Amino-Acid Sequence of Citrate-Lyase Acyl-Carrier Protein from Klebsiella aerogenes

The complete amino-acid sequence of the acyl carrier protein of citrate lyase from Klebsiella aerogenes (ATCC 13882) was determined by automated sequential Edman degrad degradations of the protein and of peptides in a liquid-phase sequencer of Edman and a solid-phase sequencer of laursen. The sequence composed of 78 resideues does not contain tyrosine of histidine restidine resideues. The primary structure has been established as Met-Glu-Met-Lys-Ile-Asp-Ala-Leu-Ala-Gly-Thr-Leu-Glu- Ser-Ser-AsP-Val-Met-Val-Arg-Ile-Gly-Pro-Ala-Ala-Gln-Pro-Gly-Ile-Gln-Leu-Ile-Asp Ser-Ile-Val-Lys-Gln-Glu-Phe-Gly-Ala-Ile-Gln-Gln-Val-Arg-Glu-Thr-Leu-Ala-Gln- Leu-Gly-Val-Lys-Glu-Cys-Asp-Asn-Val-Gln-Leu-Ala-Arg-Val-Gln-Ala-Ala-Leu-Arg-Trp-Gln-Gln. The molecular weight of the acyl carrier protein calculated from the amino acid sequence and the phosphoribosyl dephospho-CoA prostheitic group is 9378. This prostheitc group is bound in phosphodiester linkage to serine-14 of the acyl carrier protein. Circular dichroism measurements indicate that citrate lyase acyl carrier protein has a high degree of α-helical structure. In this respect and in molecular size the acyl carrier protein from citrate lyase resmbles the acyl carrier protein from Escherichia coli acid syntetase. However, wit exception of two very short sequences the mino acid sequences of these two proteins are completely different.