Typically, protein spatial structures are more conserved in evolution than amino acid
sequences. However, the recent explosion of sequence and structure information …

The last general review of the aspartic peptidase family was by David R. Davies in 1990. 1
Since then, several reviews on selected aspects of the structure and function of aspartic …

Proteolytic enzymes are intricately involved in many aspects of plant physiology and
development. On the one hand, they are necessary for protein turnover. Degradation of …

Aspartic proteinases of the A1 family are widely distributed among plant species and have
been purified from a variety of tissues. They are most active at acidic pH, are specifically …

Proteases occupy the most relevant position among industrial enzymes. Plant proteases
have been used in medicine, detergent manufacturing, and food science for many years, but …

SAPLIPs (saposin-like proteins) are a diverse family of lipid-interacting proteins that have
various and only partly understood, but nevertheless essential, cellular functions. Their …

The effect of three milk pH values, 6.0, 6.3 and 6.7, on gelation properties was monitored by
small amplitude oscillatory rheology as well as a large deformation (yield) test for gels …

The sequence of the Arabidopsis genome has given us information about one plant's
complement of aspartic proteinases. Using an in silico analysis based on the homology to …

Aspartic proteinases (AP) play major roles in physiologic and pathologic scenarios in a wide
range of organisms from vertebrates to plants or viruses. The present work deals with the …

Carnivorous plants acquire significant amounts of nitrogen from insects. The tropical
carnivorous plant Nepenthes accumulates acidic fluid containing aspartic proteinase (AP) in …