Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
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Target Concepts:
Gene/Protein
Disease
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Enzyme
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Query: UMLS:C1332347 (
ADH
)
2,230
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
L-Tyrosine (Tyr) is an aromatic amino acid synthesized
de novo
in plants and microbes. In animals, Tyr must be obtained through their diet or synthesized from L-phenylalanine. In addition to protein synthesis, Tyr serves as the precursor of neurotransmitters (e.g., dopamine and epinephrine) in animals and of numerous plant natural products, which serve essential functions in both plants and humans (e.g.,
vitamin E
and morphine). Tyr is synthesized via two alternative routes mediated by a TyrA family enzyme, prephenate, or arogenate dehydrogenase (PDH/TyrA
p
or
ADH
/TyrA
a
), typically found in microbes and plants, respectively. Although
ADH
activity is also found in some bacteria, the origin of arogenate-specific TyrA
a
enzymes is unknown. We recently identified an acidic Asp222 residue that confers
ADH
activity in plant TyrAs. In this study, structure-guided phylogenetic analyses identified bacterial homologs, closely-related to plant TyrAs, that also have an acidic 222 residue and
ADH
activity. A more distant archaeon TyrA that preferred PDH activity had a non-acidic Gln, whose substitution to Glu introduced
ADH
activity. These results indicate that the conserved molecular mechanism operated during the evolution of arogenate-specific TyrA
a
in both plants and microbes.
...
PMID:Conserved Molecular Mechanism of TyrA Dehydrogenase Substrate Specificity Underlying Alternative Tyrosine Biosynthetic Pathways in Plants and Microbes. 2916 32
