The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity (Q27651513)

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12 January 2020

title

The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity (English)

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12 January 2020

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2

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12 January 2020

Christopher Cheng

5

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12 January 2020

author name string

Wai-Kwan Tang

1

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12 January 2020

Yuk-Man Lam

3

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12 January 2020

Sun-Shin Cha

4

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12 January 2020

Wing-Ping Fong

6

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language of work or name

English

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publication date

9 August 2008

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12 January 2020

number of pages

7

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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12 January 2020

volume

582

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12 January 2020

issue

20

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12 January 2020

page(s)

3090-3096

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Homology between a human protein and a protein of the green garden pea.

12 January 2020

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Antiquitin, a relatively unexplored member in the superfamily of aldehyde dehydrogenases with diversified physiological functions

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Arabidopsis and tobacco plants ectopically expressing the soybean antiquitin-like ALDH7 gene display enhanced tolerance to drought, salinity, and oxidative stress.

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Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression.

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First purification of the antiquitin protein and demonstration of its enzymatic activity.

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Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene

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Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase

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