Acrosin, the peculiar sperm-specific serine protease
✍ Scribed by Uwe Klemm; Werner Müller-Esterl; Wolfgang Engel
- Book ID
- 104661272
- Publisher
- Springer
- Year
- 1991
- Tongue
- English
- Weight
- 772 KB
- Volume
- 87
- Category
- Article
- ISSN
- 0340-6717
No coin nor oath required. For personal study only.
✦ Synopsis
The sperm enzyme acrosin has long been known as one of the key enzymes in the mammalian fertilization 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 molecule possesses one novel domain that might convey DNA-binding properties.
📜 SIMILAR VOLUMES
## Abstract BSp120 and BSp66 are trypsin‐like serine proteases from bovine spermatozoa. The former is active in cryopreserved sperm samples while the latter shows proteolytic activity in recently obtained fresh sperm. Both proteases are immunologically related and co‐localize in the apical portion
Conservation of clusters of buried water molecules is a structural motif present throughout the serine protease family. Frequently, these clusters are shaped as water channels forming extensive hydrogen-bonding networks linked to the protein backbone. The most conspicuous example is the water channe