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Q34175574-5AEC9866-0E0D-46A8-8FF8-337D355C829B
Q34175574-5AEC9866-0E0D-46A8-8FF8-337D355C829B
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http://www.wikidata.org/entity/statement/Q34175574-5AEC9866-0E0D-46A8-8FF8-337D355C829B
Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis.
P2860
Q34175574-5AEC9866-0E0D-46A8-8FF8-337D355C829B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34175574-5AEC9866-0E0D-46A8-8FF8-337D355C829B
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wasDerivedFrom
f4a278de1cb50b0b8c28c12e64b1b98cff562978
P2860
Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins.