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A mechanistic rationalisation for the substrate specificity of recombinant mammalian 4-hydroxyphenylpyruvate dioxygenase (4-HPPD)

✍ Scribed by Nicholas P. Crouch; Robert M. Adlington; Jack E. Baldwin; Meng -Huee. Lee; Colin H. MacKinnon

Book ID: 104207809
Publisher: Elsevier Science
Year: 1997
Tongue: French
Weight: 985 KB
Volume: 53
Category: Article
ISSN: 0040-4020
DOI: 10.1016/s0040-4020(97)00398-0

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✦ Synopsis

The isolation and purification of ot-ketoisocaproate dioxygenase [ot-KICD] from rat liver is described.

Sequence determination of the purified protein revealed it to have complete homology to rat liver 4-hydroxyphenylpyruvate dioxygenase [4-HPPD] which was confirmed by the cloning and expression of the gene encoding 4-HPPD in E. coli. Examination of the substrate specificity of the resul~lg soluble recombinant protein revealed it to be capable of the oxidative decarboxylation of a range of ketoacids derived from proteinogenic amino acids. The significance of the turnover of these different ketoacids is discussed in relation to the mechanism of this fascinating enzyme.

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