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Article

The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity.

FEBS letters - 3 Sept 2008

Tang Wai-Kwan, Wong Kam-Bo, Lam Yuk-Man, Cha Sun-Shin, Cheng Christopher H K, Fong Wing-Ping

Abstract excerpt

The crystal structure of seabream antiquitin in complex with the cofactor NAD(+) was solved at 2.8A resolution. The mouth of the substrate-binding pocket is guarded by two conserved residues, Glu120 and Arg300. To test the role of these two residues, we have prepared the two mutants E120A and R300A. Our model and kinetics data suggest that antiquitin's specificity towards the substrate alpha-aminoadipic...

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PMID: 18694748
DOI: 10.1016/j.febslet.2008.07.059

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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