| Glutaredoxin | ||
|---|---|---|
| Identifiers | ||
| Symbol | Glutaredoxin | |
| Pfam | PF00462 | |
| InterPro | IPR002109 | |
| PROSITE | PDOC00173 | |
| SCOP | 1kte | |
| OPM family | 139 | |
| OPM protein | 1z9h | |
| Available PDB structures:
1ykaA:17-81 1wikA:250-314 2cq9A:69-131 2flsA:69-131 1jhb :15-80 1b4qA:15-80 1kte :15-80 1nm3B:172-230 3grx :4-63 1ilbA:4-63 1fovA:4-63 1ego :3-69 1egr :3-69 1grx :3-69 1qfnA:3-69 1aazB:2-76 1de2A:2-76 1de1A:2-76 1aba :2-76 1nhoA:5-66 1fo5A:6-67 1j08A:138-162 1a8l :138-162 1r7hB:3-61 1h75A:3-61 1z9hB:102-152 1hyuA:155-181 1zypB:155-181 1zynB:155-181 |
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Glutaredoxins[1][2][3] are small redox enzymes of approximately one hundred amino-acid residues which use glutathione as a cofactor. Pfam is a large collection of Multiple sequence alignment and Hidden Markov models covering many common protein domains and families InterPro is a database of protein families domains and functional sites in which identifiable features found in known proteins can be applied to new protein sequences PROSITE is a database of Protein families and domains. It consists of entries describing the domains families and functional sites as well as amino acid The Structural Classification of Proteins (SCOP database is a largely manual classification of protein Structural domains based on similarities of their Amino acid Orientations of Proteins in Membranes (OPM database provides spatial positions of protein three-dimensional structures with respect to the Lipid bilayer. Orientations of Proteins in Membranes (OPM database provides spatial positions of protein three-dimensional structures with respect to the Lipid bilayer. The Protein Data Bank ( PDB) is a repository for 3-D structural data of Proteins and Nucleic acids These data typically obtained by X-ray crystallography Redox (shorthand for reduction-oxidation reaction describes all Chemical reactions in which atoms have their Oxidation number ( Oxidation state Glutathione ( GSH) is a Tripeptide. It contains an unusual Peptide linkage between the amine group of Cysteine and the Carboxyl Glutaredoxins are oxidised by substrates, and reduced non-enzymatically by glutathione. In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Thioredoxins are Proteins that act as antioxidants by facilitating the reduction of other proteins by Cysteine Thiol-disulfide exchange. Thioredoxin Reductase (TR TrxR ( are the only known enzymes to reduce Thioredoxin (Trx Instead, oxidized glutathione is regenerated by glutathione reductase. Glutathione reductase, also known as GSR, is a human Gene. The Protein encoded by this gene is an Enzyme ( which reduces Glutathione Together these components compose the glutathione system[4].
Glutaredoxins function as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. A deoxyribonucleotide is the Monomer, or single unit of DNA, or deoxyribonucleic acid Ribonucleotide reductase (RNR is an Enzyme that controls the cellular concentration of Deoxyribonucleotides Biosynthesis begins with the building up of Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active centre disulfide bond[5]. Thioredoxins are Proteins that act as antioxidants by facilitating the reduction of other proteins by Cysteine Thiol-disulfide exchange. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulfide bond.
Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed[6] that Vaccinia virus protein O2L is most probably a glutaredoxin. Vaccinia virus ( VACV or VV) is a large complex enveloped Virus belonging to the Poxvirus family Finally, it must be noted that Bacteriophage T4 thioredoxin seems also to be evolutionary related. Enterobacteria phage T4 is a Phage that infects E coli bacteria. In position 5 of the pattern T4 thioredoxin has Val instead of Pro.
Contents |
Subfamilies
- Glutaredoxin subgroup IPR014025
Human proteins containing this domain
GLRX; GLRX2; GLRX3; GLRX5; PTGES2; TXNL3;
References
- ^ Holmgren A, Gleason FK (1988). Glutaredoxin (thioltransferase, also known as GLRX, is a human Gene. Glutaredoxin 2, also known as GLRX2, is a human Gene. Thioredoxin-like 2, also known as TXNL2, is a human Gene. "Thioredoxin and related proteins in procaryotes". FEMS Microbiol. Rev. 4 (4): 271–297. PMID 3152490.
- ^ Holmgren A (1988). "Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulfide bonds". Biochem. Soc. Trans. 16 (2): 95–96. PMID 3286320.
- ^ Holmgren A (1989). "Thioredoxin and glutaredoxin systems". J. Biol. Chem. 264 (24): 13963–13966. PMID 2668278.
- ^ Holmgren A, Fernandes AP (2004). "Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system". Antioxid. Redox. Signal. 6 (1): 63–74. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 14713336.
- ^ Nilsson L, Foloppe N (2004). "The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues". Structure 12 (2): 289–300. PMID 14962389.
- ^ Johnson GP, Goebel SJ, Perkus ME, Davis SW, Winslow JP, Paoletti E (1991). "Vaccinia virus encodes a protein with similarity to glutaredoxins". Virology 181 (1): 378–381. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 1994586.
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