References
1) Light, A., and Janska, H., 1989. Enterokinase (Enteropeptidase): comparative aspects. Trends in Biochemical Sciences 14: 110-112.
2) Lu, D., et al., 1999. Crystal Structure of Enteropeptidase Light Chain Complexed with an Analog of the Trypsinogen Activation Peptide. Journal of Molecular Biology 292: 361-373.
3) Light, A., and Fonseca, P., 1984. The Preparation and Properties of the Catalytic Subunit of Bovine Enterokinase. The Journal of Biological Chemistry 259: 13195-13198.
4) Chen, J., et al., 2003. Evolution of Trypsinogen Activation Peptides. Molecular Biology and Evolution 20: 1767-1777.
5) Hedstrom, E., 2002. Serine Protease Mechanism and Specificity. Chemical Reviews 102: 4501-4523.
6) Gasteiger, E., et al., 2005. Protein identification and analysis tools on the ExPASy server. The Proteonomics Protocol Handbook: 571-607.
7) Holzinger, A., et al., 2002. Mutations in the Proenteropeptidase Gene Are the Molecular Causes of Congenital Enteropeptidase Deficiency. The American Journal of Human Genetics 70: 20-25.
8) Mikhailova, A., and Rumsh, L., 2000. Enteropeptidase: Structure, Function, and Appplication in Biotechnology. Applied Biochemistry and Biotechnology 88: 159-174
9) Friedrich, R., et al., 2002. Catalytic Domain Structures of MT-SP1/Matripase, a Matrix- degrading Transmembrane Serine Proteinase. The Journal of Biological Chemistry 277: 2160-2168.
10) Altschul, S., et al., 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Research 25: 3389-3402.
11) Holm, L., and Rosenstro?m, P., 2010. Dali server: conservation mapping in 3D. Nucleic Acids Research 38: 545-549.
12) Wikipedia, the Free Encyclopedia. 2013. Serine protease mechanism.