Review
Biochemistry & Molecular Biology
Jiahui Fu, Jihui Gao, Zhongxin Liang, Dong Yang
Summary: Disulfide bonds are crucial for maintaining protein structures and biological functions, with PDIs playing a key role in regulating their formation.
Review
Biochemistry & Molecular Biology
Sabrina L. Slater, Despoina A. I. Mavridou
Summary: Protein folding is crucial for biological function and recombinant protein production, and the correct formation of disulfide bonds is essential for protein stability. In bacterial expression systems, the limitations of endogenous posttranslational modification systems can hinder the production of proteins with their native folds.
MOLECULAR MICROBIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Lisa R. Knoke, Jannik Zimmermann, Natalie Lupilov, Jannis F. Schneider, Beyzanur Celebi, Bruce Morgan, Lars I. Leichert
Summary: The thiol redox balance in the periplasm of E. coli was examined using genetically encoded redox probes (roGFP2 and roGFP-iL). The presence of an alternative system for the introduction of disulfide bonds and the role of glutathione in the oxidative folding machinery were explored.
Article
Food Science & Technology
Akiko Isomoto, Eiichi Shoguchi, Kanako Hisata, Jun Inoue, Yinrui Sun, Kenji Inaba, Noriyuki Satoh, Tomohisa Ogawa, Hiroki Shibata
Summary: This study identified genes involved in the modification and functioning of venom proteins in Protobothrops flavoviridis, a venomous snake species. Genes encoding protein disulfide isomerase (PDI) family members, Selenoprotein M (SELENOM), and Calreticulin (CALR) were highly expressed in venom glands, suggesting their potential role in protein folding and modification.
Article
Chemistry, Inorganic & Nuclear
Li-Juan Sun, Huamin Wang, Jia-Kun Xu, Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin
Summary: This study presents the design and construction of a double mutant human neuroglobin (Ngb) that can efficiently catalyze carbene N-H insertions for aromatic amine and o-phenylenediamine derivatives, leading to high yields and total turnover numbers. It also demonstrates the first example of quinoxalinone formation catalyzed by an engineered heme enzyme.
INORGANIC CHEMISTRY
(2023)
Article
Biochemistry & Molecular Biology
Shiyi Wang, Yiwen Zhao, Shufen Mao, Jiang Zhu, Yangyang Zhan, Dongbo Cai, Xin Ma, Dong Wang, Shouwen Chen
Summary: Disulfide bonds in proteins significantly affect folding efficiency by limiting conformational space. Inefficient formation of disulfide bonds is the main factor limiting enzyme activity and stability. This study aimed to increase the activity of disulfide-bond-containing proteins by promoting disulfide bond formation in Bacillus licheniformis. By introducing glutamate decarboxylase GAD from Escherichia coli into B. licheniformis, and successively overexpressing disulfide isomerase and oxidoreductase from different sources, the catalytic efficiency of GAD was improved. The engineered B. licheniformis showed significantly increased GAD activity (from 10.4 U/mg to 80.0 U/mg) and demonstrated adaptability for other disulfide-bond-containing proteins, such as UDP-glucosyltransferase from Arabidopsis thaliana. This work demonstrates the importance of disulfide bond formation for protein activity in B. licheniformis and provides a promising platform for expressing disulfide-bond-containing proteins.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Food Science & Technology
Tomohiro Noguchi
Summary: Wheat flour and water form gluten with the formation of disulfide bonds being crucial, with protein disulfide isomerase (PDI) playing a key role in the process. Vitamin C as a dough improver enhances dough quality through its cooperation with PDI.
JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY-NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI
(2021)
Article
Virology
Huanyu Zhang, Wenhua Kuang, Congcong Fu, Jiang Li, Manli Wang, Zhihong Hu
Summary: The study identified that the baculovirus core gene ac81 likely encodes a disulfide isomerase which plays a crucial role in various functions of the baculovirus life cycle. This suggests that viral disulfide bond formation could be an ancient mechanism shared by insect-specific large DNA viruses like baculoviruses, nudiviruses, and hytrosaviruses encoding AC81 and P33 (sulfhydryl oxidase).
JOURNAL OF VIROLOGY
(2022)
Article
Biochemistry & Molecular Biology
Jinxin Hu, Mei Yu, Yanan Chang, Huali Tang, Wanxin Wang, Lipu Du, Ke Wang, Yueming Yan, Xingguo Ye
Summary: In this study, wheat protein disulfide isomerase (PDI) was found to play a crucial role in wheat flour-processing quality. Mutants lacking TaPDI genes exhibited reduced grain size, increased accumulation of protein bodies, and altered rheological properties of dough.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Chemistry, Multidisciplinary
Chaemyeong Lee, Yeil Kim, Minji Kim, Hyeri Yoo, Eunji Sim, Sang-Yup Lee
Summary: In this study, we investigate the substantial alteration of molecular self-assembly suprastructure by the covalent bonds linking individual building block molecules. The role of covalent bonding within self-assembled structures of cysteinyl bolaamphiphile is focused on, and the contribution of disulfide bonds in facilitating the bending of nanobelt assembly and the formation of longer assembled structures is revealed. Molecular dynamics simulation confirms the anisotropic distribution of disulfide bonds causing the bending of nanobelt assembly.
JOURNAL OF INDUSTRIAL AND ENGINEERING CHEMISTRY
(2023)
Article
Environmental Sciences
Han Zhang, Lei Wang, Yinbin Qiu, Fahui Gong, Baoting Nong, Xinghua Pan
Summary: This study identified a large number of previously unknown conopeptide precursors in Conus caracteristicus and revealed the high diversity of conotoxins secreted by both VD and VB of this species. Additionally, a PDI gene with five thioredoxin domains shared among multiple Conus species was discovered. These findings provide novel insights for further research on the molecular evolution and function of novel conotoxins.
FRONTIERS IN MARINE SCIENCE
(2022)
Article
Chemistry, Applied
Yaoyao Lian, Ya Li, Ruyan Lv, Lifeng Wang, Wenfei Xiong
Summary: This study found that alkali concentration has a significant impact on the gel formation of rice protein, with higher concentration leading to faster gel formation. Heating can accelerate the gel formation rate, but prolonged heat treatment causes gel liquefaction. Alkali can cause depolymerization of glutelin and form a gel network, while higher alkali concentration contributes to the gel network mainly through the formation of disulfide bonds.
FOOD HYDROCOLLOIDS
(2024)
Article
Food Science & Technology
Xin Zhang, Yu Zhao, Tianyi Zhang, Yan Zhang, Lianzhou Jiang, Xiaonan Sui
Summary: This study investigated the potential use of a mixture of soy protein concentrate (SPC) and wheat gluten (WG) in the production of meat analogs through high moisture extrusion. The results showed that a blend of SPC-WG at a 50/50 ratio resulted in the best fibrous structures, and hydrogen and disulfide bonds played a major role in the extrusion process.
LWT-FOOD SCIENCE AND TECHNOLOGY
(2022)
Article
Chemistry, Applied
Renjie Li, Pernille Lund, Soren B. Nielsen, Marianne N. Lund
Summary: This study aimed to generate soluble aggregates of whey protein isolates at lower temperature through partial hydrolysis before thermal treatment. The partial hydrolysis induced structural changes and exposure of free thiol groups in the proteins, resulting in soluble protein aggregates with a particle size range of 10-100 nm in radius for BLP treatment and 7-50 nm for TP treatment. Additionally, disulfide bonds were found to contribute to the association of protein aggregates, but the aggregates obtained were not stable under UHT conditions.
FOOD HYDROCOLLOIDS
(2022)
Article
Agriculture, Multidisciplinary
Xiao-Long Li, Qiu-Tao Xie, Wen-Jie Liu, Bao-Cai Xu, Bao Zhang
Summary: Pea protein isolate nanoparticles (PPINs) were successfully prepared using potassium metabisulfite, with disulfide bonds disrupted and PPINs formed through self-assembly. The increase in beta-sheet content and formation mechanism involving hydrophobic, disulfide, and hydrogen bonding were key factors in PPIN formation. This study provided a simple and economical method for fabricating nanoparticles.
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Trang Van Tran, Hoa Nguyen, Luyen Vu, ChangWoo Lee
Summary: Glutaredoxin 3 (Grx3) is a redox protein that maintains structural integrity and glutathione (GSH) binding capabilities across different temperatures. This study investigates the roles of specific bonds in Grx3's structure and function, and how psychrophilic Grx3 variants adapt to cold environments. The highly conserved Arg51-Asp69 salt bridge and Gln56-His63 hydrogen bond are crucial for stabilizing the structure and catalytic activity of Grx3. Psychrophilic variants of Grx3 have adapted to cold environments by reducing GSH binding and increasing structural flexibility.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Amanda Lais de Souza Coto, Arthur Alexandre Pereira, Sabrina Dorta Oliveira, Milene Nobrega de Oliveira Moritz, Arthur Moraes Franco da Rocha, Paulo Roberto Dores-Silva, Noeli Soares Melo da Silva, Ana Rita de Araujo Nogueira, Lisandra Marques Gava, Thiago Vagas Seraphim, Julio Cesar Borges
Summary: J-domain proteins form a large molecular chaperone family involved in proteostasis processes, with hDjC20 playing a vital role in mitochondria and being heavily influenced by the presence of Zn+2.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Meiling Zhang, Jiaxiang Zhang, Yan Liang, Shicheng Tian, Shuyang Xie, Tong Zhou, Qin Wang
Summary: This study determined the crystal structures of RGLG2 VWA domain in Arabidopsis thaliana, revealing that Ca2+ ions act as regulators and affect the conformational change of RGLG2-VWA domain.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Alexandra Bork, Sander H. J. Smits, Lutz Schmitt
Summary: This study reveals the structure and calcium ion binding properties of CBL1 protein, and proposes a binding model of CBL1 for Ca2+. Additionally, it provides preliminary insights into the formation of the dimer interface of CBL1.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Evgeniia V. Leisi, Andrey V. Moiseenko, Sofia S. Kudryavtseva, Denis V. Pozdyshev, Vladimir I. Muronetz, Lidia P. Kurochkina
Summary: The pathogenesis of prion diseases involves the transformation of prion protein into an insoluble form. This study found that two phage chaperonins can promote the fibrillation of prion protein in an ATP-dependent manner, resulting in the formation of less toxic large clusters. These fibrils differ in morphology and properties from those formed spontaneously in acidic pH with denaturants.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Gaurab Chowdhury, Saroj Biswas, Yuthika Dholey, Puja Panja, Sumit Das, Subrata Adak
Summary: Magnesium is an important divalent cation for regulating enzyme activity. The binding of Mg2+ through the PAS domain inhibits phosphoglycerate kinase (PGK) activity in LmPAS-PGK at neutral pH, but PGK activity is derepressed at acidic pH. Mutation studies revealed that the Asp-4 residue is crucial for Mg2+ binding at neutral pH.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Shima Ghaedizadeh, Majid Zeinali, Bahareh Dabirmanesh, Behnam Rasekh, Khosrow Khajeh, Ali Mohammad Banaei-Moghaddam
Summary: Implementing hyperthermostable carbonic anhydrases into CO2 capture and storage technologies can increase the rate of CO2 absorption from industrial flue gases. This study successfully improved the thermostability of a known hyperthermostable carbonic anhydrase through rational engineering of a single-point mutation.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)
Article
Biochemistry & Molecular Biology
Khaled A. Elnahriry, Dorothy C. C. Wai, Lauren M. Ashwood, Muhammad Umair Naseem, Tibor G. Szanto, Shaodong Guo, Gyorgy Panyi, Peter J. Prentis, Raymond S. Norton
Summary: Sea anemone venom contains a peptide called Tst2, which shows sequence similarity to peptides that interact with various ion channels. Recombinant Tst2 was successfully produced and its structure and function were studied. The results showed that Tst2 is an inhibitor of the TRPV1 channel.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2024)