

BXRLWGXPSRYJDZ-VKHMYHEASA-N

Canonical SMILES

C(C#N)C(C(=O)O)N

β-cyano-L-alanine, a naturally occurring amino acid, plays pivotal roles in both research and industry. Here are the key applications of β-cyano-L-alanine presented with high perplexity and burstiness:

Biochemical Research: In the realm of biochemical exploration, β-cyano-L-alanine emerges as a versatile player, extensively employed in the probing of enzyme functionality and reaction mechanisms. Serving as both a substrate and an inhibitor in studies focusing on enzymes like cysteine synthase, this compound aids researchers in unraveling the intricacies of enzyme kinetics and uncovering potent enzyme inhibitors, shedding light on the molecular dance within biological systems.

Neurotoxicology: Delving into neurotoxicity, β-cyano-L-alanine takes center stage as a crucial tool in examining neurodegenerative disorders and the impact of neurotoxins on biological landscapes. Its neurotoxic properties render it invaluable for constructing animal models mimicking neurodegenerative conditions such as amyotrophic lateral sclerosis (ALS), offering a window into disease progression and potential therapeutic avenues through the lens of experimental models.

Agricultural Sciences: Within the realm of plant biochemistry, β-cyano-L-alanine entices researchers with its implications in stress responses and nitrogen metabolism. Found naturally in certain plants, this amino acid acts as a shield against herbivores and pathogens, bolstering plant defenses. This insight fuels the development of crop varieties resistant to environmental challenges, enriching the arsenal of strategies for sustainable agriculture.

Pharmaceutical Development: The domain of pharmaceutical advancement finds a beacon in β-cyano-L-alanine, serving as a scaffold for crafting novel drugs and therapeutic agents. Its unique structural framework provides chemists with a canvas to paint diverse derivatives with potential pharmacological activities. These derivatives undergo rigorous evaluation for efficacy and safety in combating a spectrum of diseases, positioning β-cyano-L-alanine as a prized launchpad for drug discovery endeavors.

1. Nitrile-synthesizing enzyme: Screening, purification and characterization

Michihiko Kobayashi, Sakayu Shimizu, Takuto Kumano, Takahisa Suzuki J Gen Appl Microbiol . 2016 Sep 12;62(4):167-73. doi: 10.2323/jgam.2016.02.003.

Cyanide is known as a toxic compound for almost all living organisms. We have searched for cyanide-resistant bacteria from the soil and stock culture collection of our laboratory, and have found the existence of a lot of microorganisms grown on culture media containing 10 mM potassium cyanide. Almost all of these cyanide-resistant bacteria were found to show β-cyano-L-alanine (β-CNAla) synthetic activity. β-CNAla synthase is known to catalyze nitrile synthesis: the formation of β-CNAla from potassium cyanide and O-acetyl-L-serine or L-cysteine. We found that some microorganisms were able to detoxify cyanide using O-methyl-DL-serine, O-phospho-L-serine and β-chloro-DL-alanine. In addition, we purified β-CNAla synthase from Pseudomonas ovalis No. 111 in nine steps, and characterized the purified enzyme. This enzyme has a molecular mass of 60,000 and appears to consist of two identical subunits. The purified enzyme exhibits a maximum activity at pH 8.5-9.0 at an optimal temperature of 40-50°C. The enzyme is specific for O-acetyl-L-serine and β-chloro-DL-alanine. The Km value for O-acetyl-L-serine is 10.0 mM and Vmax value is 3.57 μmol/min/mg.

2. Characterization of nitrilases from Variovorax boronicumulans that functions in insecticide flonicamid degradation and β-cyano-L-alanine detoxification

Nengdang Jiang, Yijun Dai, Kexin Chen, Huoyong Jiang, Jingjing Guo, Li Wang J Appl Microbiol . 2022 Aug;133(2):311-322. doi: 10.1111/jam.15561.

Aims:To characterize the functions of nitrilases of Variovorax boronicumulans CGMCC 4969 and evaluate flonicamid (FLO) degradation and β-cyano-L-alanine (Ala(CN)) detoxification by this bacterium.Methods and results:Variovorax boronicumulans CGMCC 4969 nitrilases (NitA and NitB) were purified, and substrate specificity assay indicated that both of them degraded insecticide FLO to N-(4-trifluoromethylnicotinoyl)glycinamide (TFNG-AM) and 4-(trifluoromethyl)nicotinol glycine (TFNG). Ala(CN), a plant detoxification intermediate, was hydrolysed by NitB. Escherichia coli overexpressing NitA and NitB degraded 41.2 and 93.8% of FLO (0.87 mmol·L-1) within 1 h, with half-lives of 1.30 and 0.25 h, respectively. NitB exhibited the highest nitrilase activity towards FLO. FLO was used as a substrate to compare their enzymatic properties. NitB was more tolerant to acidic conditions and organic solvents than NitA. Conversely, NitA was more tolerant to metal ions than NitB. CGMCC 4969 facilitated FLO degradation in soil and surface water and utilized Ala(CN) as a sole nitrogen source for growth.Conclusions:CGMCC 4969 efficiently degraded FLO mediated by NitA and NitB; NitB was involved in Ala(CN) detoxification.Significance and impact of the study:This study promotes our understanding of versatile functions of nitrilases from CGMCC 4969 that is promising for environmental remediation.

3. Purification, characterization and gene cloning of thermostable O-acetyl-L-serine sulfhydrylase forming beta-cyano-L-alanine

Masako Kuroda, Michihiko Kobayashi, Toru Nagasawa, Toyokazu Yoshida, Hironori Omura, Sakayu Shimizu J Biosci Bioeng . 2003;95(5):470-5.

A thermophilic and cyanide ion-tolerant bacterium, Bacillus stearothermophilus CN3 isolated from a hot spring in Japan, was found to produce thermostable beta-cyano-L-alanine synthase. The enzyme catalyzes the synthesis of beta-cyano-L-alanine from O-acetyl-L-serine and cyanide ions. The purified enzyme has a molecular mass of approximately 70 kDa and consists of two identical subunits. It was stable in the pH range of 6.0 to 10.0 and up to 70 degrees C. The enzyme also catalyzes the synthesis of various beta-substituted-L-alanine derivatives from O-acetyl-L-serine and nucleophilic reagents. The gene encoding the beta-cyano-L-alanine synthase was isolated from B. stearothermophilus CN3. Sequence homology analysis revealed that the beta-cyano-L-alanine synthase of the bacterium is O-acetyl-L-serine sulfhydrylase. A recombinant plasmid, constructed by ligation of the cloned gene and an expression vector, pKK223-3, was introduced into E. coli JM109. The transformed E. coli cells overexpressed beta-cyano-L-alanine synthase. Heat stable beta-cyano-L-alanine synthase can be applied to the synthesis of [4-11C]l-2,4-diaminobutyric acid as a tracer for positron emission tomography.