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Acrosin, the peculiar sperm-specific serine protease
Hum Genet (1991) 87:635-641
9 Springer-Verlag 1991
Review article
Acrosin, the peculiar sperm-specific serine protease
Uwe Klemm I, Werner Miiller-Esterl 2, and Wolfgang Engel 1
l Institut for Humangenetik der Universitfit, Gosslerstrasse 12d, W-3400 G6ttingen, Federal Republic of Germany
2Institut for Physiologische Chemie und Pathobiochemie der Universit~it, Duesbergweg 6, W-6500 Mainz, Federal Republic of Germany
Received January 8, 1991 / Revised April 10, 1991
Summary. The sperm enzyme acrosin has long been
known as one of the key enzymes in the mammalian fer-
tilization process. Elucidation of primary structures of
preproacrosin from various species have allowed a deeper
insight into the structural organization and the complex
evolution of the sperm proteinase acrosin. In addition to
the typical elements of serine proteases, the acrosin mol-
ecule possesses one novel domain that might convey
DNA-binding properties.
Introduction
The long history of the study of proteolytic enzymes of
the sperm cell was initiated in 1935 by a report of Yamane
(Yamane 1935), describing the solubilizing effect of rab-
bit sperm extracts on the outer investments of oocytes.
These findings stimulated the isolation and purification
of sperm enzymes in the following decades. Many inves-
tigators focused on the major component of the ac-
rosomal content, a trypsin-like enzyme called acrosin
(EC 3.4.21.10) (Zaneveld et al. 1971). Following de-
tailed analysis with natural and artifical substrates and
inhibitors (Stambaugh and Buckley 1968), acrosin was
classified as a member of the serine protease superfam-
ily. This classification was supported by limited amino
acid sequence information from boar (Fock-Ntizel et al.
1980, 1984) and goat acrosin (Hardy et al. 1989) ob-
tained by the classical Edmann degradation method.
Using the methods of recombinant DNA technology,
difficulties in protein sequencing were bypassed and the
primary structures for huma
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