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Literature summary for 1.14.15.7 extracted from

  • Mitsuya, S.; Kozaki, K.; Takabe, T.
    Tissue localization of the glycine betaine biosynthetic enzymes in barley leaves (2013), Plant Prod. Sci., 16, 117-122.
No PubMed abstract available
Search for more literature for 1.14.15.7

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
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 ssp. vulgare, cv. Haruna-nijyo
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Source Tissue

Source Tissue Comment Organism Textmining
bundle sheath cell colocalization with betaine aldehyde dehydrogenase Hordeum vulgare
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leaf
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 Hordeum vulgare
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mesophyll colocalization with betaine aldehyde dehydrogenase Hordeum vulgare
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additional information salt treatment results in increased expression of the enzyme mainly in the leaves but not in the roots Hordeum vulgare
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root
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 Hordeum vulgare
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Synonyms

Synonyms Comment Organism
CMO
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 Hordeum vulgare

Expression

Organism Comment Expression
Hordeum vulgare expression of CMO protein is increased by the presence of NaCl in younger leaves but decreased in older leaves down
Hordeum vulgare salt treatment results in increased expression of the enzyme mainly in the leaves but not in the roots. Thereby the expression of CMO protein is increased by the presence of NaCl in younger leaves but decreased in older leaves up

General Information

General Information Comment Organism
metabolism choline monooxygenase is the first regulatory enzyme in the biosynthetic pathway for glycine betaine Hordeum vulgare
physiological function choline monooxygenase is the first regulatory enzyme in the biosynthetic pathway for glycine betaine, which preferentially protects young organs against salt-induced damage by altering the expression of glycine betaine biosynthetic proteins at a translational level Hordeum vulgare