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Literature summary 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

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.7 Hordeum vulgare
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 ssp. vulgare, cv. Haruna-nijyo
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.15.7 bundle sheath cell colocalization with betaine aldehyde dehydrogenase Hordeum vulgare
-
1.14.15.7 leaf
-
 Hordeum vulgare
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1.14.15.7 mesophyll colocalization with betaine aldehyde dehydrogenase Hordeum vulgare
-
1.14.15.7 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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1.14.15.7 root
-
 Hordeum vulgare
-

Synonyms

EC Number Synonyms Comment Organism
1.14.15.7 CMO
-
 Hordeum vulgare

Expression

EC Number Organism Comment Expression
1.14.15.7 Hordeum vulgare expression of CMO protein is increased by the presence of NaCl in younger leaves but decreased in older leaves down
1.14.15.7 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

EC Number General Information Comment Organism
1.14.15.7 metabolism choline monooxygenase is the first regulatory enzyme in the biosynthetic pathway for glycine betaine Hordeum vulgare
1.14.15.7 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