Theanine /ˈθiːəniːn/, also known as L-theanine, L-γ-glutamylethylamide, N⁵-ethyl-L-glutamine, or γ-glutamylethylamide is a bioactive, non-proteinogenic amino acid similar to the proteinogenic amino acids glutamic acid and L-glutamine. It is produced by certain plants such as the tea plant (Camellia sinensis), and by some fungi. Theanine was discovered in 1949 as a constituent of green tea and was isolated in 1950 from gyokuro tea leaves. Additionally, theanine constitutes about 1–2% of the dry weight of green tea leaves.

The name theanine usually refers to the enantiomer L-theanine, which is the form found in tea leaves from which it is extracted as a powder. The right-handed enantiomer, D-theanine, is less-studied.

Theanine is sold as a dietary supplement. It is packaged in gelatin capsules, tablets, and as a powder, and may be an ingredient in branded supplements with caffeine. It is also used as an ingredient in food and beverages. Japan approved its unlimited use in all foods (including chocolates, soft drinks, and herb teas) except infant food in 1964, and the US Food and Drug Administration has considered it to be safe at doses up to 250 milligrams (mg) per serving since 2007.

In 2011, the European Food Safety Authority found there was insufficient evidence for a causal relationship between theanine consumption and improved cognitive function, alleviation of psychological stress, maintenance of normal sleep, or reduction of menstrual discomfort. A 2025 review found that theanine has been poorly studied to date, having inconsistent research quality and unreliable clinical trials.

The chemical name N⁵-ethyl-L-glutamine and other synonyms (see box) for theanine reflect its chemical structure. The name theanine, without prefix, is generally understood to imply the L- (S-) enantiomer, derived from the related proteinogenic L-amino acid glutamic acid. Theanine is an analog of this amino acid, and its primary amide, L-glutamine (also a proteinogenic amino acid). Theanine is a derivative of glutamine that is ethylated on the amide nitrogen (as the name N⁵-ethyl-L-glutamine describes), or alternatively, to the amide formed from ethylamine and L-glutamic acid at its γ- (5-) side chain carboxylic acid group (as the name γ-L-glutamylethylamide describes).^{[citation needed]}

Relative to theanine, the opposite (D-, R-) enantiomer is largely absent from the literature, except implicitly. While natural extracts that are not harshly treated are presumed to contain only the biosynthetic L- enantiomeric form, mishandled isolates and racemic chemical preparations of theanines necessarily contain both theanine and its D-enantiomer (and from racemic syntheses, in equal proportion), and studies have suggested that the D-isomer may actually predominate in some commercial supplement preparations. Amino acid racemization in aqueous media is a well-established chemical process promoted by elevated temperature and non-neutral pH values; prolonged heating of Camellia extracts—possible for oversteeped teas and in undisclosed commercial preparative processes—has been reported to result in increasing racemization of theanine to give increasing proportions of the nonnatural D-theanine, up to equal proportions of each enantiomer.

Theanine is found primarily in plant and fungal species. It was discovered as a constituent of tea (Camellia sinensis) in 1949, and in 1950 a laboratory in Kyoto successfully isolated it from gyokuro leaf, which has high theanine content. Theanine is substantially present in black, green, and white teas from Camellia sinensis in quantities of about 1% of the dry weight. Deliberately shading tea plants from direct sunlight, as is done for matcha and gyokuro green tea, increases L-theanine content. The L-enantiomer is the form found in freshly prepared teas and some human dietary supplements.

As a structural analog of glutamate and glutamine, the theanine in teas or supplements is absorbed in the small intestine after oral ingestion; its hydrolysis to L-glutamate and ethylamine occur both in the intestine and liver, possibly functioning as a donor for glutamate synthesis.