L-treonin 3-dehidrogenaza
| L-treonin 3-dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.1.1.103 | ||||||||
| CAS broj | 9067-99-6 | ||||||||
| 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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L-treonin 3-dehidrogenaza (EC 1.1.1.103, L-treoninska dehidrogenaza, treoninska 3-dehidrogenaza, treoninska dehidrogenaza, TDH) je enzim sa sistematskim imenom L-treonin:NAD+ oksidoreduktaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-treonin + NAD+ L-2-amino-3-oksobutanoat + NADH + H+
L-treoninska 3-dehidrogenaza deluje zajedno sa EC 2.3.1.29, glicinskom C-acetiltransferazom, u degradaciji treonina do glicina. Ovaj put treoninske degradacije je uobičajen za prokariotske i eukariotske ćelije. Ova dva enzima formiraju kompleks. U vodenom rastvoru se produkt, L-2-amino-3-oksobutanoat, može spontano dekarboksilisati, čime se formira aminoaceton.
Reference
- ↑ Green, M.L. and Elliott, W.H. (1964). „The enzymic formation of aminoacetone from threonine and its further metabolism”. Biochem. J. 92: 537-549. PMID 4284408.
- ↑ Hartshorne, D. and Greenberg, D.M. (1964). „Studies on liver threonine dehydrogenase”. Arch. Biochem. Biophys. 105: 173-178. PMID 14165492.
- ↑ Newman, E.B., Kapoor, V. and Potter, R. (1976). „Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli”. J. Bacteriol. 126: 1245-1249. PMID 7548.
- ↑ Epperly, B.R. and Dekker, E.E. (1991). „L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies”. J. Biol. Chem. 266: 6086-6092. PMID 2007567.
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 L-threonine+3-dehydrogenase
- 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
