Phytepsin |
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Identifiers |
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EC no. | 3.4.23.40 |
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CAS no. | 219715-98-7 |
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Databases |
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IntEnz | IntEnz view |
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BRENDA | BRENDA entry |
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ExPASy | NiceZyme view |
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KEGG | KEGG entry |
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MetaCyc | metabolic pathway |
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PRIAM | profile |
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PDB structures | RCSB PDB PDBe PDBsum |
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Search |
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PMC | articles |
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PubMed | articles |
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NCBI | proteins |
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Phytepsin |
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Identifiers |
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Symbol | phytepsin |
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InterPro | IPR033869 |
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CDD | cd06098 |
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Phytepsin (EC 3.4.23.40) 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.
References
- ^ Runeberg-Roos P, Törmäkangas K, Ostman A (December 1991). "Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D". European Journal of Biochemistry. 202 (3): 1021–7. doi:10.1111/j.1432-1033.1991.tb16465.x. PMID 1722454.
- ^ Kervinen J, Sarkkinen P, Kalkkinen N, Mikola L, Saarma M (March 1993). "Hydrolytic specificity of the barley grain aspartic proteinase". Phytochemistry. 32 (4): 799–803. doi:10.1016/0031-9422(93)85208-9. PMID 7763475.
- ^ Asakura T, Watanabe H, Abe K, Arai S (August 1995). "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. doi:10.1111/j.1432-1033.1995.tb20783.x. PMID 7556174.
- ^ Kervinen J, Törmäkangas K, Runeberg-Roos P, Guruprasad K, Blundell T, Teeri TH (1995). "Structure and possible function of aspartic proteinases in barley and other plants". Advances in Experimental Medicine and Biology. 362: 241–54. doi:10.1007/978-1-4615-1871-6_28. ISBN 978-1-4613-5761-2. PMID 8540324.
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