Initial studies on the substrate specificity of soluble recombinant 4-hydroxyphenylpyruvate dioxygenase from rat liver-Reference-Cited by-同舟云学术

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Initial studies on the substrate specificity of soluble recombinant 4-hydroxyphenylpyruvate dioxygenase from rat liver

Published:1996-07 Issue:13 Volume:6 Page:1503-1506
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Crouch N.P.,Baldwin J.E.,Lee M.-H.,MacKinnon C.H.,Zhang Z.H.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference19 articles.

1. 4-Hydroxyphenylpyruvate dioxygenase appears to display α-ketoisocaproate dioxygenase activity in rat liver

2. Purification of p-Hydroxyphenylpyruvate Hydroxylase from Human Liver.

3. Further Studies on Phenylpyruvate Oxidase

4. p-HYDROXYPHENYLPYRUVATE OXIDASE OF LIVER

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1. Synthesis and Herbicidal Activities of Novel 3-(α-Hydroxymethylene) pyrrolidine-2,4-dione Derivatives Containing a Cyclopropane Moiety;Journal of Heterocyclic Chemistry;2013-03

2. Alteration of the Co-substrate Selectivity of Deacetoxycephalosporin C Synthase;Journal of Biological Chemistry;2001-05

3. SAR studies of 2- o -substituted-benzoyl- and 2-alkanoyl-cyclohexane-1,3-diones as inhibitors of 4-hydroxyphenylpyruvate dioxygenase;Bioorganic & Medicinal Chemistry Letters;2000-05

4. The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism (1967 to 1999);Natural Product Reports;2000

5. Cloning, Expression, and Purification of Mammalian 4-Hydroxyphenylpyruvate Dioxygenase/α-Ketoisocaproate Dioxygenase;Branched-Chain Amino Acids, Part B;2000

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