Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition (Q24324237)

xenobiotic metabolic process

GOA release 2020-03-11

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GOA release 2020-03-11

Jennifer L Martin

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author name string

Niranjali U Gamage

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Ronald G Duggleby

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Amanda C Barnett

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Michael Tresillian

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Catherine F Latham

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Nancy E Liyou

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Michael E McManus

Journal of Biological Chemistry

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language of work or name

English

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publication date

28 February 2003

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published in

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volume

278

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issue

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page(s)

7655-62

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cites work

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X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity

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Phenol sulphotransferase SULT1A1*1 genotype is associated with reduced risk of colorectal cancer

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A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3

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Expression and Characterization of a Novel Thyroid Hormone-Sulfating Form of Cytosolic Sulfotransferase from Human Liver

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The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study

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inferred from DOI database lookup

7 January 2021

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Sulfation and sulfotransferases. Introduction: changing view of sulfation and the cytosolic sulfotransferases

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inferred from DOI database lookup

7 January 2021

based on heuristic

Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes

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