Ask about this productRelated genes to: NAGK antibody
- 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 antibody
Related articles to: NAGK antibody
- 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 - -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 - Head and neck squamous cell carcinoma (HNSCC) has a poor prognosis and a high fatality rate. To predict the prognosis of HNSCC, this study developed a prognostic model based on nitrogen metabolism (NM)-related genes. - Source: PubMed
Publication date: 2026/01/09
Shen YimingSun WenfangDai Chunfu - Newly harvested wheat kernels undergo a critical after-ripening period that impairs storage stability and limits its utilization, while the key indicators and metabolic pathways underlying quality improvement in wheat grains remain poorly unclear. This study analyzed wheat kernels stored at 25 °C for 120 days using physiological, transcriptomic, and metabolomic approaches. Results showed germination rate, along with activities of catalase, NADPH oxidase, glucose-6-phosphate dehydrogenase and malate dehydrogenase, underwent significant changes during the first 60 days before stabilizing. In contrast, key quality parameters, including glutenin content, gluten index, lactic acid solvent retention capacity, disulfide bonds content and farinograph properties, stabilized after 80 d. Moreover, multi-omics analysis further revealed that the after-ripening process induced significantly alterations in multiple metabolic pathways, especially the 'starch and sucrose metabolism', 'nitrogen metabolism', and 'amino acid metabolism', up-regulated the expression of key genes (TPP, GAD, PAL, PD, ASL, NAGK and AGM) involved in them, as well as increased the levels of trehalose, D-gluconic acid and phenylalanine and decreased the content of sucrose, L-glutamate, and tyrosine, ultimately refine the maturation of wheat grain quality. These changes synergistically enhanced gluten network and starch functionality, providing molecular insight into quality maturation and scientific support for improving wheat storage and processing quality. - Source: PubMed
Publication date: 2025/12/22
Tian QishengWu QiongZhang YurongHuang JianghuiXu SongyueMiao SenZhang Dongdong