DOPA decarboxylase

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Introduction

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spinqualitylabelsall models PDB ID 1js3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
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 exists as a homodimer, typical of this class of enzymes. It 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. Currently, the design of more specific inhibitors is a major objective in Parkinson's Disease research.