Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases
Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases
复制标题
大鼠颌下肌张力的氨基酸序列揭示了与丝氨酸蛋白酶的相似性
作者:
C. Lazure;R. Leduc;N. Seidah;G. Thibault;J. Genest;M. Chrétien
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.
DOI:
--
发表时间:
1981
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Thomas,KA;Baglan,NC;Bradshaw,RA
通讯作者:
Bradshaw,RA
影响因子:
3.9
作者:
Schenkein,I;Franklin,EC;Frangione,B
通讯作者:
Frangione,B