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1: Biochem J. 1988 Feb 1;249(3):779-88.Click here to read Links

The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.

Freemont PS, Dunbar B, Fothergill-Gilmore LA.

Department of Biochemistry, University of Aberdeen, Marischal College, U.K.

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].

PMID: 3355497 [PubMed - indexed for MEDLINE]

PMCID: PMC1148774