hydroxylases การใช้
- Tyrosine hydroxylase is a tetramer of four identical aromatic amino acid hydroxylases.
- JmjC domain-containing proteins are predicted to function as protein hydroxylases or histone demethylases.
- In normal circumstances after injury HIF-1a is degraded by prolyl hydroxylases ( PHDs ).
- When iron, 2-oxoglutarate and oxygen are present, HIF is inactivated by HIF hydroxylases.
- Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines.
- Fumarate and succinate have been identified as potent inhibitors of prolyl hydroxylases, thus leading to the stabilisation of HIF.
- Tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases.
- Several hydroxylase enzymes are believed to incorporate an NIH shift in their mechanism, including 4-hydroxyphenylpyruvate dioxygenase and the tetrahydrobiopterin dependent hydroxylases.
- In addition, the coordinated activity of the prolyl hydroxylases ( PHDs ) maintain the appropriate balance of HIF1A protein in the post-translation phase.
- Recent work has demonstrated an important link between intermediates of the citric acid cycle and the regulation of hypoxia-inducible factors ( prolyl 4-hydroxylases.
- It has been proposed that cosubstrate and iron concentrations poise the HIF hydroxylases to respond to an appropriate " hypoxic window " for a particular cell type or tissue.
- In this alternative pathway, the enzymes involved are likely to be cytochrome p450 hydroxylases, and S-adenosyl-L-methionine-dependent O-methyltransferases ( OMT ).
- Tryptophan hydroxylase ( TPH ), tyrosine hydroxylase ( TH ) and phenylalanine hydroxylase ( PAH ) are members of a superfamily of aromatic amino acid hydroxylases, catalyzing key steps in important metabolic pathways.
- A class of prolyl hydroxylases which act specifically on HIF has been identified; hydroxylation of HIF allows the protein to be targeted for degradation . kidney disease, ischemia, anemia, and other important diseases.
- "' Tyrosine hydroxylase "'or "'tyrosine 3-monooxygenase "'is the enzyme responsible for catalyzing the conversion of the amino acid aromatic amino acid hydroxylases ( AAAHs ).
- Tryptophan hydroxylases catalyze the biopterin-dependent monooxygenation of tryptophan to 5-hydroxytryptophan ( 5-HTP ), which is subsequently decarboxylated to form the neurotransmitter serotonin ( 5-hydroxytryptamine or 5-HT ).
- PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin ( BH 4, a pteridine cofactor ) and a non-heme iron for catalysis.
- PAH is unusual among the aromatic amino acid hydroxylases for its involvement in catabolism; tyrosine and tryptophan hydroxylases, on the other hand, are primarily expressed in the central nervous system and catalyze rate-limiting steps in neurotransmitter / hormone biosynthesis.
- PAH is unusual among the aromatic amino acid hydroxylases for its involvement in catabolism; tyrosine and tryptophan hydroxylases, on the other hand, are primarily expressed in the central nervous system and catalyze rate-limiting steps in neurotransmitter / hormone biosynthesis.
- A subset of Cytochrome P450 ( CYP450 ) microsome-bound ?-hydroxylases ( see 20-Hydroxyeicosatetraenoic acid ) metabolize arachidonic acid to 20-Hydroxyeicosatetraenoic acid ( 20-HETE ) and 19-hydroxyeicosatetraenoic acid by an omega oxidation reaction.
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