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・ 4-hydroxyglutamate transaminase
・ 4-hydroxymandelate oxidase
・ 4-hydroxymandelate synthase
・ 4-Hydroxymandelic acid
・ 4-hydroxymuconic-semialdehyde dehydrogenase
・ 4-Hydroxynonenal
・ 4-hydroxynonenal-lysine
・ 4-hydroxyphenylacetaldehyde dehydrogenase
・ 4-hydroxyphenylacetaldehyde oxime monooxygenase
・ 4-hydroxyphenylacetate 1-monooxygenase
・ 4-Hydroxyphenylacetate 3-monooxygenase
・ 4-hydroxyphenylacetate decarboxylase
・ 4-Hydroxyphenylacetic acid
・ 4-Hydroxyphenylacetone
・ 4-hydroxyphenylpyruvate decarboxylase
4-Hydroxyphenylpyruvate dioxygenase
・ 4-hydroxyphenylpyruvate dioxygenase inhibitor
・ 4-hydroxyphenylpyruvate oxidase
・ 4-Hydroxyphenylpyruvic acid
・ 4-hydroxyproline epimerase
・ 4-hydroxyquinoline 3-monooxygenase
・ 4-Hydroxytestosterone
・ 4-hydroxythreonine-4-phosphate dehydrogenase
・ 4-Iodo-N,N-dimethylaniline
・ 4-Iodopropofol
・ 4-Koma Nano Ace
・ 4-Maleylacetoacetic acid
・ 4-manifold
・ 4-MBC
・ 4-Me-αMT


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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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