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Human kallikrein 6 (protease M/zyme/neurosin) is a serine protease that has been suggested to be a serum biomarker for ovarian cancer and may also be involved in pathologies of the CNS. The precursor form of human kallikrein 6 (proh-K6) was overexpressed in  Pichia pastoris  and found to be autoprocessed to an active but unstable mature enzyme that subsequently yielded the inactive, self-cleavage product, hK6 (D[81]K[244]). Site-directed mutagenesis was used to investigate the basis for the intrinsic catalytic activity and the activation mechanism of pro-hK6. A single substitution R[80]-&gt;Q stabilized the activity of the mature enzyme, while substitution of the active site serine (S[197]-&gt;A) resulted in complete loss of hK6 proteolytic activity and facilitated protein production. Our data suggest that the enzymatic activity of hK6 is regulated by an autoactivation/autoinactivation mechanism. Mature hK6 displayed a trypsin-like activity against synthetic substrates and human plasminogen was identified as a putative physiological substrate for hK6, as specific cleavage at the plasminogen internal bond S[460]-V[461] resulted in the generation of angiostatin, an endogenous inhibitor of angiogenesis and metastatic growth.

Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation