| EC |
3.4.23.12 |
| Accepted name: |
nepenthesin |
| Reaction: |
Similar to pepsin, but also cleaves on either side of Asp and at Lys┼Arg |
| Other name(s): |
Nepenthes aspartic proteinase; Nepenthes acid proteinase; nepenthacin; nepenthasin; aspartyl endopeptidase |
| Comments: |
From the insectivorous plants Nepenthes spp. (secretions) and Drosera peltata (ground-up leaves). Aspartic endopeptidases are probably present in many other plants, including Lotus [3] and sorghum [2]. In peptidase family A1 (pepsin A family) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9073-80-7 |
| References: |
| 1. |
Amagase, S., Nakayama, S. and Tsugita, A. Acid protease in Nepenthes. II. Study on the specificty of nepenthesin. J. Biochem. (Tokyo) 66 (1969) 431–439. [PMID: 5354017] |
| 2. |
Garg, G.K. and Virupaksha, T.K. Acid protease from germinated sorghum. 2. Substrate specificity with synthetic peptides and ribonuclease A. Eur. J. Biochem. 17 (1970) 4–12. [DOI] [PMID: 5486576] |
| 3. |
Shinano, S. and Fukushima, K. Studies on lotus seed protease. Part III. Some physicochemical and enzymic properties. Agric. Biol. Chem. 35 (1971) 1488–1494. |
| 4. |
Amagase, S. Digestive enzymes in insectivorous plants. III. Acid proteases in the genus Nepenthes and Drosera peltata. J. Biochem. (Tokyo) 72 (1972) 73–81. [PMID: 5069751] |
| 5. |
Takahashi, K., Chang, W-J. and Ko, J-S. Specific inhibition of acid proteases from brain, kidney, skeletal muscle, and insectivorous plants by diazoacetyl-DL-norleucine methyl ester and by pepstatin. J. Biochem. (Tokyo) 76 (1974) 897–899. [PMID: 4436292] |
| 6. |
Tökés, Z.A., Woon, W.C. and Chambers, S.M. Digestive enzymes secreted by the carnivorous plant Nepenthes macferlani L. Planta 119 (1974) 39–46. [DOI] [PMID: 16526095] |
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| [EC 3.4.23.12 created 1972 as EC 3.4.99.4, transferred 1978 to EC 3.4.23.12, modified 1981] |
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