Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit.
The primary structure of the beta-subunit (acyl lyase subunit) of citrate lyase from Klebsiella pneumoniae (ATCC 13,882) was determined with protein chemical methods. The polypeptide chain consists of 289 amino acid residues and has a molecular mass of 31,352 Da. The two half-cystine residues of the subunit are present as cysteines and not involved in disulfide bridges. The sequence shows no homology to known sequences of proteins or nucleic acids and reads (sequence; see text)
Institut für Physiologische Chemie, Technischen Universität München, Federal Republic of Germany.
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Hupperich
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Henschen
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Eggerer
D000595:Amino Acid Sequence; D003488:Cyanogen Bromide / Q000378:metabolism; D004220:Disulfides; D010450:Endopeptidases / Q000378:metabolism; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes; D007652:Oxo-Acid-Lyases; D010449:Peptide Mapping; D010455:Peptides / Q000302:isolation & purification / Q000378:metabolism; D013438:Sulfhydryl Compounds; D014357:Trypsin / Q000378:metabolism
D004220:Disulfides; D009097:Multienzyme Complexes; D010455:Peptides; D013438:Sulfhydryl Compounds; D010450:Endopeptidases; D014357:Trypsin; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase; D007652:Oxo-Acid-Lyases; C019909:citrate (pro-3S)-lyase; D003488:Cyanogen Bromide