Aromatična-L-aminokiselinska dekarboksilaza
| Aromatična-L-aminokiselinska dekarboksilaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 4.1.1.28 | ||||||||
| CAS broj | 9042-64-2 | ||||||||
| 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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Aromatična-L-aminokiselinska dekarboksilaza (EC 4.1.1.28, DOPA dekarboksilaza, triptofanska dekarboksilaza, hidroksitriptofanska dekarboksilaza, L-DOPA dekarboksilaza, aromatična amino kiselinska dekarboksilaza, 5-hidroksitriptofanska dekarboksilaza, aromatična-L-amino-kiselinska karboksi-lijaza (formira triptamin)) je enzim sa sistematskim imenom aromatična-L-aminokiselina karboksi-lijaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) L-dopa dopamin + CO2
- (2) 5-hidroksi-L-triptofan 5-hidroksitriptamin + CO2
Ovaj enzim je piridoksal-fosfatni protein.
Reference
- ↑ Christenson, J.G., Dairman, W. and Udenfriend, S. (1972). „On the identity of DOPA decarboxylase and 5-hydroxytryptophan decarboxylase (immunological titration-aromatic L-amino acid decarboxylase-serotonin-dopamine-norepinephrine)”. Proc. Natl. Acad. Sci. USA 69: 343-347. PMID 4536745.
- ↑ Lovenberg, W., Weissbach, H. and Udenfriend, S. (1962). „Aromatic L-amino acid decarboxylase”. J. Biol. Chem. 237: 89-93. PMID 14466899.
- ↑ McGilvery, R.W. and Cohen, P.P. (1948). „The decarboxylation of L-phenylalanine by Streptococcus faecalis R”. J. Biol. Chem. 174: 813-816.
- ↑ Sekeris, C.E. (1963). „Zur Tyrosinstoffwechsel der Insekten. XII. Reinigung, Eigenschaften und Substratspezifität der DOPA-Decarboxylase”. Hoppe-Seyler's Z. Physiol. Chem. 332: 70-78.
- ↑ Weissbach, H., Bogdanski, D.F., Redfield, B.G. and Udenfriend, S. (1957). „Studies on the effect of vitamin B6 on 5-hydroxytryptamine (serotonin) formation”. J. Biol. Chem. 227: 617-624. PMID 13462983.
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.
Vanjske veze
- MeSH Aromatic-L-amino-acid+decarboxylase
- 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
