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Amino acid sequences of ovomucoid third domains from 27 additional species of birds

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Abstract

Ovomucoids consist of a single polypeptide chain which is composed of three tandem Kazal domains. Each Kazal domain is an actual or putative protein inhibitor of serine proteinases. Ovomucoid third domains were already isolated and sequenced from 126 species of birds (Laskowskiet al., 1987, 1990). This paper adds 27 new species. A number of generalizations are made on the basis of sequences from 153 species. The residues that are in contact with the enzyme in enzyme-inhibitor complexes are strikingly hypervariable. While the primary specificity residue,P 1, is the most variable; substitutions occur predominantly among aliphatic, hydrophobic residues. Consensus sequences for an avian ovomucoid third domain, for a b-type Kazal domain (i.e., a COOH terminal domain of multidomain inhibitors) and for a general Kazal domain are given. Finally, the individual new sequences are briefly discussed.

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Author notes

  1. Izydor Apostol

    Present address: Somatogen, Inc., 5797 Central Ave., 80301, Boulder, Colorado

  2. Tomoko Komiyama

    Present address: Department of Pathology, Duke University Medical Center, 27710, Durham, North Carolina

Authors and Affiliations

  1. Department of Chemistry, Purdue University, 47907, West Lafayette, Indiana

    Izydor Apostol, Anthony Giletto, Tomoko Komiyama, WenLei Zhang & Michael Laskowski Jr.

Authors
  1. Izydor Apostol
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  2. Anthony Giletto
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  3. Tomoko Komiyama
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  4. WenLei Zhang
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  5. Michael Laskowski Jr.
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Apostol, I., Giletto, A., Komiyama, T. et al. Amino acid sequences of ovomucoid third domains from 27 additional species of birds. J Protein Chem 12, 419–433 (1993). https://doi.org/10.1007/BF01025042

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