Search by BoMiProt ID - Bomi72


Primary Information

BoMiProt ID Bomi72
Protein Name Peroxiredoxin-1
Organism Bos taurus
Uniprot IdQ5E947
Milk FractionMFGM, Exosome
Amino Acid Lenth 199
Molecular Weight 22210
Fasta Sequence https://www.uniprot.org/uniprot/Q5E947.fasta
Gene Name PRDX1
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Presence in other biological fluids/tissue/cells expression of Prx1 in Cytosol, nucleus; prx2 in Cytosol, membrane; prx3 in Mitochondria; prx4 in Cytosol, Golgi, secreted; prx5 in Mitochondria, peroxisome, cytosol; prx 6 in Cytosol
Protein Function Peroxiredoxins (Prxs) are a ubiquitous family of cysteine-dependent peroxidase enzymes that play dominant roles in regulating peroxide levels within cells; the peroxidase activity of Prx enzymes towards H2O2, organic hydroperoxides and peroxynitrite is critical to protect cellular components from oxidative damage; play cytoprotective antioxidant role in inflammation
Biochemical Properties Mammalian cells express six Prx isoforms (PrxI to PrxVI), which can be classified into 2-Cys (PrxI to PrxIV), atypical 2-Cys (PrxV), and 1-Cys (PrxVI) subfamilies;hydrogen peroxide caused rapid inactivation of human Prx I by hyperoxidation during catalytic turnover; cysteine-based peroxidases that do not require any special cofactors for their activity; a peroxidatic Cys (CP) thiolate (CP-S−) attacks a hydroperoxide substrate and is oxidized to a CP-sulfenic acid (CP-SOH); In mammals, Prx1 subfamily enzymes are in the cytosol and nucleus (PrxI and PrxII), the mitochondria (PrxIII) and the endoplasmic reticulum (PrxIV); In Prxs, the CP pKa values determined for nearly a dozen representatives are clustered between 5.1 and 6.3; 83% of the CP residues being present in the thiolate form at pH 7; Factors promoting oligomerization in typical 2-Cys Prxs include high [37] or low [34,39] ionic strength, low pH [40], high magnesium [34] or calcium [41,42] concentrations, reduction of the redox-active disulfide center [20,22,36], and ‘overoxidation’ of the peroxidatic cysteine to a sulfinic acid
Significance in milk induce the oxidation of various leuco compounds by hydrogen peroxide - distinguishes between raw and boiled milk; milk sterilized at or above 80’ C, do not show the peroxidase reaction; whereas raw milks, as a class, do give the reaction;
PTMs phosphorylation of mammalian PrxI, PrxII, PrxIII and PrxIV at the conserved residue Thr89 (PrxII numbering) by cyclin-dependent kinases ;lipid raft associated prx1 undergoes phosphorylation at Tyr194; centrosomeassociated PrxI through phosphorylation at Thr9;
Significance of PTMs phosphorylation leads to inactivation of this enxyme
Linking IDs Bomi2505 Bomi2506 Bomi2507
Bibliography 1. Kappeler, S. R., Heuberger, C., Farah, Z., & Puhan, Z. (2004). Expression of the peptidoglycan recognition protein, PGRP, in the lactating mammary gland. Journal of Dairy Science, 87(8), 2660–2668. https://doi.org/10.3168/jds.S0022-0302(04)73392-5.
2. Dziarski, R. (2004). Peptidoglycan recognition proteins (PGRPs). Molecular Immunology, 40(12), 877–886. https://doi.org/10.1016/j.molimm.2003.10.011.
3. Parsonage, D., Youngblood, D. S., Sarma, G. N., Wood, Z. A., Karplus, P. A., & Poole, L. B. (2005). Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry, 44(31), 10583–10592. https://doi.org/10.1021/bi050448i.
4. Tydell, C. C., Yuan, J., Tran, P., & Selsted, M. E. (2006). Bovine peptidoglycan recognition protein-S: antimicrobial activity, localization, secretion, and binding properties. Journal of Immunology (Baltimore, Md. : 1950), 176(2), 1154–1162. https://doi.org/10.4049/jimmunol.176.2.1154.