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4-Hydroxyphenylpyruvate dioxygenase : ウィキペディア英語版 | 4-Hydroxyphenylpyruvate dioxygenase
4- Hydroxyphenylpyruvate dioxygenase (HPPD) is an Fe(II)-containing non-heme oxygenase that catalyzes the second reaction in the catabolism of tyrosine - the conversion of 4-hydroxyphenylpyruvate into homogentisate. HPPD is an enzyme that is found in nearly all aerobic forms of life. The reaction that HPPD achieves is shown here ==Enzyme Mechanism==
HPPD is categorized within a class of oxygenase enzymes that usually utilize α-ketoglutarate and diatomic oxygen to oxygenate or oxidize a target molecule.〔Hausinger, Robert (2004). "Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes." Critical Reviews in Biochemistry and Molecular Biology. 39(1) 21-68. http://informahealthcare.com/doi/abs/10.1080/10409230490440541〕 However, HPPD differs from most molecules in this class due to the fact that it does not use α-ketoglutarate, and it only utilizes two substrates while adding both atoms of diatomic oxygen into the product, homogentisate.〔Moran GR. (4-Hydroxyphenylpyruvate dioxygenase ) Arch Biochem Biophys. 2005 Jan 1;433(1):117-28. PMID 15581571〕 The HPPD 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. The predicted mechanism of HPPD can be seen in the following figure
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