DOPA decarboxylase

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Revision as of 23:34, 3 May 2011

Introduction

1js3, resolution 2.25Å ()

Ligands:

, ,

Activity:

Aromatic-L-amino-acid decarboxylase, with EC number 4.1.1.28

Related:

1js6

Structural annotation:
Resources:	CATH : 1Js3A01, 1Js3A03, 1Js3A02, 1Js3B03, 1Js3B02, 1Js3B01 InterPro : Ipr010977, Ipr002129, Ipr015421, Ipr015424, Ipr015422 Pfam : PF00282 SCOP : d1js3a_, d1js3b_ UniProt : P80041

Functional annotation:
Biological process:	carboxylic acid metabolic process amino acid and derivative metabolic process catecholamine biosynthetic process
Molecular function:	lyase activity carboxy-lyase activity catalytic activity pyridoxal phosphate binding aromatic-L-amino-acid decarboxylase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

DOPA decarboxylase (DDC, aromatic L-amino acid decarboxylase, tryptophan decarboxylase, 5-hydroxytryptophan decarboxylase, AAAD) is an approximately 52 kDa protein that belongs to the aspartate aminotransferase family (fold type 1) of PLP-dependent enzymes. The catalytically active form of the enzyme exists as a homodimer, typical of this class of enzymes.^[1] The homodimeric form of the enzyme purified from sus scrofa is shown in complex with the inhibitor carbidopa to the right. DOPA decarboxylase is responsible for the synthesis of dopamine and serotonin from L-DOPA and L-5;hydroxytryptophan, respectively. Due to its role in neurotransmitter synthesis, DOPA decarboxylase has been implicated in Parkinson's disease, a disease thought to be the result of the degeneration of dopamine-producing cells in the brain. Currently, treatment for the disease is aimed at DOPA decarboxylase inhibition, which would allow greater amounts of exogenously administered L-DOPA to reach the brain.