Results 1 to 10 of about 5,574 (177)

Comparative Analysis of Mesophilic YqfB-Type Amidohydrolases

Biomolecules, 2022
The widespread superfamily of the human activating signal cointegrator homology (ASCH) domain was identified almost 20 years ago; however, the amount of experimental data regarding the biological function of the domain is scarce.
Roberta Statkevičiūtė, Mikas Sadauskas, Juta Rainytė, Karolina Kavaliauskaitė, Rolandas Meškys   +4 more
doaj   +3 more sources

Genome-Guided Identification of an OTA-Degrading Amidohydrolase AMH2102 from Acinetobacter kookii AK4 with Enhanced Soluble Expression in Escherichia coli [PDF]

Toxins
Ochratoxin A (OTA) is a globally distributed mycotoxin that poses serious threats to food safety and human health due to its nephrotoxic, hepatotoxic, and carcinogenic properties. Previous enzymatic detoxification strategies for OTA have been constrained
Zehui Niu, Shengyue Bai, Yuyun Xiao, Jingran Lai, Yuxin Jin, Zitong Zhao, Yan Yang, Shujuan Cun, Zhihong Liang   +8 more
doaj   +2 more sources

Structural and mechanistic insights into the divergence of pterin deaminase and sepiapterin deaminase [PDF]

Applied Microbiology and Biotechnology
Pterin deaminase and sepiapterin deaminase are key members of the amidohydrolase superfamily and play essential roles in pteridine metabolism across a wide range of biological systems.
Nivetha Shanmuganathan, Sasireka Manikandan, Jerimon Johnson, Sabaridaran Balasubramani, Angayarkanni Jayaraman, Sruthi Paleri, Theertha Ranjith, Thasleema Parveen A   +7 more
doaj   +2 more sources

Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27. [PDF]

Acta Crystallogr F Struct Biol Commun
H. pylori carbon–nitrogen hydrolase was produced and crystallized, and its 2.1 Å resolution structure is reported.Carbon–nitrogen hydrolases (CNHs) are members of the diverse nitrilase superfamily of enzymes that facilitate cellular adaptation to environmental stress by metabolizing nitrogen, detoxifying xenobiotics and catabolizing environmentally ...
Srivastava A, Ayanlade JP, Suleiman L, Udell H, Abendroth J, Lorimer DJ, Edwards TE, Staker BL, Zigweid R, Subramanian S, Myler PJ, Chakafana G, Asojo OA.   +12 more
europepmc   +2 more sources

Safety evaluation of the food enzyme glutaminase from the genetically modified <i>Bacillus subtilis</i> strain Glu3-3. [PDF]

EFSA J
Abstract The food enzyme glutaminase (l‐glutamine amidohydrolase; EC 3.5.1.2) is produced with the genetically modified Bacillus subtilis strain Glu3‐3 by Angel Yeast Co., Ltd. The production strain of the food enzyme contains multiple copies of acquired antimicrobial resistance genes.
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Van Loveren H, Vernis L, Aguilera J, Andryszkiewicz M, Cavanna D, Liu Y.   +16 more
europepmc   +2 more sources

Revisiting D‐Acylases for D‐Amino Acid Production [PDF]

Microbial Biotechnology
N‐Acyl‐D‐amino acid deacylases (EC 3.5.1.81, also known as D‐acylases) have been studied for decades for their utility in the kinetic resolution of N‐acetyl‐D,L‐amino acids (NAAs) due to a marked stereospecificity. In conjunction with an N‐succinyl‐amino
Sergio Martínez‐Rodríguez, Jose Antonio Gavira   +1 more
doaj   +2 more sources

Thermotolerant D-Hydantoinases for Efficient and Stereoselective Intermediate Synthesis of (R)-3-Isobutylglutaric Acid Monoamide, a Key Intermediate in Pregabalin Production. [PDF]

Microb Biotechnol
We engineered thermo‐alkali‐stable D‐hydantoinases via mutagenesis (M63A/F65H/C317T) to resolve Pregabalin's challenging chiral splitting, achieving ee value > 97% for key intermediate (R)‐3‐isobutylglutaric acid monoamide (R‐IBM) synthesis under extreme conditions (pH 10, 70°C–80°C).
Zhang J, Zhi B, Xie Z, Zhang B, Wang N, Wang W.   +5 more
europepmc   +2 more sources

Comparative Genomic and Transcriptomic Analysis Reveals Why Paenarthrobacter Strains Are Specialists in the Degradation of the Fungicide Iprodione. [PDF]

Microb Biotechnol
Paenarthrobacter are specialists in degrading the fungicide iprodione. We showed that this trait has evolved through gene duplication of ipaH and ddaH genes, being in the core genome of paenarthrobacters, and further genetic optimisation, with different strains being at different evolution stages depending on their prior exposure to iprodione ...
Michelioudakis V, Zafranas A, Myrisiotis C, Makri S, Katsoula A, Campos M, Vasileiadis S, Karpouzas DG.   +7 more
europepmc   +2 more sources

The Allosteric Regulation of Β-Ureidopropionase Depends on Fine-Tuned Stability of Active-Site Loops and Subunit Interfaces

Biomolecules, 2023
The activity of β-ureidopropionase, which catalyses the last step in the degradation of uracil, thymine, and analogous antimetabolites, is cooperatively regulated by the substrate and product of the reaction.
Daniela Cederfelt, Dilip Badgujar, Ayan Au Musse, Bernhard Lohkamp, U. Helena Danielson, Doreen Dobritzsch   +5 more
doaj   +1 more source

Identification of a metabolic-related gene signature predicting the overall survival for patients with stomach adenocarcinoma [PDF]

PeerJ, 2021
Background The reprogramming of energy metabolism and consistently altered metabolic genes are new features of cancer, and their prognostic roles remain to be further studied in stomach adenocarcinoma (STAD).
Yuan Nie, Linxiang Liu, Qi Liu, Xuan Zhu
doaj   +2 more sources