1.14.15.7: choline monooxygenase
This is an abbreviated version!
For detailed information about choline monooxygenase, go to the full flat file.
Word Map on EC 1.14.15.7
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1.14.15.7
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betaine
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osmoprotectant
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drought
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badhs
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oleracea
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spinacia
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glycinebetaine
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halophyte
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beet
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atriplex
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rieske-type
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rieske
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suaeda
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phosphocholine
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amaranthus
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hortensis
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ferredoxin-dependent
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amaranthaceae
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salsa
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tricolor
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agriculture
- 1.14.15.7
- betaine
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osmoprotectant
- drought
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badhs
- oleracea
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spinacia
- glycinebetaine
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halophyte
- beet
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atriplex
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rieske-type
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rieske
- suaeda
- phosphocholine
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amaranthus
- hortensis
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ferredoxin-dependent
- amaranthaceae
- salsa
- tricolor
- agriculture
Reaction
Synonyms
AhCMO, AnCMO, ApCMO, choline monooxygenase, choline oxygenase, CMO, CMO1, EC 1.14.14.4, Os06g48510
ECTree
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General Information
General Information on EC 1.14.15.7 - choline monooxygenase
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metabolism
physiological function
additional information
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the CMO upstream regulatory region reveals a number of stress response-related elements, some of which may be involved in the stress tolerance shown by this species. Salt stress is perceived differently by cells than in whole plants
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choline monooxygenase and betaine aldehyde dehydrogenase catalyze the first and second steps in the biosynthesis of glycine betaine in betaine-accumulating plants
metabolism
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choline monooxygenase is the first regulatory enzyme in the biosynthetic pathway for glycine betaine
metabolism
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choline monooxygenase is the first regulatory enzyme in the biosynthetic pathway for glycine betaine
metabolism
glycine betaine is a compatible quaternary amine that enables plants to tolerate abiotic stresses, including salt, drought and cold. In plants, glycine betaine is synthesized through two-step of successive oxidations from choline, catalyzed by choline monooxygenase and betaine aldehyde dehydrogenase, respectively. Oryza sativa is a typical non-glycine betaine accumulating species. The genome sequencing reveals orthologues of both choline monooxygenase and betaine aldehyde dehydrogenase, but, while the betaine aldehyde dehydrogenase is functional, the choline monooxygenase of japonica rice plant is not. Nevertheless the heterologously expressed rice enzyme is active in tabacco plants, overview
metabolism
the enzyme catalyzes the first stepin biosynthesis of glycine betaine. The second step is catalyzed by betaine aldehyde dehydrogenase
the enzyme catalyzes the first step in the biosynthesis of glycinebetaine from cholesterol via betaine aldehyde. Glycine betaine is an osmoprotectant that accumulates in case of high salinity, and drought or cold stress
physiological function
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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
physiological function
antisense CMO plants show decreased activity of glycine betaine synthesis from choline compared to wild-type plants, with glycine betaine contents being similar between transgenic and wild-type plants with the exception of young leaves and storage roots. Transgenic plants show enhanced susceptibility to salt stress
physiological function
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increase of betaine content in bladder hairs under high salinity is associated with induced expression of the choline monooxygenayse protein in mature leaves
physiological function
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the ability to utilize choline as a sole nitrogen source correlates strongly with the presence of Cmo1. Deletion of the gene abolishes the ability of Scheffersomyces stipitis to utilize choline as the sole nitrogen source, but does not affect its ability to use methylamine, dimethylamine, trimethylamine, ethylamine, diethylamine, ethanolamine or glycine as nitrogen sources
physiological function
the intracellular glycine betaine level and the tolerance to salt stress of the transgenic lines overexpressing CMO1 are significantly enhanced
physiological function
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the ability to utilize choline as a sole nitrogen source correlates strongly with the presence of Cmo1. Deletion of the gene abolishes the ability of Scheffersomyces stipitis to utilize choline as the sole nitrogen source, but does not affect its ability to use methylamine, dimethylamine, trimethylamine, ethylamine, diethylamine, ethanolamine or glycine as nitrogen sources
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