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. 2018 Nov 27;9:2838. doi: 10.3389/fmicb.2018.02838

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Copyright © 2018 VanDrisse and Escalante-Semerena.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Pathway for biosynthesis of L-Cys in Salmonella enterica. Sulfate is sequestered by the sulfate-binding protein (sbp) and uptake is mediated by the CysUWA sulfate/thiosulfate transporter. The ATP sulfurylase [CysD (catalytic subunit)/CysN (GTP-binding subunit), EC 2.7.7.4] activates sulfate to adenosine 5′-phosphate (APS), which is a substrate for APS kinase (CysC, EC 2.7.1.25). 3-phosphoadenosine 5′-phosphosulfate (PAPS) is reduced to sulfite by the PAPS reductase (CysH, EC 1.8.4.8) and sulfite is reduced to sulfide by a NADPH-sulfite reductase (CysJI, EC 1.8.1.2). A serine acetyltransferase (CysE, EC 2.3.1.30) produces OAS from L-Ser and AcCoA. OAS and sulfide are then substrates for cysteine synthase (CysK, EC 2.5.1.47), which produces L-Cys. Transcription of cysJIH and cysK is upregulated upon binding of CysB and acetyl-serine.