Literature summary for 1.14.13.2 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.

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Crystallization (Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
Y201F	crystals differ from the wild-type enzyme at two surface positions, 228 and 249	Pseudomonas aeruginosa
Y385F	crystals differ from the wild-type enzyme at two surface positions, 228 and 249	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)