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β-(2-Thiazolyl)-DL-alanine

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

Category

DL-Amino Acids

Catalog number

BAT-005807

CAS number

1596-65-2

Molecular Formula

C6H8N2O2S

Molecular Weight

172.21

IUPAC Name

2-amino-3-(1,3-thiazol-2-yl)propanoic acid

Synonyms

DL-Ala(2-thiazolyl)-OH; (+/-)-2-Amino-3-(2-thiazolyl)propionic acid; 2-Thiazolepropanoic acid, α-amino-, (±)-; 2-Thiazolepropionic acid, α-amino-, DL-; α-Amino-2-thiazolepropanoic acid; (±)-2-Amino-3-(2-thiazolyl)propionic acid; 2-Amino-3-(thiazol-2-yl)propanoic acid; 2-Thiazole-DL-alanine; 2-Thiazolealanine; 2-Thiazolyl-DL-alanine; H-DL-Ala(thiazol-2-yl)(thiazol-2-yl)-OH; H-β-(2-Thiazolyl)-Ala-OH

Related CAS

1007-43-8 (Deleted CAS)

Appearance

Yellowish powder

Purity

≥95%

Density

1.433±0.06 g/cm3

Melting Point

197-198°C (dec.)

Boiling Point

339.9±37.0°C at 760 mmHg

Storage

Store at 2-8°C

InChI

InChI=1S/C6H8N2O2S/c7-4(6(9)10)3-5-8-1-2-11-5/h1-2,4H,3,7H2,(H,9,10)

InChI Key

PXFXXRSFSGRBRT-UHFFFAOYSA-N

Canonical SMILES

C1=CSC(=N1)CC(C(=O)O)N

β-(2-Thiazolyl)-DL-alanine, a compound with versatile applications in diverse research and clinical settings, plays a pivotal role in various domains. Here are the key applications, each presented with high perplexity and burstiness:

Antibiotic Research: Serving as a crucial precursor in the synthesis of broad-spectrum antibiotics such as thiamphenicol and florfenicol, β-(2-Thiazolyl)-DL-alanine occupies a significant position in combating bacterial infections in both human and veterinary medicine. Delving into the intricate mechanisms of this compound aids in the development of novel antibiotics with heightened efficacy and decreased resistance levels, reshaping the landscape of antimicrobial therapy.

Enzyme Inhibition Studies: In the realm of biochemical research, β-(2-Thiazolyl)-DL-alanine emerges as a cornerstone for unraveling the complexities of enzyme inhibition pathways, particularly those associated with bacterial cell wall synthesis. By deciphering the specific enzyme inhibitory actions of this compound, researchers pave the way for designing potent inhibitors tailored for therapeutic applications. This pursuit holds the promise of groundbreaking antimicrobial drug discoveries targeting resilient bacterial strains, marking a new era in combating drug-resistant infections.

Nutritional Biochemistry: Within the domain of nutritional studies, β-(2-Thiazolyl)-DL-alanine serves as a valuable tool for investigating amino acid metabolism and its profound impact on various physiological processes. Researchers delve deep into understanding how this compound modulates growth and development in model organisms, shedding light on the intricate web of amino acid requirements and their implications on overall health and disease outcomes. This holistic approach contributes significantly to advancing our comprehension of the intricate interplay between amino acids and physiological well-being.

Chemical Synthesis: Embracing an essential role in chemical synthesis, β-(2-Thiazolyl)-DL-alanine emerges as a building block for crafting complex organic molecules with diverse functionalities. Its unique composition, incorporating the thiazole and alanine moieties, renders it as a valuable starting material for synthesizing a myriad of bioactive compounds. This versatile application streamlines the process of discovering and developing novel therapeutic agents and functional materials, ushering in a realm of innovation and advancement in the field of chemical synthesis.

1. Cloning of the ATP phosphoribosyl transferase gene of Corynebacterium glutamicum and application of the gene to L-histidine production

T Mizukami, A Hamu, M Ikeda, T Oka, R Katsumata Biosci Biotechnol Biochem. 1994 Apr;58(4):635-8. doi: 10.1271/bbb.58.635.

Corynebacterium glutamicum mutants lacking ATP phosphoribosyl transferase (PRT) were selected by complementation with the Escherichia coli PRT gene. The recombinant plasmid pCH13 carrying a wild type PRT gene from C. glutamicum T106 was obtained in one of the mutants, LH13. Transformants, LH13/pCH13 and T106/pCH13, had three times higher PRT specific activity than T106. The plasmid pCH99 specifying the PRT, which was desensitized to feedback inhibition by L-histidine fifty-fold higher than the wild type PRT, was derived from pCH13. L-Histidine productivity of C. glutamicum F81, was markedly decreased by pCH13, but increased twice by pCH99. In cultivation in jar fermentors, F81/pCH99 continued to accumulate L-histidine through fermentation and yielded to the titer of 22/5 g/liter, while F81 accumulated only 11.5 g/liter due to production retardation halfway through fermentation. Moreover, F81/pCH99 had a larger production rate than F81 even in its production phase. These results indicate that the yield improvement results from amplification of the highly desensitized PRT provided by pCH99.

2. Genetic and biochemical characterization of Corynebacterium glutamicum ATP phosphoribosyltransferase and its three mutants resistant to feedback inhibition by histidine

Yun Zhang, Xiuling Shang, Aihua Deng, Xin Chai, Shujuan Lai, Guoqiang Zhang, Tingyi Wen Biochimie. 2012 Mar;94(3):829-38. doi: 10.1016/j.biochi.2011.11.015. Epub 2011 Dec 8.

ATP phosphoribosyltransferase (ATP-PRT) catalyzes the condensation of ATP and PRPP at the first step of histidine biosynthesis and is regulated by a feedback inhibition from product histidine. Here, we report the genetic and biochemical characterization of such an enzyme, HisG(Cg), from Corynebacterium glutamicum, including site-directed mutagenesis of the histidine-binding site for the first time. Gene disruption and complementation experiments showed that HisG(Cg) is essential for histidine biosynthesis. HisG(Cg) activity was noncompetitively inhibited by histidine and the α-amino group of histidine were found to play an important role for its binding to HisG(Cg). Homology-based modeling predicted that four residues (N215, L231, T235 and A270) in the C-terminal domain of HisG(Cg) may affect the histidine inhibition. Mutating these residues in HisG(Cg) did not cause significant change in the specific activities of the enzyme but resulted in the generation of mutant ones resistant to histidine inhibition. Our data identified that the mutant N215K/L231F/T235A resists to histidine inhibition the most with 37-fold increase in K(i) value. As expected, overexpressing a hisG(Cg) gene containing N215K/L231F/T235A mutations in vivo promoted histidine accumulation to a final concentration of 0.15 ± 0.01 mM. Our results demonstrated that the polarity change of electrostatic potential of mutant protein surface prevents histidine from binding to the C-terminal domain of HisG(Cg), resulting in the release of allosteric inhibition. Considering that these residues were highly conserved in ATP-PRTs from different genera of Gram-positive bacteria the mechanism by histidine inhibition as exhibited in Corynebacterium glutamicum probably represents a ubiquitously inhibitory mechanism of ATP-PRTs by histidine.

3. Modification of histidine biosynthesis pathway genes and the impact on production of L-histidine in Corynebacterium glutamicum

Yongsong Cheng, Yunjiao Zhou, Lei Yang, Chenglin Zhang, Qingyang Xu, Xixian Xie, Ning Chen Biotechnol Lett. 2013 May;35(5):735-41. doi: 10.1007/s10529-013-1138-1. Epub 2013 Jan 26.

Histidine biosynthesis in Corynebacterium glutamicum is regulated not only by feedback inhibition by the first enzyme in the pathway, but also by repression control of the synthesis of the histidine enzymes. C. glutamicum histidine genes are located and transcribed in two unlinked loci, hisEG and hisDCB-orf1-orf2-hisHA-impA-hisFI. We constructed plasmid pK18hisDPtac to replace the native hisD promoter with the tac promoter, and overexpressed phosphoribosyl-ATP-pyrophosphohydrolase, encoded by hisE, and ATP-phosphoribosyltransferase, encoded by hisG. The L-histidine titer at 0.85 g l(-1) was 80 % greater in the transformed bacterium and production of byproducts, L-alanine and L-tryptophan, was significantly decreased. However, accumulation of glutamic acid increased by 58 % (2.8 g l(-1)). This study represents the first attempt to substitute the histidine biosynthesis pathway promoter in the chromosome with a stronger promoter to increase histidine production.