World Library  
Flag as Inappropriate
Email this Article

Aromatic L-amino acid decarboxylase

Article Id: WHEBN0000905107
Reproduction Date:

Title: Aromatic L-amino acid decarboxylase  
Author: World Heritage Encyclopedia
Language: English
Subject: Dopamine, Phenethylamine, Monoamine oxidase, Histidine decarboxylase, Catecholamine
Collection: Ec 4.1.1
Publisher: World Heritage Encyclopedia
Publication
Date:
 

Aromatic L-amino acid decarboxylase

aromatic-L-amino-acid decarboxylase
Ribbon diagram of a DOPA decarboxylase dimer.[1]
Identifiers
EC number 4.1.1.28
CAS number 9042-64-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
DOPA decarboxylase (aromatic L-amino acid decarboxylase)
Identifiers
Symbol DDC
Entrez 1644
HUGO 2719
OMIM 107930
RefSeq NM_000790
UniProt P20711
Other data
EC number 4.1.1.28
Locus Chr. 7 p11

Aromatic L-amino acid decarboxylase (EC 4.1.1.28, synonyms: DOPA decarboxylase, tryptophan decarboxylase, 5-hydroxytryptophan decarboxylase, AAAD,[2] AADC) is a lyase enzyme.

Contents

  • Reactions 1
  • As a rate-limiting step 2
  • Genetics 3
  • See also 4
  • References 5
  • External links 6

Reactions

It catalyzes several different decarboxylation reactions:[3]

The enzyme uses pyridoxal phosphate, the active form of vitamin B6, as a cofactor.

Human biosynthesis pathway for trace amines and catecholamines[4][5]
In humans, catecholamines and phenethylaminergic trace amines are derived from the amino acid phenylalanine.
Human serotonin biosynthesis pathway

As a rate-limiting step

In normal dopamine and serotonin (5-HT) neurotransmitter synthesis, AAAD is not the rate-limiting step in either reaction. However, AAAD becomes the rate-limiting step of dopamine synthesis in patients treated with L-DOPA (such as in Parkinson's Disease), and the rate-limiting step of serotonin synthesis in people treated with 5-HTP (such as in mild depression or dysthymia). AAAD is inhibited by Carbidopa outside of the blood brain barrier to inhibit the premature conversion of L-DOPA to Dopamine in the treatment of Parkinson's.

In humans, AAAD is also the rate-limiting enzyme in the formation of trace amine neurotransmitters.

Genetics

The gene encoding the enzyme is referred to as DDC and located on chromosome 7 in humans.[6] Single nucleotide polymorphisms and other gene variations have been investigated in relation to neuropsychiatric disorders, e.g., a one-base pair deletion at –601 and a four-base pair deletion at 722–725 in exon 1 in relation to bipolar disorder[7] and autism. No direct correlation between gene variation and autism was found.[8]

See also

References

  1. ^ ​; Burkhard P, Dominici P, Borri-Voltattorni C, Jansonius JN, Malashkevich VN (November 2001). "Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase". Nat. Struct. Biol. 8 (11): 963–7.  
  2. ^ Logan, Carolynn M.; Rice, M. Katherine (1987). Logan's Medical and Scientific Abbreviations. Philadelphia:  
  3. ^ "AADC". Human Metabolome database. Retrieved 17 February 2015. 
  4. ^ Broadley KJ (March 2010). "The vascular effects of trace amines and amphetamines". Pharmacol. Ther. 125 (3): 363–375.  
  5. ^ Lindemann L, Hoener MC (May 2005). "A renaissance in trace amines inspired by a novel GPCR family". Trends Pharmacol. Sci. 26 (5): 274–281.  
  6. ^ Lisa J. Scherer, John D. McPherson, John J. Wasmuth and J. Lawrence Marsh (June 1992). "Human dopa decarboxylase: Localization to human chromosome 7p11 and characterization of hepatic cDNAs".  
  7. ^ A. D. Borglum, T. G. Bruun, T. E. Kjeldsen, H. Ewald, O. Mors, G. Kirov, C. Russ, B. Freeman, D. A. Collier & T. A. Kruse (November 1999). "Two novel variants in the DOPA decarboxylase gene: association with bipolar affective disorder".  
  8. ^ Marlene B. Lauritsen, Anders D. Borglum, Catalina Betancur, Anne Philippe, Torben A. Kruse, Marion Leboyer & Henrik Ewald (May 2002). "Investigation of two variants in the DOPA decarboxylase gene in patients with autism".  

External links

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and USA.gov, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for USA.gov and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
 
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
 
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.
 



Copyright © World Library Foundation. All rights reserved. eBooks from World eBook Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.