Amino acid sequence around the active site of two class I fructose-1,6-bisphosphate aldolases from staphylococci.
The amino acid sequences of a 26-residue segment containing the active-site lysyl residue of the class I fructose-1,6-bisphosphate aldolases from Staphylococcus aureus and Staphylococcus epidermidis have been determined. The sequence homology within the active sites between these enzymes and those from several eucaryotic class I aldolases showed a maximum of 21%. The similarity may indicate the origin of both procaryotic and eucaryotic class I aldolases from a common ancestor.
D000595:Amino Acid Sequence; D001665:Binding Sites; D005634:Fructose-Bisphosphate Aldolase / Q000302:isolation & purification / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D013210:Staphylococcus / Q000201:enzymology*; D013211:Staphylococcus aureus / Q000201:enzymology*; D014357:Trypsin
D010446:Peptide Fragments; D014357:Trypsin; D005634:Fructose-Bisphosphate Aldolase