Disease relevance of cysE

• When a tnaA-disrupted E. coli strain expressing the altered cysE gene was transformed with a plasmid carrying the bcr gene, the transformant exhibited more L-cysteine production than cells carrying the vector only [1].

High impact information on cysE

• T. vaginalis appears to lack serine acetyltransferase, the source of O-acetylserine in many cells, but has a functional 3-phosphoglycerate dehydrogenase and an O-phosphoserine aminotransferase that together result in the production of O-phosphoserine, suggesting that this is the physiological substrate [2].
• In contrast, the growth of an DeltayrhA mutant or a luxS mutant, inactivated for the S-ribosyl-homocysteinase step of the S-adenosylmethionine recycling pathway, was strongly reduced with methionine, whereas a DeltayrhA DeltacysK or cysE mutant did not grow at all under the same conditions [3].
• We previously found a marked production of L-cysteine from glucose in recombinant Escherichia coli cells expressing an altered cysE gene encoding feedback inhibition-insensitive serine acetyltransferase [1].
• To increase the cysteine content of the commercial potato cultivar White Lady the chimeric SAT-coding cysE gene from Escherichia coli under the control of the constitutive CaMV 35S promoter and fused to the chloroplast targeting rbcS 5'-transit peptide sequence was introduced into the White Lady genome [4].
• Cysteine is synthesised from O-acetyl-l-serine formed by serine acetyltransferase (SAT) [4].

Biological context of cysE

• OASS-B did not form a complex with E. coli serine acetyltransferase (SAT, EC 2.3.1.30) and showed a wide range of substrate specificity in nonproteinaceous amino acid synthesis [5].

References