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Front Mol Biosci. 2017 Feb 9;4:5. doi: 10.3389/fmolb.2017.00005. eCollection 2017.

Structural Basis of the Substrate Specificity and Enzyme Catalysis of a Papaver somniferum Tyrosine Decarboxylase.

Author information

1
Key Laboratory of Tropical Biological Resources of Ministry of Education, Hainan UniversityHainan, China; Hainan Key Laboratory of Sustainable Utilization of Tropical Bioresources, College of Agriculture, Hainan UniversityHainan, China; Laboratory of Tropical Veterinary Medicine and Vector Biology, Hainan UniversityHaikou, Hainan, China.
2
Biology Department, Brookhaven National Laboratory, Upton New York, NY, USA.
3
Department of Biochemistry, Virginia Tech Blacksburg, VA, USA.

Abstract

Tyrosine decarboxylase (TyDC), a type II pyridoxal 5'-phosphate decarboxylase, catalyzes the decarboxylation of tyrosine. Due to a generally high sequence identity to other aromatic amino acid decarboxylases (AAADs), primary sequence information is not enough to understand substrate specificities with structural information. In this study, we selected a typical TyDC from Papaver somniferum as a model to study the structural basis of AAAD substrate specificities. Analysis of the native P. somniferum TyDC crystal structure and subsequent molecular docking and dynamics simulation provide some structural bases that explain substrate specificity for tyrosine. The result confirmed the previous proposed mechanism for the enzyme selectivity of indolic and phenolic substrates. Additionally, this study yields the first crystal structure for a plant type II pyridoxal-5'-phosphate decarboxylase.

KEYWORDS:

Papaver somniferum; aromatic amino acid decarboxylase; crystal structure; decarboxylase; substrate specificity; tyrosine decarboxylases

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