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4-hydroxyphenylpyruvate dioxygenase
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| Identifiers | |
| Symbol | HPD |
| Alt. Symbols | PPD; |
| Entrez | 3242 |
| HUGO | 5147 |
| OMIM | 609695 |
| RefSeq | NM_002150 |
| UniProt | P32754 |
| Other data | |
| EC number | 1.13.11.27 |
| Locus | Chr. 12 q24-qter |
4-Hydroxyphenylpyruvate dioxygenase HPD is a Cu-containing enzyme, that catalyzes the third reaction in the catabolism of phenylalanine and tyrosine - the conversion of 4-hydroxyphenylpyruvate to homogentisate.
The HPD reaction occurs through a NIH shift and involves the oxidative decarboxylation of an α-oxo acid as well as aromatic ring hydroxylation. The NIH-shift, which has been demonstrated through isotope-labeling studies, involves migration of an alkyl group to form a more stable carbocation. The shift, accounts for the observation that C3 is bonded to C4 in 4-hydroxyphenylpyruvate but to C5 in homogentisate.
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