Evidence for the Mechanism of Hydroxylation by 4-Hydroxyphenylpyruvate Dioxygenase and Hydroxymandelate Synthase from Intermediate Partitioning in Active Site Variants-Reference-Cited by-同舟云学术

Evidence for the Mechanism of Hydroxylation by 4-Hydroxyphenylpyruvate Dioxygenase and Hydroxymandelate Synthase from Intermediate Partitioning in Active Site Variants

Published:2011-08-16 Issue:35 Volume:50 Page:7694-7704
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Shah Dhara D.¹,Conrad John A.¹,Heinz Brian¹,Brownlee June M.¹,Moran Graham R.¹

Affiliation:

1. Department of Chemistry and Biochemistry, University of Wisconsin—Milwaukee, 3210 N. Cramer St., Milwaukee, Wisconsin 53211-3029, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi2009344

Reference55 articles.

1. Interaction of (4-Hydroxyphenyl)pyruvate Dioxygenase with the Specific Inhibitor 2-[2-Nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione

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3. The Secreted Pyomelanin Pigment of Legionella pneumophila Confers Ferric Reductase Activity

4. Pyomelanin is produced by Shewanella algae BrY and affected by exogenous iron

5. Distribution of coenzyme F420 and properties of its hydrolytic fragments

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