NAGK Control Peptide antibody _CP
- Known as:
- NAGK Control Peptide (anti-) _CP
- Catalog number:
- 'AP13658CP-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- NAGK Control Peptide antibody _CP
Related genes to: NAGK Control Peptide antibody _CP
- Gene:
- NAGK NIH gene
- Name:
- N-acetylglucosamine kinase
- Previous symbol:
- -
- Synonyms:
- GNK
- Chromosome:
- 2p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-16
- Date modifiied:
- 2016-04-25
Related products to: NAGK Control Peptide antibody _CP
Related articles to: NAGK Control Peptide antibody _CP
- Arginine is a semi-essential amino acid and holds significant value in the pharmaceutical and nutraceutical industries. Corynebacterium glutamicum is a promising host for arginine production, yet its industrial titers remain limited. Biosensor-based high-throughput screening enables rapid isolation of overproducers. However, the native LysG-based biosensor in C. glutamicum lacks arginine specificity, limiting its efficiency for screening high arginine-producing strains. Here, we developed an arginine-specific biosensor pLysG in C. glutamicum, by combining semi-rational design and directed evolution of LysG, an endogenous regulator responsive to basic amino acids. Structural and interaction analyses revealed that the F222I substitution in LysG retained high affinity for arginine while significantly decreasing its responsiveness to histidine and lysine. Subsequently, this arginine-specific biosensor was successfully applied to screen a library of N-acetylglutamate kinase (NAGK) mutants, identifying 18 novel NAGK mutants with enhanced arginine production compared with previously reported variants. The strain integrated with the optimal NAGK mutant was further subjected to mutagenesis and screening, yielding an engineered strain that achieved an arginine titer of 56.07 g/L in a 5-L bioreactor, a 42% increase relative to the original starting strain. Overall, this study provides a powerful tool for accelerating the metabolic engineering of C. glutamicum for high-level arginine production. - Source: PubMed
Publication date: 2026/05/25
Cai NingyunWang YeRen PengchengRao DemingShi TuoWang ZiyaoShen JieZhou WenjuanQi LinlinWang LixianChen NingChen JiuzhouZheng PingSun Jibin - PII protein is widely acknowledged to regulate intracellular nitrogen and carbon metabolism by interacting with several crucial proteins. N-acetyl-L-glutamate kinase (NAGK), a rate-limiting enzyme for arginine biosynthesis, is regarded as a potential target of PII protein. Nevertheless, the regulatory function remains ambiguous in green algae and has not been investigated in Haematococcus pluvialis. In this study, the NAGK enzyme and PII protein of H. pluvialis (designated as HpNAGK and HpPII, respectively) and their interaction relationships were characterized. The results indicated that HpNAGK showed high similarity with the same enzyme in the green algae. A subcellular localization assay indicated that both HpPII and HpNAGK were located in the chloroplasts. Yeast two-hybrid, pull-down, and bimolecular fluorescence complementation assays distinctly verified the interaction between HpPII and HpNAGK, which occurs in the chloroplasts. The structure of the HpPII-HpNAGK complex was predicted through docking analysis. Moreover, the HpNAGK activity was significantly enhanced by HpPII in the presence of glutamine in vitro. Under nitrogen starvation, HpNAGK activity declined in vivo, concomitant with a reduction in arginine accumulation. The regulatory function of HpPII on HpNAGK activity aligned with that in Chlamydomonas reinhardtii but differed from that in Dunaliella salina, suggesting species specificity among green algae. These findings provide insights into the regulatory function of PII protein in green algae and help to unveil the response mechanisms of H. pluvialis to different nitrogen statuses. - Source: PubMed
Publication date: 2026/04/18
Ma RuijuanChen ZiyueLiu JunjieMeng XingTao XinyiChen YuchengZhang ChunxiaoWang LingLu KangleLi XueshanSong KaiChen JianfengXie Youping - Beta-lactams are among the most successful antibiotics for treating bacterial infections, but its use is impeded by increasing resistance. The contribution of BlrAB and CreBC two-component regulatory systems (TCSs) to β-lactam resistance is reported in spp. and , respectively. , an opportunistic pathogen, is resistant to most β-lactams due to the chromosomally encoded β-lactamases L1 and L2. The role of CreBC TCS in the β-lactam resistance of is still unclear. In this article, we aimed to address this issue. - Source: PubMed
Publication date: 2026/04/16
Yang Tsuey-ChingLu Hsu-FengWu Chao-JungHu En-WeiLu Yu-LiangLi Li-Hua - -acetylglucosamine (GlcNAc) is an amino sugar that serves as a structural component, nutrient source, and signal molecule in bacteria. In this study, we sought to identify the genes involved in GlcNAc utilization in and to evaluate the impact of GlcNAc utilization on antibiotic susceptibility, oxidative stress tolerance, and swimming motility. The roles of the operon, , and in GlcNAc utilization were investigated through mutant construction and growth assays. NagPsm and NagF mediated GlcNAc transport across the inner membrane, while NagK phosphorylated GlcNAc in the cytoplasm. NagA and NagA2 exhibited functional redundancy as -acetylglucosamine-6-phosphate deacetylases, and NagB functioned as a glucosamine-6-phosphate deaminase. The operon was repressed by NagI and derepressed in response to GlcNAc-6P. Antibiotic susceptibility and oxidative stress tolerance were assessed by E-test and menadione IC, respectively. Among the clinical isolates tested, 71.4% (5/7) and 57.1% (4/7) of the strains showed increases in MIC values for colistin and ceftazidime (CAZ) of 1.3 to 2.6 times and 1.3 to 2 times, respectively. Furthermore, GlcNAc utilization enhanced swimming motility but had little effect on oxidative stress tolerance. Overall, the operon, , and contribute to GlcNAc utilization, which in turn can increase resistance to CAZ and colistin and promote swimming motility in some clinical isolates of .IMPORTANCE-acetylglucosamine (GlcNAc) is widely used as a dietary supplement due to its proposed cartilage-protective and anti-inflammatory properties. In bacteria, however, GlcNAc functions as a structural component of peptidoglycan and lipopolysaccharide, as a signal molecule, and as a nutrient source. is a gram-negative opportunistic pathogen associated with nosocomial infections, particularly in cystic fibrosis (CF) patients. The abundance of amino sugars derived from mucin degradation is present in the CF lung. Utilization of GlcNAc can reprogram bacterial metabolism, leading to pleiotropic effects on physiology and stress tolerance. We were therefore interested in how bacteria adapt their physiology and stress tolerance when residing in GlcNAc-rich infection niches. Here, we investigated GlcNAc utilization and its impact on physiology and stress tolerance in . - Source: PubMed
Publication date: 2026/03/16
Liao Chun-HsingLu Hsu-FengWu Shao-ChiHu En-WeiLi Li-HuaLin Yi-TsungYang Tsuey-Ching - N-Acetyl-L-glutamate kinase (NAGK) catalyzes the first committed step in arginine biosynthesis in organisms that perform the cyclic pathway of ornithine synthesis. In cyanobacteria and most Archaeplastida, the activity of NAGK is controlled by the PII signal transduction protein. During evolution, representatives of the class Mamiellophyceae, and lost the gene encoding PII, while retained this gene. Here, we perform coupled enzyme and pull-down assays and show that NAGK is activated by N-acetyl-L-glutamate and inhibited by arginine but is not controlled by PII proteins. This loss may have been compensated for by the enzyme's low sensitivity to arginine. In contrast, PII relieved NAGK from feedback inhibition by arginine. These observations suggest that NAGK possesses a unique feature: it has lost the ability to interact with PII protein. The findings are discussed in the context of the relationship between NAGK control and the PII role in Mamiellophyceae. - Source: PubMed
Publication date: 2026/02/18
Vlasova VitalinaLapina TatianaErmilova Elena