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Aromatična-L-aminokiselinska dekarboksilaza
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
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

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

\rightleftharpoons

dopamin + CO₂

(2) 5-hidroksi-L-triptofan

\rightleftharpoons

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

[1] 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.

[2] Lovenberg, W., Weissbach, H. and Udenfriend, S. (1962). „Aromatic L-amino acid decarboxylase”. J. Biol. Chem. 237: 89-93. PMID 14466899.

[3] McGilvery, R.W. and Cohen, P.P. (1948). „The decarboxylation of L-phenylalanine by Streptococcus faecalis R”. J. Biol. Chem. 174: 813-816.

[4] 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.

[5] 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.

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