Structured Summary
Abstract
An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC 2.3.1.28.
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Synonyms
8 entry terms
- CAT Enzyme
- Chloramphenicol Acetyltransferase
- Chloramphenicol Transacetylase
- Acetyltransferase, Chloramphenicol
- Chloramphenicol O Acetyltransferase
- Enzyme, CAT
- O-Acetyltransferase, Chloramphenicol
- Transacetylase, Chloramphenicol
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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
1998(1989)
MeSH Record
Previous Indexing
- Acetyltransferases (1973-1988)
- Transferases (1966-1972)
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AMA Style
References
- National Library of Medicine. Chloramphenicol O-Acetyltransferase. Medical Subject Headings (MeSH). 2026. Unique ID D015500. http://id.nlm.nih.gov/mesh/2026/D015500
- Chloramphenicol O-Acetyltransferase. In: Wikipedia. https://en.wikipedia.org/wiki/Chloramphenicol_acetyltransferase
- Chloramphenicol O-Acetyltransferase. In: Wikidata. https://www.wikidata.org/wiki/Q24744759