HPD Human
Description
HPD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is an essential enzyme in the catabolic pathway of the amino acid tyrosine. It catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate, a crucial step in the breakdown of tyrosine. This enzyme is found in nearly all aerobic organisms and plays a significant role in various metabolic processes.
HPPD is an Fe(II)-containing non-heme oxygenase. The enzyme typically forms homodimers in eukaryotes, with each subunit having a mass of approximately 40-50 kDa . The active site of HPPD is composed of residues near the C-terminus of the enzyme, and it contains an iron ion essential for its catalytic activity .
The reaction catalyzed by HPPD involves the oxidative decarboxylation of 4-hydroxyphenylpyruvate, leading to the formation of homogentisate. This process includes an NIH shift, where an alkyl group migrates to form a more stable carbocation . The enzyme’s mechanism is unique because it does not use α-ketoglutarate as a cofactor, unlike other oxygenases in its class .
HPPD is involved in the catabolism of tyrosine, an aromatic amino acid. This pathway is crucial for the proper metabolism of tyrosine, and defects in the HPPD gene can lead to metabolic disorders such as tyrosinemia type 3 and hawkinsinuria . These conditions result from the accumulation of toxic intermediates due to the impaired breakdown of tyrosine.
Recombinant HPPD refers to the enzyme produced through recombinant DNA technology, where the HPPD gene is cloned and expressed in a host organism, such as Escherichia coli. This approach allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant HPPD retains the same structural and functional properties as the native enzyme, making it a valuable tool for studying its biochemical characteristics and potential applications.
Research on HPPD has significant implications for both basic science and clinical applications. Understanding the enzyme’s structure and function can provide insights into its role in metabolic pathways and its potential as a target for therapeutic interventions. For instance, inhibitors of HPPD are used as herbicides, and there is ongoing research into their potential use in treating metabolic disorders related to tyrosine catabolism .
