Enzymes
| UniProtKB help_outline | 1 proteins |
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| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline choline sulfate Identifier CHEBI:16822 (Beilstein: 3905491; CAS: 4858-96-2) help_outline Charge 0 Formula C5H13NO4S InChIKeyhelp_outline WXCQAWGXWVRCGP-UHFFFAOYSA-N SMILEShelp_outline C[N+](C)(C)CCOS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline choline Identifier CHEBI:15354 (Beilstein: 1736748; CAS: 62-49-7) help_outline Charge 1 Formula C5H14NO InChIKeyhelp_outline OEYIOHPDSNJKLS-UHFFFAOYSA-N SMILEShelp_outline C[N+](C)(C)CCO 2D coordinates Mol file for the small molecule Search links Involved in 56 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sulfate Identifier CHEBI:16189 (Beilstein: 3648446; CAS: 14808-79-8) help_outline Charge -2 Formula O4S InChIKeyhelp_outline QAOWNCQODCNURD-UHFFFAOYSA-L SMILEShelp_outline [O-]S([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 89 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:20820 | RHEA:20821 | RHEA:20822 | RHEA:20823 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Presence of a gene encoding choline sulfatase in Sinorhizobium meliloti bet operon: choline-O-sulfate is metabolized into glycine betaine.
Oesteras M., Boncompagni E., Vincent N., Poggi M.-C., Le Rudulier D.
Glycine betaine is a potent osmoprotectant accumulated by Sinorhizobium meliloti to cope with osmotic stress. The biosynthesis of glycine betaine from choline is encoded by an operon of four genes, betICBA, as determined by sequence and mutant analysis. The betI and betC genes are separated by an ... >> More
Glycine betaine is a potent osmoprotectant accumulated by Sinorhizobium meliloti to cope with osmotic stress. The biosynthesis of glycine betaine from choline is encoded by an operon of four genes, betICBA, as determined by sequence and mutant analysis. The betI and betC genes are separated by an intergenic region containing a 130-bp mosaic element that also is present between the betB and betA genes. In addition to the genes encoding a presumed regulatory protein (betI), the betaine aldehyde dehydrogenase (betB), and the choline dehydrogenase (betA) enzymes also found in Escherichia coli, a new gene (betC) was identified as encoding a choline sulfatase catalyzing the conversion of choline-O-sulfate and, at a lower rate, phosphorylcholine, into choline. Choline sulfatase activity was absent from betC but not from betB mutants and was shown to be induced indifferently by choline or choline-O-sulfate as were the other enzymes of the pathway. Unlike what has been shown in other bacteria and plants, choline-O-sulfate is not used as an osmoprotectant per se in S. meliloti, but is metabolized into glycine betaine. S. meliloti also can use this compound as the sole carbon, nitrogen, and sulfur source for growth and that depends on a functional bet locus. In conclusion, choline-O-sulfate and phosphorylcholine, which are found in higher plants and fungi, appear to be substrates for glycine betaine biosynthesis in S. meliloti. << Less
Proc. Natl. Acad. Sci. U.S.A. 95:11394-11399(1998) [PubMed] [EuropePMC]