4-hydroxyphenylpyruvate dioxygenase

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4-hydroxyphenylpyruvate dioxygenase
4-hydroxyphenylpyruvate dioxygenase
Homodimer of HPPD. Catalytic domain red, orange spheres: Fe 2+ , oligomeric domain blue

Existing structure data : 1SP9

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
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.

The reaction catalyzed by the HPPD. The whereabouts of the atoms involved in the reaction are highlighted.

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 .

The proposed reaction mechanism (the 4-hydroxy group is missing in the middle row)

Individual evidence

  1. 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 .
  2. 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).
  3. ^ TW Goodwin, EI Mercer: Introduction to Plant Biochemistry. Pergamon Press, 1983.