Structured Summary
Abstract
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
MeSH Record
Classification
Broader headings
Related Concepts
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MeSH Record
Synonyms
10 entry terms
- Glutaredoxin
- Thioltransferase
- Glutaredoxin 1
- Glutaredoxin 2
- Glutaredoxin 3
- Glutaredoxin 5
- TTase-1
- Thioltransferase-1
- TTase 1
- Thioltransferase 1
MeSH Record
Aspects Covered
29 allowable subheadings
Indexed with the subheadings administration & dosage, adverse effects, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.
MeSH Record
History Note
2008(1980); use PROTEINS 1979
MeSH Hierarchy
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AMA Style
References
- National Library of Medicine. Glutaredoxins. Medical Subject Headings (MeSH). 2026. Unique ID D054477. http://id.nlm.nih.gov/mesh/2026/D054477
- Glutaredoxins. In: Wikidata. https://www.wikidata.org/wiki/Q21103160