User:Emma Ste.Marie/Sandbox 1
From Proteopedia
| Line 1: | Line 1: | ||
| - | <Structure load='4j56' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />== Introduction == | + | <Structure load='4j56' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> |
| + | |||
| + | == Introduction == | ||
Thioredoxin reductases (TRs) are a family of pyridine nucleotide-disulphide oxidoreductases that catalyze the reduction of thioredoxin, a class of small redox proteins known to be present in all organisms. Thioredoxin plays a role in many important biological processes, including redox signalling. There are two classes of TRs that differ by size and the number of redox centers present in the enzyme. The lower molecular weight TRs from bacteria have two redox centers (FADH and a disulfide redox center), while higher molecular weight TRs from higher eukaryotes contain three redox centers (FADH and two disulfide redox centers)1. Mammalian Thioredoxin reductases (mTRs) are considered higher molecular weight and have mechanistic similarities to glutathione reductases2. Like other TRs, mTRs catalyse the NADPH-dependent reduction of the redox protein thioredoxin (Trx), as well as of other endogenous and exogenous compounds2. Unlike glutathione reductase or Escherichia coli (E. coli) thioredoxin reductase, type 1 mTRs contain a second redox-active site: A C-terminal Gly-Cys-Sec-Gly motif in which the penultimate Sec residue and the neighboring Cys residue exist in an 8-membered ring containing a selenosulfide bond in its reduced state1-3. | Thioredoxin reductases (TRs) are a family of pyridine nucleotide-disulphide oxidoreductases that catalyze the reduction of thioredoxin, a class of small redox proteins known to be present in all organisms. Thioredoxin plays a role in many important biological processes, including redox signalling. There are two classes of TRs that differ by size and the number of redox centers present in the enzyme. The lower molecular weight TRs from bacteria have two redox centers (FADH and a disulfide redox center), while higher molecular weight TRs from higher eukaryotes contain three redox centers (FADH and two disulfide redox centers)1. Mammalian Thioredoxin reductases (mTRs) are considered higher molecular weight and have mechanistic similarities to glutathione reductases2. Like other TRs, mTRs catalyse the NADPH-dependent reduction of the redox protein thioredoxin (Trx), as well as of other endogenous and exogenous compounds2. Unlike glutathione reductase or Escherichia coli (E. coli) thioredoxin reductase, type 1 mTRs contain a second redox-active site: A C-terminal Gly-Cys-Sec-Gly motif in which the penultimate Sec residue and the neighboring Cys residue exist in an 8-membered ring containing a selenosulfide bond in its reduced state1-3. | ||
Revision as of 21:19, 26 April 2018
|
Introduction
Thioredoxin reductases (TRs) are a family of pyridine nucleotide-disulphide oxidoreductases that catalyze the reduction of thioredoxin, a class of small redox proteins known to be present in all organisms. Thioredoxin plays a role in many important biological processes, including redox signalling. There are two classes of TRs that differ by size and the number of redox centers present in the enzyme. The lower molecular weight TRs from bacteria have two redox centers (FADH and a disulfide redox center), while higher molecular weight TRs from higher eukaryotes contain three redox centers (FADH and two disulfide redox centers)1. Mammalian Thioredoxin reductases (mTRs) are considered higher molecular weight and have mechanistic similarities to glutathione reductases2. Like other TRs, mTRs catalyse the NADPH-dependent reduction of the redox protein thioredoxin (Trx), as well as of other endogenous and exogenous compounds2. Unlike glutathione reductase or Escherichia coli (E. coli) thioredoxin reductase, type 1 mTRs contain a second redox-active site: A C-terminal Gly-Cys-Sec-Gly motif in which the penultimate Sec residue and the neighboring Cys residue exist in an 8-membered ring containing a selenosulfide bond in its reduced state1-3.
Your Heading Here (maybe something like 'Structure')
| |||||||||||
References
1. Hondal, R. J.; Ruggles, E. L., Differing views of the role of selenium in thioredoxin reductase. Amino acids 2011, 41 (1), 73-89. 2. Mustacich, D.; Powis, G., Thioredoxin reductase. Biochemical Journal 2000, 346 (1), 1-8. 3. (a) Lothrop, A. P.; Snider, G. W.; Flemer Jr, S.; Ruggles, E. L.; Davidson, R. S.; Lamb, A. L.; Hondal, R. J., Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry 2014, 53 (4), 664-674; (b) Ruggles, E. L.; Deker, P. B.; Hondal, R. J., Conformational analysis of oxidized peptide fragments of the C‐terminal redox center in thioredoxin reductases by NMR spectroscopy. Journal of Peptide Science 2014, 20 (5), 349-360.
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
