6232-19-5

Basic information

• Product Name: BETA-CYANO-L-ALANINE
• Synonyms: H-ALA(3-CN)-OH;H-ALA(BETA-CN)-OH;H-BETA-CYANO-ALA-OH;H-BETA-CYANO-L-ALA-OH;BETA-CYANO-ALANINE;BETA-CYANO-L-ALANINE;3-CYANO-L-ALANINE;B-cyano-L-alanine
• CAS NO: 6232-19-5
• Molecular Formula: C₄H₆N₂O₂
• Molecular Weight: 114.1
• Product Categories: A - H;Amino Acids;Modified Amino Acids
• Mol File: 6232-19-5.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 368.1 °C at 760 mmHg
• Flash Point: 176.4 °C
• Appearance: /
• Density: 1.317 g/cm³
• Vapor Pressure: 2E-06mmHg at 25°C
• Refractive Index: 1.501
• Storage Temp.: −20°C
• CAS DataBase Reference: BETA-CYANO-L-ALANINE(CAS DataBase Reference)
• NIST Chemistry Reference: BETA-CYANO-L-ALANINE(6232-19-5)
• EPA Substance Registry System: BETA-CYANO-L-ALANINE(6232-19-5)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 6232-19-5(Hazardous Substances Data)

Usage

Description

Hydrogen sulfide (H2S) is a naturally-occurring gasotransmitter with vasodilator and inflammatory modulating activity. H2S is synthesized naturally in a range of mammalian tissues principally by the activity of two enzymes, cystathionine γ lyase (CSE) and cystathionine β synthetase (CBS). β-cyano-L-Alanine (BCA) is a reversible inhibitor of the H2S-synthesizing enzyme CSE. BCA 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. BCA at 50 mg/kg blocked both L-cysteine- and LPS-induced hyperalgesia in rats.

Chemical Properties

White to off-white powder

Uses

β-L-cyanoalanine is an amino acid that promotes seed germination in A. albus seeds. Beta-Cyano-L-alanine in the diet of adult locusts causes a decrease in the hemolymph volume thereby affecting water balance responses. L-β-cyanoalanine is an inhibitor of vitamin B6.

Definition

ChEBI: A cyanoamino acid that is the 3-cyano-derivative of L-alanine.

Biochem/physiol Actions

β-Cyano-L-alanine (BCA) is used as a cystathione γ-lyase (CSE) inhibitor to study the physiological roles of hydrogen sulfide in processes such as angiogenesis and hypertension.

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

Upstream product

• 52-90-4 L-Cysteine 
• 143-33-9 sodium cyanide 
• 120042-14-0 (2S)-2-amino-4-azidobutanoic acid 
• 98541-64-1 (S)-3-(tert-butoxycarbonylamino)-oxetan-2-one 
• 5147-00-2 O-acetyl-L-serine 
• 56-45-1 L-serin 
• 302-72-7 rac-Ala-OH 
• 31883-91-7 (S)-3-Cyano-2-(4-methoxy-benzyloxycarbonylamino)-propionic acid 
• 3309-41-9 N-(benzyloxycarbonyl)-3-cyano-L-alanine 
• 10442-39-4 tetra-n-butylammonium cyanide 
• 112839-94-8 (S)-3-amino-2-oxetanone trifluoroacetic acid salt 
• 52-89-1 l-cysteine hydrochloride 

Downstream Products

• 145385-60-0 (S)-2-[(S)-2-(8-tert-Butoxycarbonylamino-octanoylamino)-3-cyano-propionylamino]-3-phenyl-propionic acid tert-butyl ester 
• 3130-87-8 ASPARAGINE 
• 617-45-8 aspartic Acid 

Relevant articles and documents

Repurposing Nonheme Iron Hydroxylases to Enable Catalytic Nitrile Installation through an Azido Group Assistance

Three mononuclear nonheme iron and 2-oxoglutarate dependent enzymes, l-Ile 4-hydroxylase, l-Leu 5-hydroxylase and polyoxin dihydroxylase, are previously reported to catalyze the hydroxylation of l-isoleucine, l-leucine, and l-α-amino-δ-carbamoylhydroxyvaleric acid (ACV). In this study, we showed that these enzymes can accommodate leucine isomers and catalyze regiospecific hydroxylation. On the basis of these results, as a proof-of-concept, we demonstrated that the outcome of the reaction can be redirected by installation of an assisting group within the substrate. Specifically, instead of canonical hydroxylation, these enzymes can catalyze non-native nitrile group installation when an azido group is introduced. The reaction is likely to proceed through C - H bond activation by an Fe(IV)-oxo species, followed by azido-directed C-N bond formation. These results offer a unique opportunity to investigate and expand the reaction repertoire of Fe/2OG enzymes.

Syntheses of optically pure α-amino acids from 3-amino-2-oxetanone salts

A process for the preparation of optically pure α-amino acids comprising the nucleophilic ring-opening of 3-amino-2-oxetanone salts. N-Protected serine β-lactones are deprotected to form heretofore unknown 3-amino-2-oxetanone and its corresponding salts. In turn these previously unknown 3-amino-2-oxetanone salts may be used in the synthesis of other novel or rare stereochemically-pure free amino acids.

PURIFICATION AND PROPERTIES OF β-CYANO-L-ALANINE SYNTHASE FROM SPINACIA OLERACEA

β-Cyano-L-alanine synthase was purified ca 6200-fold to homogeneity from the leaves of spinach (Spinacia oleracea).The purified enzyme has an apparent Mr of 60 000 and can be dissociated into identical subunits of Mr 30 000.The subunits each contain one molecule of pyridoxal 5'-phosphate.The Km value is 2.3 mM for L-cysteine and 0.73 mM for cyanide. β-Cyano-L-alanine synthase from S. oleracea also catalyses the formation of some S-substituted L-cysteines and some heterocyclic β-substituted alanines from L-cysteine or O-acetyl-L-serine.The specificity of these additional catalytic activities of the purified enzyme are compared with those of cysteine synthase purified from the same plant, and with those of β-cyano-L-alanine synthase purified from other sources.Some other properties, including the amino acid composition of the purified enzyme, are also described. - Key Word Index: Spinacia oleracea; Chenopodiaceae; spinach; β-cyano-L-alanine synthase; cysteine synthase; enzyme purification; amino acid composition; L-cysteine; O-acetyl-L-serine; β-cyano-L-alanine; heterocyclic β-substituted alanines.