A mutation in Escherichia coli K-12 results in a requirement for thiamine and a decrease in L-serine deaminase activity.
Mutants of Escherichia coli K-12 deficient in L-serine deaminase (L-SD) activity have been isolated. These strains required thiamine and grew normally when it was provided. The decrease in L-SD activity caused no obvious metabolic deficiency. A study of revertants and transductants showed that a single mutation was responsible for the thiamine requirement and for the decrease in L-SD activity.
D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D005998:Glycine / Q000378:metabolism; D012695:L-Serine Dehydratase / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid; D012694:Serine / Q000378:metabolism; D013831:Thiamine / Q000502:physiology*; D014161:Transduction, Genetic; D001616:beta-Galactosidase / Q000096:biosynthesis
D011773:Pyruvates; D012694:Serine; D019289:Pyruvic Acid; D001616:beta-Galactosidase; D012695:L-Serine Dehydratase; D007930:Leucine; D005998:Glycine; D013831:Thiamine