Nepentezin
| Nepentezin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.23.12 | ||||||||
| CAS broj | 9073-80-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Nepentezin (EC 3.4.23.12, nepentesna aspartička proteinaza, nepentesno kiselinska proteinaza, nepentacin, nepentazin, aspartilna endopeptidaza) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Specifičnost je slična pepsinu, ali dodatno se razlažu veze na obe strane ostatka Asp i u Lys-Arg
Ovaj enzim je prisutan u biljkama Nepenthes spp. i Drosera peltata.
Reference
- ↑ Amagase, S., Nakayama, S. and Tsugita, A. (1969). „Acid protease in Nepenthes. II. Study on the specificty of nepenthesin”. J. Biochem. (Tokyo) 66: 431-439. PMID 5354017.
- ↑ Garg, G.K. and Virupaksha, T.K. (1970). „Acid protease from germinated sorghum. 2. Substrate specificity with synthetic peptides and ribonuclease A”. Eur. J. Biochem. 17: 4-12. PMID 5486576.
- ↑ Shinano, S. and Fukushima, K. (1971). „Studies on lotus seed protease. Part III. Some physicochemical and enzymic properties”. Agric. Biol. Chem. 35: 1488-1494.
- ↑ Amagase, S. (1972). „Digestive enzymes in insectivorous plants. III. Acid proteases in the genus Nepenthes and Drosera peltata”. J. Biochem. (Tokyo) 72: 73-81. PMID 5069751.
- ↑ Takahashi, K., Chang, W-J. and Ko, J-S. (1974). „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: 897-899. PMID 4436292.
- ↑ Tökés, Z.A., Woon, W.C. and Chambers, S.M. (1974). „Digestive enzymes secreted by the carnivorous plant Nepenthes macferlani L”. Planta 119: 39-46. PMID 16526095.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Nepenthesin
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
