Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase

PLoS ONE

Volumn 5, Issue 1, 2010, Pages

  Han, Qian ^a   Ding, Haizhen ^a   Robinson, Howard ^b   Christensen, Bruce M ^c   Li, Jianyong ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC LEVO AMINO ACID DECARBOXYLASE; DOPAMINE; SEROTONIN; TRYPTOPHAN; TYROSINE; AROMATIC L AMINO ACID DECARBOXYLASE, DROSOPHILA; AROMATIC L-AMINO ACID DECARBOXYLASE, DROSOPHILA; DROSOPHILA PROTEIN; PRIMER DNA;

ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL ANALYSIS; CHEMICAL STRUCTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DROSOPHILA MELANOGASTER; ENZYME SPECIFICITY; NONHUMAN; PH MEASUREMENT; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; TEMPERATURE MEASUREMENT; AMINO ACID SEQUENCE; ANIMAL; BIOCATALYSIS; CHEMISTRY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PH; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

DROSOPHILA MELANOGASTER; HEXAPODA;

AMINO ACID SEQUENCE; ANIMALS; AROMATIC-L-AMINO-ACID DECARBOXYLASES; BASE SEQUENCE; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 77952475277     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0008826     Document Type: Article

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