Disease relevance of serC

• These results lead to the conclusion that serC is directly involved in B6 biosynthesis in E. coli, but not in B. subtilis [1].
• The possible involvement of serC in vitamin B6 (B6) biosynthesis in Bacillus subtilis was investigated and compared with that in Escherichia coli [1].

High impact information on serC

• The M. maripaludis homolog complemented a serC mutation in the Escherichia coli phosphoserine aminotransferase [2].
• The arrangement of the Escherichia coli serC (pdxF) and aroA genes into a cotranscribed multifunctional operon allows coregulation of two enzymes required for the biosynthesis of L-serine, pyridoxal 5'-phosphate, chorismate, and the aromatic amino acids and vitamins [3].
• Maximization of transcription of the serC (pdxF)-aroA multifunctional operon by antagonistic effects of the cyclic AMP (cAMP) receptor protein-cAMP complex and Lrp global regulators of Escherichia coli K-12 [3].
• The serC and aroA open reading frames contain 362 and 428 codons, respectively, and the deduced amino acid sequences share 78% and 81% homology, respectively, with the corresponding E. coli genes [4].
• 3-hydroxypyruvate substitutes for pyridoxine in serC mutants of Escherichia coli K-12 [5].

Chemical compound and disease context of serC

• However, the serC-disrupted E. coli mutant grown in a minimal medium supplemented with L-serine and GA synthesized B6 at a level less than 20% of that synthesized by the wild type [1].
• In contrast to E. coli, the serC-disrupted B. subtilis mutant required L-serine or glycine for growth, but did not require PN [1].

Biological context of serC

• Escherichia coli K-12 mutants with serC genotype required pyridoxine and serine for normal growth, as do E. coli B mutants of this type [5].
• The most probable gene order is serC-rpsA-cmlB [6].

Associations of serC with chemical compounds

• Some tetracycline-sensitive mutants of aroA554::Tn10 strains required serine and pyridoxine, indicating loss of serC function, and some that were found to be SerC- did not produce gas from glucose, indicating a loss of pfl function [7].
• Mutants of the K-12 strain, however, reverted easily to pyridoxine independence without regaining activity in the 3-phosphoserine oxoglutarate transaminase coded for by the serC gene [5].

References