Leucilna aminopeptidaza
| Leucilna aminopeptidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.11.1 | ||||||||
| CAS broj | 9001-61-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Leucilna aminopeptidaza (EC 3.4.11.1, leucinska aminopeptidaza, leucilna peptidaza, peptidaza S, citozolna aminopeptidaza, katepsin III, L-leucinska aminopeptidaza, leucinaminopeptidaza, leucinamidna aminopeptidaza, FTBL protein, proteinska FTBL, aminopeptidaza II, aminopeptidaza III) je enzim.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Oslobađanje N-terminalnih aminokiselina, Xaa-Yaa-, gde je Xaa preferentno Leu, mada može da bude druga aminokiselina uključujući Pro. Ne može da bude Arg ili Lys. Yaa može da bude Pro. Amidi aminokiselina i metil estri se takođe lako hidrolizuju. Brzine hidrolize arilamida su veoma male
Ovaj cinkov enzim je izolovan iz bubega svinja i sočiva goveda.
Reference
- ↑ Himmelhoch, S.R. (1970). „Leucine aminopeptidase from swine kidney”. Methods Enzymol. 19: 508-513.
- ↑ Delange, R.J. and Smith, E.L. (1971). „Leucine aminopeptidase and other N-terminal exopeptidases”. u: Boyer, P.D.. The Enzymes. 3 (3rd izd.). New York: Academic Press. str. 81-118.
- ↑ van Loon-Klaasen, L.A.H., Cuypers, H.T., van Westreenen, H., de Jong, W.W. and Bloemendal, H. (1980). „The primary structure of bovine lens leucine aminopeptidase. Complete amino acid sequence of the N-terminal cyanogen bromide fragment and site limited tryptic digestion”. Biochem. Biophys. Res. Commun. 95: 334-341. PMID 7417261.
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.
- Delange, R.J. and Smith, E.L. (1971). „Leucine aminopeptidase and other N-terminal exopeptidases”. u: Boyer, P.D.. The Enzymes. 3 (3rd izd.). New York: Academic Press. str. 81-118.
Spoljašnje veze
- MeSH Leucyl+aminopeptidase
- 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
