Auto-hydroxylation of FIH-1: an Fe(ii), α-ketoglutarate-dependent human hypoxia sensor
نویسندگان
چکیده
منابع مشابه
Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel.
Factor inhibiting HIF (FIH, also known as HIF1AN) is an oxygen-dependent asparaginyl hydroxylase that regulates the hypoxia-inducible factors (HIFs). Several proteins containing ankyrin repeat domains (ARDs) have been characterised as substrates of FIH, although there is little evidence for a functional consequence of hydroxylation on these substrates. This study demonstrates that the transient...
متن کاملHypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply pro...
متن کاملCarnitine Biosynthesis /3-HYDROXYLATION OF TRIMETHYLLYSINE BY AN a-KETOGLUTARATE-DEPENDENT MITOCHONDRIAL DIOXYGENASE*
Rat liver mitochondria were found to hydroxylate E-Ntrimethyl+lysine to produce P-hydroxy-c-N-trimethyl-L-lysine, an intermediate in carnitine biosynthesis. The hydroxylating system requires a-ketoglutarate, Fez+, and ascorbate, but does not require NADPH nor NADH. No activity was found in the microsomal or soluble fractions of liver extracts. The hydroxylated a-amino acid was isolated and char...
متن کاملSyrB2 in syringomycin E biosynthesis is a nonheme FeII -ketoglutarate- and O2-dependent halogenase
The nine-residue lipodepsipeptide syringomycin E, elaborated as a phytotoxin by Pseudomonas syringae pv. syringae B301D contains a 4-Cl-L-Thr-9 moiety where failure to chlorinate results in a 3-fold drop in biological activity. The proteins SyrB1 and SyrB2 encoded by the biosynthetic cluster are shown to act as a substrate and enzyme pair for SyrB2-mediated chlorination of the aminoacyl-Senzyme...
متن کاملSyrB2 in syringomycin E biosynthesis is a nonheme FeII alpha-ketoglutarate- and O2-dependent halogenase.
The nine-residue lipodepsipeptide syringomycin E, elaborated as a phytotoxin by Pseudomonas syringae pv. syringae B301D contains a 4-Cl-L-Thr-9 moiety where failure to chlorinate results in a 3-fold drop in biological activity. The proteins SyrB1 and SyrB2 encoded by the biosynthetic cluster are shown to act as a substrate and enzyme pair for SyrB2-mediated chlorination of the aminoacyl-S-enzym...
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ژورنال
عنوان ژورنال: Chemical Communications
سال: 2008
ISSN: 1359-7345,1364-548X
DOI: 10.1039/b809099h