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Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases

Nature volume 307, pages 555–558 (1984)Cite this article

Abstract

Tonin1, an ester protease isolated from rat sub maxillary gland, is a serine protease with trypsin-and chymotrypsin-like activity. The substrate specificity of tonin shows that it differs from kallikreins and is definitely not a renin-like enzyme or an angiotensin-converting enzyme2. Tonin can produce directly the vasoactive peptide angiotensin II, from angiotensin I, angiotensinogen and the synthetic tetradecapeptide substrate of renin by cleavage of a Phe-His bond. It has also been found to cleave some Phe and Arg bonds in various substrates such as β-lipotropin (β-LPH), adrenocorticotropin (ACTH), proopiomelanocortin (POMC)3 and substance P4. Here we describe the complete amino acid sequence of rat submaxillary gland, tonin. Comparison of the sequence of 219 amino acids with other serine proteases, particularly kallikreins, γ-subunit of nerve growth factor (NGF) and the recently described γ-renin, reveals extensive similarities. More interestingly, it also reveals the substitution of an Asp residue always found in the serine protease active site triad (Asp, His, Ser) by a Leu residue. This unusual substitution does not seem to affect the proteolytic activity of the enzyme.

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Authors and Affiliations

  1. Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal, Canada, H2W 1R7

    Claude Lazure, Richard Leduc, Nabil G. Seidah, Gaétan Thibault, Jacques Genest & Michel Chrétien

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  1. Claude Lazure
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  2. Richard Leduc
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  3. Nabil G. Seidah
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  4. Gaétan Thibault
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  5. Jacques Genest
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  6. Michel Chrétien
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Lazure, C., Leduc, R., Seidah, N. et al. Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases. Nature 307, 555–558 (1984). https://doi.org/10.1038/307555a0

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