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...

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Veröffentlicht in:European journal of biochemistry 1990-08, Vol.192 (1), p.161-166
Hauptverfasser: Hupperich, M, Henschen, A, Eggerer, H
Format: Artikel
Sprache:eng
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Zusammenfassung: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)
ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1990.tb19209.x