Mouse kallikrein arginyl-esteropeptidase genes: analysis of cloned cDNAs suggests rapid functional divergence from a common ancestral sequence.
A previously-cloned cDNA coding for a member of the kallikrein arginyl-esteropeptidase group of serine proteases, (pMK-1), was used as a hybridization probe to identify a second partial cDNA clone (pMK-2) from mouse submaxillary gland. pMK-2 shares more than a 98% nucleotide sequence homology with pMK-1; the 3' untranslated regions are identical and there are only two predicted amino acid changes over the C-terminal 66 amino acids. The site of one change is implicated in determining substrate specificity, while the other may affect the catalytic mechanism. Thus despite the marked similarity of pMK-1 and pMK-2, the differences probably give rise to functionally distinct enzymes and are not simply polymorphic alleles.
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000378:metabolism; D001483:Base Sequence; D005075:Biological Evolution; D004247:DNA / Q000235:genetics; D005796:Genes; D007610:Kallikreins / Q000235:genetics*; D051379:Mice; D013363:Submandibular Gland / Q000201:enzymology; D013379:Substrate Specificity
D004247:DNA; D001120:Arginine; D007610:Kallikreins