The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) . The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
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SYSTEMATIC NAME
IUBMB Comments
choline,reduced-ferredoxin:oxygen oxidoreductase
The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [7]. The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
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
choline monooxygenase and betaine aldehyde dehydrogenase catalyze the first and second steps in the biosynthesis of glycine betaine in betaine-accumulating plants
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
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
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
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
increase of betaine content in bladder hairs under high salinity is associated with induced expression of the choline monooxygenayse protein in mature leaves
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
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