The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.
The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase, comprising 363 residues, was determined. The sequence was deduced by automated sequencing of CNBr-cleavage, o-iodosobenzoic acid-cleavage, trypsin-digest and staphylococcal-proteinase-digest fragments. Comparison of the sequence with other class I aldolase sequences shows that the mammalian muscle isoenzyme is one of the most highly conserved enzymes known, with only about 2% of the residues changing per 100 million years. Non-mammalian aldolases appear to be evolving at the same rate as other glycolytic enzymes, with about 4% of the residues changing per 100 million years. Secondary-structure predictions are analysed in an accompanying paper [Sawyer, Fothergill-Gilmore & Freemont (1988) Biochem. J. 249, 789-793].
Freemont
P S
PS
Department of Biochemistry, University of Aberdeen, Marischal College, U.K.
Dunbar
B
B
Fothergill-Gilmore
L A
LA
D000595:Amino Acid Sequence; D005075:Biological Evolution; D002851:Chromatography, High Pressure Liquid; D005634:Fructose-Bisphosphate Aldolase; D006801:Humans; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D010446:Peptide Fragments; D014357:Trypsin; D005634:Fructose-Bisphosphate Aldolase