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

Biochem J. 1988 Feb 1;249(3):779-88. doi: 10.1042/bj2490779.

Abstract

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].

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biological Evolution
  • Chromatography, High Pressure Liquid
  • Fructose-Bisphosphate Aldolase*
  • Humans
  • Molecular Sequence Data
  • Muscles / enzymology*
  • Peptide Fragments / analysis
  • Trypsin

Substances

  • Peptide Fragments
  • Trypsin
  • Fructose-Bisphosphate Aldolase