4-hydroxyphenylpyruvate dioxygenase
4-hydroxyphenylpyruvate dioxygenase | ||
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Homodimer of HPPD. Catalytic domain red, orange spheres: Fe 2+ , oligomeric domain blue | ||
Properties of human protein | ||
Mass / length primary structure | 445 amino acids | |
Secondary to quaternary structure | Homotetramer in bacteria, homodimer in plants | |
Cofactor | Ascorbate , Fe 2+ | |
Identifier | ||
Gene name | HPD | |
External IDs |
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Enzyme classification | ||
EC, category | 1.13.11.27 , dioxygenase | |
Response type | oxidation | |
Substrate | 4-hydroxyphenylpyruvic acid + O 2 | |
Products | Homogentisic acid + CO 2 | |
Occurrence | ||
Homology family | HOG000221584 | |
Parent taxon | Creature |
The 4-hydroxyphenylpyruvate dioxygenase (HPPD) is a non-heme-Fe (II) - oxygenase that the second step Tyrosinemia, the conversion of 4-Hydroxy phenylpyruvic in homogentisic acid catalyzed and carbon dioxide. It can be found in almost every aerobic form of life.
Biological function
The reaction catalyzed by HPPD is an intermediate step in the breakdown of tyrosine into acetoacetic acid and fumaric acid .
Plants need HPPD to produce plastoquinones and tocopherol .
Individual evidence
- ↑ M. Gunsior, J. Ravel, GL Challis, CA Townsend: Engineering p-hydroxyphenylpyruvate dioxygenase to a p-hydroxymandelate synthase and evidence for the proposed benzene oxide intermediate in homogeneous formation. In: Biochemistry. Volume 43, Number 3, January 2004, pp. 663-674, ISSN 0006-2960 . doi: 10.1021 / bi035762w . PMID 14730970 .
- ↑ WE KNOX, M. LeMAY-KNOX: The oxidation in liver of l-tyrosine to acetoacetate through p-hydroxyphenylpyruvate and homogeneous acid. In: The Biochemical journal. Volume 49, Number 5, October 1951, pp. 686-693, ISSN 0264-6021 . PMID 14886367 . PMC 1197578 (free full text).
- ^ TW Goodwin, EI Mercer: Introduction to Plant Biochemistry. Pergamon Press, 1983.