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Literature summary extracted from

  • Lah, M.S.; Palfey, B.A.; Schreuder, H.A.; Ludwig, M.L.
    Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: The Tyr201Phe, Tyr385Phe, and Asn300Asp variants (1994), Biochemistry, 33, 1555-1564.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.2 crystal structure of mutant enzyme Y201F, Y385F, and N300D Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.2 N300D mutation has profound effect on enzyme structure. The side chain of Asp300 moves away from the flavin, disrupting the interaction of the carboxamide group with the flavin O(2) atom, and the alpha-helix H10 that begins at residue 297 is displaced, altering its dipole interaction with the flavin ring Pseudomonas aeruginosa
1.14.13.2 Y201F crystals differ from the wild-type enzyme at two surface positions, 228 and 249 Pseudomonas aeruginosa
1.14.13.2 Y385F crystals differ from the wild-type enzyme at two surface positions, 228 and 249 Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.2 Pseudomonas aeruginosa
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.2 4-hydroxybenzoate + NADPH + O2
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 Pseudomonas aeruginosa protocatechuate + NADP+ + H2O
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