Disease relevance of serC

• All six recombinant plasmids which complemented aroA also complemented the serC mutation in E. coli K-12 strain KL282 [1].
• Genes aroA and serC of Salmonella typhimurium constitute an operon [2].
• Genetic analyses by Hfr conjugation and P1 phage transduction indicate that the mutation affecting S1 (rpsA) is located close to the serC gene [20 min on the E. coli genetic map of Bachmann et al. (1976)], with a co-transduction frequency of 61% [3].

High impact information on serC

• Phosphoserine aminotransferase (PSAT; EC 2.6.1.52), a member of subgroup IV of the aminotransferases, catalyses the conversion of 3-phosphohydroxypyruvate to l-phosphoserine [4].
• Evidence is presented which confirms that the aroA and serC genes constitute an operon which has the novel feature of encoding enzymes from two different amino acid biosynthetic pathways [5].
• Both genes are expressed as a polycistronic message which is transcribed from a promotor located 58 bp upstream of serC [5].
• This gene has been identified as serC, the structural gene for 3-phosphoserine aminotransferase, an enzyme of the serine biosynthetic pathway [5].
• The M. maripaludis homolog complemented a serC mutation in the Escherichia coli phosphoserine aminotransferase [6].

Chemical compound and disease context of serC

• The bacterial expression of the cDNA could functionally rescue the auxotrophy of serine in the serC- mutant, Escherichia coli KL282 [7].

Biological context of serC

• Tn5 mutagenesis suggested serC encoding 3-phosphoserine aminotransferase was the proximal gene in an operon with aroA [1].
• Since serine alone was inadequate to provide the nutritional requirement of serC mutants, these mutants must have been unable to synthesize 3-hydroxypyruvate from serine [8].

Associations of serC with chemical compounds

• Chromosomal insertions in serC caused a requirement for pyridoxine, serine, and aromatic compounds, which directly verified that SerC functions in the pyridoxine biosynthetic pathway [9].
• Growth responses of pdxA, pdxB, and serC mutants to beta-hydroxypyruvate, D-alanine, and glycolate could also be reconciled with the proposed pathway [9].
• Both serine and chorismate are precursors of enterochelin; this may be why serC and aroA are in a single operon [2].

References