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Phylogeny of metabolic pathways: O ‐acetylserine sulphydrylase A is homologous to the tryptophan synthase beta subunit
Author(s) -
Levy S.,
Danchinl A.
Publication year - 1988
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1988.tb00089.x
Subject(s) - tryptophan synthase , biology , gene , peptide sequence , biochemistry , nucleic acid sequence , protein subunit , atp synthase , enzyme , genetics , amino acid , escherichia coli , structural gene , sequence (biology)
Summary The cysK gene of Escherichia coli K‐12 encoding O ‐acetylserine sulphydrylase A, was cloned and its nucleotide sequence, together with that of the flanking regions, was determined. The deduced amino acid sequence of the carboxy‐terminal moiety of O ‐acetylserine sulphydrylase A shows significant similarity to the amino acid sequence of tryptophan synthase beta chain from several organisms. This sequence similarity is likely to reflect the structural homologies of substrates shared by both enzymes. This may indicate that these proteins, although catalysing different reactions in different metabolic pathways, have evolved from a common ancestral gene.