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Q45404294-CD6BD58B-C0B6-4325-A39B-7E8A2D7FF0E8
Q45404294-CD6BD58B-C0B6-4325-A39B-7E8A2D7FF0E8
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http://www.wikidata.org/entity/statement/Q45404294-CD6BD58B-C0B6-4325-A39B-7E8A2D7FF0E8
Conserved Molecular Mechanism of TyrA Dehydrogenase Substrate Specificity Underlying Alternative Tyrosine Biosynthetic Pathways in Plants and Microbes.
P2860
Q45404294-CD6BD58B-C0B6-4325-A39B-7E8A2D7FF0E8
BestRank
Statement
http://www.wikidata.org/entity/statement/Q45404294-CD6BD58B-C0B6-4325-A39B-7E8A2D7FF0E8
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wasDerivedFrom
d3c8c0a33239182dc5148a78eef3858ee3e4d942
P2860
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms.