Structure and Catalysis in the Escherichia coli Hotdog-fold Thioesterase Paralogs YdiI and YbdB (Q27684644)

8

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author name string

Rui Wu

1

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John A Latham

2

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Danqi Chen

3

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Jeremiah Farelli

4

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Hong Zhao

5

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Kaila Matthews

6

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Karen N Allen

The Catalytic Mechanism of the Hotdog-fold Enzyme Superfamily 4-Hydroxybenzoyl-CoA Thioesterase from Arthrobacter sp. Strain SU

7

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language of work or name

English

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publication date

29 July 2014

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published in

Biochemistry

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volume

53

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issue

29

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page(s)

4788-805

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cites work

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The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU

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Divergence of substrate specificity and function in the Escherichia coli hotdog-fold thioesterase paralogs YdiI and YbdB.

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Co-evolution of HAD phosphatase and hotdog-fold thioesterase domain function in the menaquinone-pathway fusion proteins BF1314 and PG1653.

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A Thioester Substrate Binds to the Enzyme Arthrobacter Thioesterase in Two Ionization States; Evidence from Raman Difference Spectroscopy

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The Akt C-terminal modulator protein is an acyl-CoA thioesterase of the Hotdog-Fold family

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In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH

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