Code | CSB-YP332605ENV |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP332605ENV |
MSDS | |
Size | Pls inquire |
Source | E.coli |
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Code | CSB-EP332605ENV-B |
MSDS | |
Size | Pls inquire |
Source | E.coli |
Conjugate | Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. |
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Code | CSB-BP332605ENV |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP332605ENV |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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Ubiquinone biosynthesis protein UbiV is a crucial component in the biosynthesis of ubiquinone (UQ), also known as coenzyme Q. UbiV is involved in the anaerobic UQ biosynthesis pathway, working in conjunction with other proteins such as UbiU and UbiT under anaerobic conditions [1]. The biosynthesis of UQ initiates with the conversion of chorismate to 4-hydroxybenzoate, followed by the transfer of the aliphatic chain of farnesylfarnesylgeranyl-PP to the hydroxybenzoate, a process in which UbiV plays a significant role [2]. Additionally, UbiV is essential for the hydroxylation reactions of the O2-independent UQ biosynthesis pathway, indicating its crucial function in UQ biosynthesis [3].
Furthermore, the UbiV protein is part of a group of enzymes that are solely required under anaerobic conditions, highlighting its specific role in adapting to changing respiratory conditions [1]. The identification of UbiV and its conserved domain structure has contributed to a better understanding of the UQ biosynthesis pathway, emphasizing its significance in cellular metabolism and energy production [4].
References:
[1] R. Arias-Cartin, K. Ferizhendi, E. Scotet, L. Pelosi, C. Loeuillet, F. Pierrelet al., "Role of theescherichia coliubiquinone-synthesizing ubiuvt pathway in adaptation to changing respiratory conditions",, 2023. https://doi.org/10.1101/2023.03.15.532739
[2] E. Rangarajan, Y. Li, P. Iannuzzi, A. Tocilj, L. Hung, A. Matteet al., "Crystal structure of a dodecameric fmn‐dependent ubix‐like decarboxylase (pad1) from escherichia coli o157: h7", Protein Science, vol. 13, no. 11, p. 3006-3016, 2004. https://doi.org/10.1110/ps.04953004
[3] L. Pélosi, C. Vo, S. Abby, L. Loiseau, B. Rascalou, M. Chehadeet al., "Ubiquinone biosynthesis over the entire o2 range: characterization of a conserved o2-independent pathway", Mbio, vol. 10, no. 4, 2019. https://doi.org/10.1128/mbio.01319-19
[4] M. Cevallos and M. Esposti, "New alphaproteobacteria thrive in the depths of the ocean with oxygen gradient", Microorganisms, vol. 10, no. 2, p. 455, 2022. https://doi.org/10.3390/microorganisms10020455
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KEGG: ecj:JW5530
STRING: 316385.ECDH10B_3332