Open AccessPrimary structure of porcine heart citrate synthase.
Author(s) -
David P. Bloxham,
David C. Parmelee,
Santosh Kumar,
Roger D. Wade,
Lowell H. Ericsson,
Hans Neurath,
Kenneth A. Walsh,
Koiti Titani
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.9.5381
Subject(s) - cyanogen bromide , citrate synthase , chemistry , biochemistry , cleavage (geology) , proteolysis , trypsin , protein primary structure , atp citrate lyase , peptide sequence , enzyme , lyase , peptide , peptide bond , chymotrypsin , amino acid , stereochemistry , biology , paleontology , fracture (geology) , gene
The sequence of 437 amino acid residues of porcine heart citrate synthase [citrate oxaloacetate-lyase (pro-3S-CH2COO leads to acetyl-CoA), EC 4. 1. 3. 7] has been determined by the alignment of fragments generated by cleavage with cyanogen bromide and with trypsin. Isolation of the peptides was facilitated by recent developments in the high-performance liquid chromatography of peptide mixtures. The alignment of these peptides was consistent with that previously deduced from fragments derived by restricted cleavage of citrate synthase by limited proteolysis and cleavage of aspartyl-prolyl bonds and asparaginyl-glycyl bonds. The enzyme contains a modified amino acid, trimethyllysine, at residue 368, showing that the enzyme is subjected to post-translational modification.