2003
DOI: 10.1042/bj20021455
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Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation

Abstract: The facultatively anaerobic bacterium Alcaligenes defragrans NKNTAU was found to oxidize taurine (2-aminoethanesulphonate) with nitrate as the terminal electron acceptor. Taurine was transaminated to 2-sulphoacetaldehyde. This was not converted into sulphite and acetate by a "sulphoacetaldehyde sulpho-lyase" (EC 4.4.1.12), but into sulphite and acetyl phosphate, which was identified by three methods. The enzyme, which required the addition of phosphate, thiamin diphosphate and Mg(2+) ions for activity, was ren… Show more

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Cited by 71 publications
(119 citation statements)
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“…Primers were selected from a set designed to amplify the highly similar gene clusters from other Paracoccus spp. (Ruff et al, 2003;Brüggemann et al, 2004;T. H. M. Smits, unpublished).…”
Section: Methodsmentioning
confidence: 98%
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“…Primers were selected from a set designed to amplify the highly similar gene clusters from other Paracoccus spp. (Ruff et al, 2003;Brüggemann et al, 2004;T. H. M. Smits, unpublished).…”
Section: Methodsmentioning
confidence: 98%
“…The assay for taurine dehydrogenase, analogous to that for N-methyltaurine dehydrogenase, was described previously (Brüggemann et al, 2004). Sulfoacetaldehyde acetyltransferase (Xsc) was assayed by the colorimetric determination of acetyl phosphate or by the formation of sulfite (Ruff et al, 2003). Phosphotransacetylase was assayed photometrically as the CoA-SH-dependent formation of acetyl-CoA (Bergmeyer et al, 1983).…”
Section: Methodsmentioning
confidence: 99%
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