Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/14992
Title: Conversion of hydroxyphenylpyruvate dioxygenases into hydroxymandelate synthases by directed evolution.
Authors: O'Hare, HM
Huang, F
Holding, A
Choroba, OW
Spencer, JB
First Published: 12-Jun-2006
Citation: FEBS LETT, 2006, 580 (14), pp. 3445-3450
Abstract: Hydroxymandelate synthase (HmaS) and hydroxyphenylpyruvate dioxygenase (HppD) are non-heme iron-dependent dioxygenases, which share a common substrate and first catalytic step. The catalytic pathways then diverge to yield hydroxymandelate for secondary metabolism, or homogentisate in tyrosine catabolism. To probe the differences between these related active sites that channel a common intermediate down alternative pathways, we attempted to interconvert their activities by directed evolution. HmaS activity was readily introduced to HppD by just two amino acid changes. A parallel attempt to engineer HppD activity in HmaS was unsuccessful, suggesting that homogentisate synthesis places greater chemical and steric demands on the active site.
DOI Link: 10.1016/j.febslet.2006.05.018
ISSN: 0014-5793
Links: http://hdl.handle.net/2381/14992
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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