Together with SuyA, desulfonates sulfolactate to pyruvate and sulfite. (R)-3-sulfolactate = H+ + pyruvate + sulfite

MALDFSNATVKAWRRENGRVGVRNHVLILPVDDISNAACEAVANNVKGTLAIPHAYGRLQ FGEDLELHFRTIIGTGANPNVAAVVVIGIEPEWTQVIVDGIAKTGKPVTGFSIEQKGDFE TIRQAGWKAKEYVHWASELQKEDCPISDLWISTKCGESDTTTGLSSCPTVGNMYDKLLPQ GIYGCFGETSEITGAEHICEKRAANPETARKFKEIWQAYSDDVIFAHQTDDLSDSQPTKG NILGGLTTIEEKALGNLEKIGRTSTYIDAMGPAETPSKGPGLYFMDSSSAAAECVTLMAA GGYVIHTFPTGQGNVVGNPIVPVIKISGNPRTLRTMSEHIDVDVTGVLTREMTIDQAGDA LIEMIIRTANGRMTAAEALGHREFSMTKLYRSA399

	PMID	Title & Author	Abstract	Year	Unnamed: 4
0	20007684	Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase Karin Denger , Alasdair M Cook	Chromohalobacter salexigens DSM 3043, whose genome has been sequenced, is known to degrade (R,S)-sulfolactate as a sole carbon and energy source for growth. Utilization of the compound(s) was shown to be quantitative, and an eight-gene cluster (Csal_1764-Csal_1771) was hypothesized to encode the enzymes in the degradative pathway. It comprised a transcriptional regulator (SuyR), a Tripartite Tricarboxylate Transporter-family uptake system for sulfolactate (SlcHFG), two sulfolactate dehydrogenases of opposite sulfonate stereochemistry, namely novel SlcC and ComC [(R)-sulfolactate dehydrogenase] [EC 1.1.1.272] and desulfonative sulfolactate sulfo-lyase (SuyAB) [EC 4.4.1.24]. Inducible reduction of 3-sulfopyruvate, inducible SuyAB activity and induction of an unknown protein were detected. Separation of the soluble proteins from induced cells on an anion-exchange column yielded four relevant fractions. Two different fractions reduced sulfopyruvate with NAD(P)H, a third yielded SuyAB activity, and the fourth contained the unknown protein. The latter was identified by peptide-mass fingerprinting as SlcH, the candidate periplasmic binding protein of the transport system. Separated SuyB was also identified by peptide-mass fingerprinting. ComC was partially purified and identified by peptide-mass fingerprinting. The (R)-sulfolactate that ComC produced from sulfopyruvate was a substrate for SuyAB, which showed that SuyAB is (R)-sulfolactate sulfo-lyase. SlcC was purified to homogeneity. This enzyme also formed sulfolactate from sulfopyruvate, but the latter enantiomer was not a substrate for SuyAB. SlcC was obviously ( S)-sulfolactate dehydrogenase.	2009
1	15758220	Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA Ulrike Rein , Ronnie Gueta , Karin Denger , Jürgen Ruff , Klaus Hollemeyer , Alasdair M Cook	Paracoccus pantotrophus NKNCYSA utilizes (R)-cysteate (2-amino-3-sulfopropionate) as a sole source of carbon and energy for growth, with either nitrate or molecular oxygen as terminal electron acceptor, and the specific utilization rate of cysteate is about 2 mkat (kg protein)(-1). The initial degradative reaction is catalysed by an (R)-cysteate : 2-oxoglutarate aminotransferase, which yields 3-sulfopyruvate. The latter was reduced to 3-sulfolactate by an NAD-linked sulfolactate dehydrogenase [3.3 mkat (kg protein)(-1)]. The inducible desulfonation reaction was not detected initially in cell extracts. However, a strongly induced protein with subunits of 8 kDa (alpha) and 42 kDa (beta) was found and purified. The corresponding genes had similarities to those encoding altronate dehydratases, which often require iron for activity. The purified enzyme could then be shown to convert 3-sulfolactate to sulfite and pyruvate and it was termed sulfolactate sulfo-lyase (Suy). A high level of sulfite dehydrogenase was also induced during growth with cysteate, and the organism excreted sulfate. A putative regulator, OrfR, was encoded upstream of suyAB on the reverse strand. Downstream of suyAB was suyZ, which was cotranscribed with suyB. The gene, an allele of tauZ, encoded a putative membrane protein with transmembrane helices (COG2855), and is a candidate to encode the sulfate exporter needed to maintain homeostasis during desulfonation. suyAB-like genes are widespread in sequenced genomes and environmental samples where, in contrast to the current annotation, several presumably encode the desulfonation of 3-sulfolactate, a component of bacterial spores.	2005

Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K., and Cook, A.M. (2005) Dissimilation of cysteate via 3‐sulfolactate sulfo‐lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151: 737–747.