Ask about this productRelated genes to: NIT1 antibody
- Gene:
- NIT1 NIH gene
- Name:
- nitrilase 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 1q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-04-27
- Date modifiied:
- 2016-10-05
Related products to: NIT1 antibody
Related articles to: NIT1 antibody
- Lipotoxicity caused β-cell mass decrease and impaired β-cell function in type 2 diabetes mellitus (T2DM). We previously reported that caveolin-1 (Cav-1) deficiency protected pancreatic β cells against palmitate (PA)-induced apoptosis and dysfunction in both NIT-1 cells and isolated islets. In this study, we firstly established inducible β-cell-specific Cav-1 knockout (iβ-Cav1 KO) mice model. Next, we investigated whether Cav-1 depletion in vitro or in vivo affected β-cell function and survival through the regulation of autophagy under lipotoxicity. Our results showed that Cav-1 depletion exhibited increased islets size, improved insulin resistance and glucose tolerance in lipid stressing conditions. In addition, knockout of Cav-1 also increased β-cell viability through suppression of gene expression of proapopototic molecules (BIM, BID, SMAC, Apaf, Caspase9, Caspase3, AIF and Endo G). Mechanism studies revealed that Cav-1 depletion protected β cells from PA-induced apoptosis through p38 MAPK signaling pathway. Meanwhile, we also found that Cav-1 depletion enhanced autophagy through elevated expression of Beclin-1 and Lc3b, and increased degradation of p62 protein. Further investigation indicated that mTOR signaling pathway was participated in the regulation of PA-induced autophagy. Taking together, our data suggested that Cav-1 depletion ameliorated PA-induced glucose metabolism abnormality, increased cell viability, and improved β-cell apoptosis through the enhancement of autophagy. Our findings would provide valuable clues for developing novel treatments based on Cav-1 inhibition against diabetes under lipotoxicity. - Source: PubMed
Publication date: 2026/04/22
Zeng WenCai NanLiu JiaLiu KunyingLin ShuoYang XubinZeng Longyi - The reaction mechanism of nitrilase () toward the aliphatic dinitrile substrate pentanedinitrile (PD) was elucidated using quantum mechanical dynamics (QMD) simulations containing a cluster model having the catalytic triad (C164, K130, and E38). The elucidated reaction mechanism pathway revealed a sequential conversion of PD to 4-cyanobutanoic acid (CA) and pentanedioic acid (PA), involving two hydrolytic (2HO) steps mediated by the catalytic triad. Key intermediates and transition states were identified, highlighting water-mediated proton-transfer relays, thioimidate formation, and acyl-enzyme formation. The comparative analysis with the aromatic substrate benzonitrile (BN) showed a conserved reaction mechanism pathway but lower activation energy barriers for aliphatic substrates (PD and CA), highlighting a reduced π-electron delocalization and steric effects in aliphatic substrates. The identified rate-limiting step corresponded to the nucleophilic attack step () for PD and the ammonia release step () for CA, with relative energies of 14.2 kcal mol and 14.3 kcal mol, respectively. The elucidated reaction mechanism advances the insight and mechanistic understanding of nitrilase biocatalysis, substrate preferences, and rational understanding of the engineering of for industrial biocatalysis. - Source: PubMed
Publication date: 2026/04/01
Kumar AbhishekGunaseelan Gladstone SigamaniLalitha RoopaTingirikari Jagan Mohan RaoKumar Ramalingam Pravin - L., a salt-sensitive horticultural crop, is severely affected by soil salinity, which disrupts photosynthetic efficiency and metabolic homeostasis. This study quantified the effects of Plant Growth-Promoting Rhizobacteria (PGPR)-, , , and -on key enzymatic indicators of cucumber seedlings exposed to 0, 50, 100, and 150 mM NaCl. PGPR inoculation significantly enhanced bacterial stress-mitigation and hormonal pathways, with ACC-deaminase activity increasing by up to 78.8% (, 150 mM NaCl) and nitrilase activity by 50.5% (, 50 mM NaCl). Auxin-related pathways were strongly induced, as reflected by increases of up to 51.1% in the IAM pathway () and 42.9% in the IPA pathway (). In plant tissues, key metabolic enzymes exhibited high stability under salinity, with ProDH and NDPK activities increasing by up to 4.5% and 2.35%, respectively, while RuBisCO activity remained unaffected across treatments. These results demonstrate that PGPR function as effective bioestimulants by coordinating hormonal regulation and metabolic resilience, providing a sustainable biotechnological strategy to enhance cucumber tolerance to salinity stress. - Source: PubMed
Publication date: 2026/02/03
Pérez-García Laura-AndreaSáenz-Mata JorgeFortis-Hernandez ManuelPreciado-Rangel Pablo - Cyanide is widely used in industries due to its affinity for metals, a property that also underlies its toxicity. Industries, therefore, must reduce cyanide concentration before the final disposal of wastewater. Physical, chemical, and biological methods have been developed for this; however, knowledge about the structure of enzymes involved in cyanide degradation remains limited. Structural characterization of these proteins could facilitate the development of enzymes with enhanced bioremediation potential. Here, we present the single-particle cryo-electron microscopy structures of a cyanide dihydratase from Bacillus safensis and a cyanide hydratase from Gloeocercospora sorghi at 2.2 Å and 2.0 Å resolution, respectively. We provide a comprehensive description and comparative analysis alongside all previously determined nitrilase structures. Importantly, our full-length structures reveal new features in the C-terminal as well as specific intermolecular interactions between protomer interfaces and within the helix lumen. Finally, our findings offer insights into the reaction mechanisms of these two enzymes. - Source: PubMed
Publication date: 2026/02/17
Justo Arevalo SantiagoValle-Riestra Felice ValeriaBarahona Acuña MikaelaOrdinola Flores KatiaQuiñones Aguilar MauroBalan AndreaFarah Chuck Shaker - - Source: PubMed
Publication date: 2026/02/18
Zang TabeaHaack Tobias BSchlotterbek MichaelZeltner LenaSchöls LudgerHengel Holger