Phytepsin Explained
| Phytepsin |
| Ec Number: | 3.4.23.40 |
| Cas Number: | 219715-98-7 |
Phytepsin is an enzyme.[1] [2] [3] [4] This enzyme catalyses the following chemical reaction
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-Asp- and -Asp-Asp- bonds in 2S albumin from plant seeds
This enzyme is present in barley grain and other plants. It is an aspartic protease with a plant-specific insert.
Notes and References
- Runeberg-Roos P, Törmäkangas K, Ostman A . Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D . European Journal of Biochemistry . 202 . 3 . 1021–7 . December 1991 . 1722454 . 10.1111/j.1432-1033.1991.tb16465.x . free .
- Kervinen J, Sarkkinen P, Kalkkinen N, Mikola L, Saarma M . Hydrolytic specificity of the barley grain aspartic proteinase . Phytochemistry . 32 . 4 . 799–803 . March 1993 . 7763475 . 10.1016/0031-9422(93)85208-9 .
- Asakura T, Watanabe H, Abe K, Arai S . Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases . European Journal of Biochemistry . 232 . 1 . 77–83 . August 1995 . 7556174 . 10.1111/j.1432-1033.1995.tb20783.x . free .
- Kervinen J, Törmäkangas K, Runeberg-Roos P, Guruprasad K, Blundell T, Teeri TH . Structure and possible function of aspartic proteinases in barley and other plants . 362 . 241–54 . 1995 . 8540324 . 10.1007/978-1-4615-1871-6_28 . 978-1-4613-5761-2 . Advances in Experimental Medicine and Biology .
