advances-in-protein-chemistry

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Editors Dr. Ghulam Md Ashraf (Email: ashraf.gm@gmail.com) Dr. Ishfaq Ahmed Sheikh (Email: sheikhishfaq@gmail.com) King Fahd Medical Research Center King Abdulaziz University, P.O. Box 80216 Jeddah, Saudi Arabia
Tyrosine Nitrated Proteins: Biochemistry and Pathophysiology Abstract Haseeb Ahsan* Department of Biochemistry, Faculty of Dentistry, Jamia Millia Islamia (A Central University), Okhla, New Delhi – 110025, India *Corresponding author: Dr. Haseeb Ahsan, Department of Biochemistry, Faculty of Dentistry, Jamia Millia Islamia (A Central University), Okhla, New Delhi – 110025, India, E-mail: drhahsan@ gmail.com The free radical-mediated damage to proteins results in the modification of amino acid residues, cross-linking of side chains and fragmentation. L-tyrosine and protein bound tyrosine are prone to attack by various mediators and reactive nitrogen intermediates to form 3-nitrotyrosine (3-NT). 3-NT formation is also catalyzed by a class of peroxidases utilizing nitrite and hydrogen peroxide as substrates. Evidence supports the formation of 3-NT in vivo in diverse pathologic conditions and 3-NT is thought to be a relatively specific marker of oxidative damage. The formation of nitrotyrosine represents a specific peroxynitrite-mediated protein modification; thus, detection of nitrotyrosine in proteins is considered as a biomarker for endogenous peroxynitrite activity. Formation of tyrosine nitrated proteins is considered to be a post-translational modification with important pathophysiological consequences and is one of the markers of nitrosative stress that have been reported in neurodegeneration, inflammatory and other pathological conditions. Introduction Most proteins contain tyrosine residues with a natural abundance of about 3% [1]. Tyrosine (one letter abbreviation, Y; three letter abbreviation, Tyr; also known as 4-hydroxyphenylalanine) is a non-essential amino acid and a member of the aromatic amino acid group. Tyrosine is mildly hydrophilic, a characteristic feature that is explained by the rather hydrophobic aromatic benzene ring carrying a hydroxyl group. As a consequence, tyrosine is often surface-exposed in proteins (only 15% of tyrosine residues are buried inside a protein) and therefore should be available for modification such as nitration by various factors [2-4]. Tyrosine can be modified by the addition of a nitro group (-NO 2 ) in vivo with several agents resulting in the formation of 3-nitrotyrosine (3-NT) or tyrosine nitrated proteins (Figure 1). 3-NT [(2-Amino-3-(4-hydroxy-3-nitrophenyl) propanoic acid)] is a post-translational modification in proteins occurring through the action of a nitrating agent resulting in the addition of a -NO 2 group (in ortho position RNS COO- COO- NO 2 metabolism OH Tyrosine (Tyr) Tyrosine decarboxylase OH Nitrotyrosine (3-NT) Tyramine oxidase metabolism COO- + + NH 3 NH 3 COO- RNS OH p-hydroxyphenylacetic acid (PHPA) OH NO 2 3-nito-4-hydroxyphenylacetic acid (NHPA) Figure 1: Metabolism of tyrosine leading to the formation of products: p-hydroxyphenylacetic acid and 3-nitro-4-hydroxyphenylacetic acid (adapted from Mani et al., 2003). OMICS Group eBooks 003
Page 1: www.esciencecentral.org/ebooks Adva
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Proteins and Peptides- Reemergence
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purification methodology and laid t
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