102579-71-5

Basic information

• Product Name: (-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID
• Synonyms: (-)-(1S,4R)-GAMMA-HOMOCYCLOLEU-2-ENE;2-Cyclopentene-1-carboxylicacid,4-amino-,(1R,4R)-rel-(9CI);Trans-4-aMino-2-Cyclopentene-1-carboxylic acid;trans-4-Aminocyclopent-2-enecarboxylic acid
• CAS NO: 102579-71-5
• Molecular Formula: C₆H₉NO₂
• Molecular Weight: 127.14
• Product Categories: AMINOACID;Unusual amino acids
• Mol File: 102579-71-5.mol

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: (-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID(102579-71-5)
• EPA Substance Registry System: (-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID(102579-71-5)

Safety Data

• Statements: 43
• Safety Statements: 36/37
• Hazardous Substances Data: 102579-71-5(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
(-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID is used as a key intermediate in the synthesis of various pharmaceuticals for its unique structure and properties. Its ability to interact with target proteins due to its specific stereochemistry makes it a valuable component in the development of new drugs.
Used in Organic Synthesis:
In the field of organic synthesis, (-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID serves as a versatile building block for creating a range of biologically active compounds. Its cycloalkene and amino functionalities allow for diverse chemical reactions, facilitating the synthesis of complex organic molecules with potential applications in various industries.
Used in Research and Development:
(-)-(1S,4R)-4-AMINOCYCLOPENT-2-ENECARBOXYLIC ACID is utilized as a research molecule to explore its biological activity and binding interactions with target proteins. Its stereochemistry plays a significant role in these studies, providing insights into the development of more effective drugs and understanding the molecular mechanisms of action.

Upstream product

• 49805-27-8 3-tosyl-2-azabicyclo [2.2.1]hepta-2,5-diene 
• 49805-30-3 2-azabicyclo[2.2.1.]hept-5-en-3-one 
• 542-92-7 cyclopenta-1,3-diene 
• 49805-30-3 racemic 2-azabicyclo[2.2.1]hept-5-en-3-one 
• 112531-51-8 (-)-(1S,4R)-4-(acetylamino)-2-cyclopentene-1-carboxylic acid 
• 157810-21-4 (1R,4S)-N-hydroxymethyl-2-azabicyclo<2.2.1>hept-5-en-3-one 
• 79200-56-9 (-)-2-azabicyclo[2.2.1]hept-5-en-3-one 
• 419563-22-7 (1S,4R)-4-aminocyclopent-2-ene-1-carboxylic acid methyl ester tartrate 
• 61865-49-4 ester methylique de l'acide (acetamido-cis-4)-cyclopentene-2-carboxylique 
• 157732-11-1 (1R,4S)-N-acetoxymethyl-2-azabicyclo[2.2.1]hept-5-en-3-one 
• 183074-62-6 N-acetoxymethyl-2-azabicyclo[2.2.1]hept-5-en-3-one 
• 157732-10-0 2-hydroxymethyl-2-azabicyclo<2.2.1>hept-5-en-3-one 
• 130931-83-8 (1S,4R)-2-azabicyclo[2,2,1]hept-5-en-3-one 

Downstream Products

• 130931-83-8 (1S,4R)-2-azabicyclo[2,2,1]hept-5-en-3-one 
• 141352-48-9 (1S,4R)-4-(benzyloxycarbonylamino)-2-cyclopentene-1-methanol 
• 141352-47-8 (1S,4R)-4-(benzyloxycarbonylamino)-2-cyclopentene-1-carboxylic acid methyl ester 
• 151907-78-7 (1S,4R)-4-Benzoylamino-cyclopent-2-enecarboxylic acid methyl ester 
• 194087-01-9 (1S,3R)-3-Benzyloxymethyl-cyclopentylamine 
• 426226-50-8 PMC6 
• 426226-50-8 (1S,3R)-1-(9-adenenyl)-3-(N-hydroxycarbamoyl)cyclopentane 
• 229613-83-6 (–)-methyl (1S,4R)-4-aminocyclopent-2-ene-1-carboxylate hydrochloride 
• 138923-03-2 (1S,4R)-(-)-methyl-4-aminocyclopent-2-en-1-carboxylate hydrochloride 
• 151907-79-8 (1S-cis)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-2-cyclopentene-1-carboxylic acid 
• 19042-34-3 trans-3-aminocyclopentane-1-carboxylic acid 
• 155755-47-8 (+/-)-ethyl (1SR,4RS)-4-acetamido-cyclopent-2-ene carboxylate 
• 61865-49-4 ester methylique de l'acide (acetamido-cis-4)-cyclopentene-2-carboxylique 
• 77745-27-8 (±)-4-aminocyclopent-1-enecarboxylic acid 

Relevant articles and documents

Biocatalytical Transformations. IV. Enantioselective Enzymatic Hydrolyses of Building Blocks for the Synthesis of Carbocyclic Nucleosides

Enantiomerically pure alkyl (1S,4R)- and (1R,4S)-4-acetamido-cyclopent-2-ene-carboxylates are obtained from their corresponding racemates by hydrolysis with PLE or the lipase from Candida cylindracea.

Identification and application of enantiocomplementary lactamases for Vince lactam derivatives

Four enzymes showing hydrolytic activity on derivatives of 2-azabicyclo[2.2.1]hept-5-en-3-one (Vince lactam) were successfully identified through analysis of protein crystal structure and amino acid sequence alignments. Enantiocomplementary activities were observed on Vince lactam and its saturated analog 2-azabicyclo[2.2.1]heptan-3-one with non-heme chloroperoxidase (CPO-T) from Streptomyces aureofaciens, cyclic imide hydrolase (CIH) from Pseudomonas putida, polyamidase (NfpolyA) from Nocardia farcinica, and amidase (AMI) from Rhodococcus globerulus, and perfect kinetic resolution was achieved (E>200). Computational analysis of amide bond resonance stabilization in lactams correlated well with the overall reactivity pattern of the lactams as a function of ring size and strain. The biocatalysts cloned and investigated in this study could be of interest for the synthesis of enantiopure carbocyclic nucleoside analogues.

Development of the Biocatalytic Resolution of 2-azabicyclohept-5-en-3-one as an entry to Single-Enantiomer Carbocyclic Nucleosides

For the resolution of the bicyclic lactam 2-azabicyclohept-5-en-3-one, efficient whole cell biocatalysts have been identified and from these, enzymes (lactamases) have been isolated.While the two enzymes obtained act on different enantiomers of the lactam, either can be used in scaleable processes to obtain synthons for carbocyclic nucleosides having the natural configuration.

Lipase-catalyzed resolution of 2-azabicyclo[2.2.1]hept-5-en-3-ones

The lipase-catalyzed asymmetric resolution of 2-azabicyclo[2.2.1]hept-5-en-3-ones is reported; non-racemic chiral 2-azabicyclo[2.2.1]hept-5-en-3-ones were obtained conveniently by lipase-catalyzed enantioselective transesterification or hydrolysis of N-hydroxymethyl-2-azabicyclo[2.2.1]hept-5-en-3-one or N-acyloxymethyl-2-azabicyclo[2.2.1]hept-5-en-3-one.

Study on immobilization of (+) γ-lactamase using a new type of epoxy graphene oxide carrier

In this article, a new type of graphene oxide material was obtained by modification with epoxy chloropropane, which was used for the (+) γ-lactamase immobilization research. The enzymatic properties of the immobilized (+) γ-lactamase were systematically tested and compared with those of the free enzyme. The free and immobilized enzymes have the same optimum temperature (80 °C) and pH (8.0), the range of pH tolerance increased from pH 8.0-9.0 to pH 4.0-10.0 after immobilization, and the immobilized enzyme is less tolerant to heat than the free enzyme. Kinetic experiments showed that the Km value of the immobilized enzyme was about 2.66 times higher than that of the free enzyme, whereas Vmax decreased 40%. Subsequently, the apparent activation energies (Ea) of the free and immobilized enzymes became 40.03 and 35.62 kJ/mol, respectively. Finally, a reusability assay demonstrated that 70% of the enzyme activity remained after 15 repeated batch experiments.

Inhibition and substrate activity of conformationally rigid vigabatrin analogues with γ-aminobutyric acid aminotransferase

Several cyclopentene GABA analogues were synthesized as conformationally rigid analogues of the epilepsy drug vigabatrin and tested as inhibitors and substrates of γ-aminobutyric acid aminotransferase (GABA-AT). None of these compounds produced time-dependent inhibition. (1R,4S)-(+)-4-Amino-2- cyclopentene-1-carboxylic acid ((+)-3), (4R)-(-)-4-amino-1-cyclopentene-1- carboxylic acid ((-)-4), and d,l-3-amino-1-cyclopentene-1-carboxylic acid (6) are good substrates. The K(m) and k(cat) values for the latter two compounds are very similar to those of GABA, suggesting that they bind in an orientation similar to that of GABA. The K(m) value for (+)-3 is 24 times lower than that for GABA, although its k(cat) value is only one-fourth that for GABA; nonetheless, it is a better substrate for GABA-AT than is GABA. All of these compounds, as well as the enantiomers of 3 and 4 and d,l-trans-4- amino-2-cyclopentene-1-carboxylic acid (5), are competitive inhibitors of GABA-AT. These results demonstrate the effects of the carboxylate group orientation and the stereochemistry of the amino and carboxylate groups on the substrate activity and inhibitor activity, and this should be important to the future design of inhibitors of GABA-AT.

Stereo- and regiocontrolled synthesis of highly functionalized cyclopentanes with multiple chiral centers

The synthesis of some highly substituted three-dimensional cyclopentanes with multiple chiral centers and with high regiochemical and stereochemical diversity has been accomplished starting from cyclopentadiene-derived aminocyclopentenecarboxylic acids. The small-molecular design consisted of stereo- and regiocontrolled functionalization of the starting cyclopentene β- and γ-amino acids through oxirane formation/oxirane opening and afforded regio- and diastereoisomers of orthogonally protected aminocyclopentanecarboxylates.

Enzymatic preparation of optically pure (+)-2-azabicyclo[2.2.1]hept-5-en-3-one by (-)-γ-lactamase from Bradyrhizobium japonicum USDA 6

Whole cells of Bradyrhizobium japonicum USDA 6 showed both (+)-γ-lactamase activity and (-)-γ-lactamase activity. Insight into the genome of B. japonicum USDA 6 revealed two potential γ-lactamases: a type I (+)-γ-lactamase and a (-)-γ-lactamase, making it the first strain to contain two totally different enantioselective lactamases. Both recombinant enzymes could easily be used to prepare either optically pure (+)-γ-lactam ((+)-2-azabicyclo[2.2.1]hept-5-en-3-one) or optically pure (-)-γ-lactam ((-)-2-azabicyclo[2.2.1]hept-5-en-3-one), which are versatile synthetic building blocks for the synthesis of various carbocyclic nucleosides and carbocyclic sugar analogues. Bioinformatic analysis showed that the type I (+)-γ-lactamase belongs to the amidase signature family, with 504 amino acids; the (-)-γ-lactamase, which consists of 274 amino acids, belongs to the hydrolase family. Here, we report that B. japonicum USDA contains a (-)-γ-lactamase in addition to a (+)-γ-lactamase, and it is the (-)-γ-lactamase from this strain that is examined in detail in this Letter. Enzymatic synthesis of optically pure (+)-γ-lactam with nearly 50% isolated yield and >99% ee was achieved.

Chemical preparation method of 2-azabicyclo [2.2.1] hept-5-ene-3-one with optical activity

The invention discloses a chemical preparation method of 2-azabicyclo [2.2.1] hept-5-ene-3-one with optical activity. The chemical preparation method comprises the following steps: racemic 2-azabicyclo [2.2.1] hept-5-ene-3-one which is easily available on the market is used as a raw material and is subjected to chemical resolution to obtain (+/-) 4-aminocyclopent-2-ene-1-carboxylic acid methyl ester with optical activity, (+/-) 4-aminocyclopent-2-ene-1-carboxylic acid is prepared by hydrolysis, and the (+/-) 4-aminocyclopent-2-ene-1-carboxylic acid is subjected to intramolecular condensation to obtain the 2-azabicyclo [2.2.1] hept-5-ene-3-one with optical activity. The method has the advantages that the use of an enzyme fermentation method is avoided, the repeatability is good, and the yield is high.

Method for synthesizing (1R,4S)-1-amino-4-hydroxymethyl-2-cyclopentene hydrochloride

The invention relates to a method for synthesizing (1R,4S)-1-amino-4-hydroxymethyl-2-cyclopentene hydrochloride. According to the method, the reaction conditions are mild, (1S,4R)-(-)-2-azabicyalo[2,2,1]hepta-5-alkene-3-ketone is directly used, (1R,4S)-1-amino-4-hydroxymethyl-2-cyclopentene hydrochloride is obtained through the reactions of hydrolysis and reducing, the yield is high, and the optical purity is high.