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Literature DB >> 12215170

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.

Luke A McNeill¹, Kirsty S Hewitson, Timothy D Claridge, Jürgen F Seibel, Louise E Horsfall, Christopher J Schofield.

Abstract

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 production of the threo -isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro -isomer.

Entities: Chemical Disease Gene Species

Mesh：

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Year: 2002 PMID： 12215170 PMCID： PMC1222951 DOI： 10.1042/BJ20021162

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

25 in total

1. Asymmetric synthesis of orthogonally protected L-threo-beta-hydroxyasparagine.

Authors: D L Boger; R J Lee; P Y Bounaud; P Meier
Journal: J Org Chem Date: 2000-10-06 Impact factor: 4.354

2. Occurrence of beta-hydroxylated asparagine residues in non-vitamin K-dependent proteins containing epidermal growth factor-like domains.

Authors: C T Przysiecki; J E Staggers; H G Ramjit; D G Musson; A M Stern; C D Bennett; P A Friedman
Journal: Proc Natl Acad Sci U S A Date: 1987-11 Impact factor: 11.205

3. 1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X.

Authors: M Selander; E Persson; J Stenflo; T Drakenberg
Journal: Biochemistry Date: 1990-09-04 Impact factor: 3.162

Review 4. Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors.

Authors: J Stenflo
Journal: Blood Date: 1991-10-01 Impact factor: 22.113

Review 5. Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1.

Authors: G L Semenza
Journal: Annu Rev Cell Dev Biol Date: 1999 Impact factor: 13.827

6. A model for the complex between the hypoxia-inducible factor-1 (HIF-1) and its consensus DNA sequence.

Authors: G Michel; E Minet; I Ernest; I Roland; F Durant; J Remacle; C Michiels
Journal: J Biomol Struct Dyn Date: 2000-10

7. Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma.

Authors: L Lavaissiere; S Jia; M Nishiyama; S de la Monte; A M Stern; J R Wands; P A Friedman
Journal: J Clin Invest Date: 1996-09-15 Impact factor: 14.808

8. cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase.

Authors: S Jia; W J VanDusen; R E Diehl; N E Kohl; R A Dixon; K O Elliston; A M Stern; P A Friedman
Journal: J Biol Chem Date: 1992-07-15 Impact factor: 5.157

9. Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase.

Authors: J Stenflo; E Holme; S Lindstedt; N Chandramouli; L H Huang; J P Tam; R B Merrifield
Journal: Proc Natl Acad Sci U S A Date: 1989-01 Impact factor: 11.205

10. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.

Authors: G L Wang; B H Jiang; E A Rue; G L Semenza
Journal: Proc Natl Acad Sci U S A Date: 1995-06-06 Impact factor: 11.205

64 in total

Review 1. Regulation of erythropoietin production.

Authors: Wolfgang Jelkmann
Journal: J Physiol Date: 2010-11-15 Impact factor: 5.182

Review 2. Adaptive and maladaptive cardiorespiratory responses to continuous and intermittent hypoxia mediated by hypoxia-inducible factors 1 and 2.

Authors: Nanduri R Prabhakar; Gregg L Semenza
Journal: Physiol Rev Date: 2012-07 Impact factor: 37.312

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.

1. Asymmetric synthesis of orthogonally protected L-threo-beta-hydroxyasparagine.

2. Occurrence of beta-hydroxylated asparagine residues in non-vitamin K-dependent proteins containing epidermal growth factor-like domains.

3. 1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X.

Review 4. Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors.

Review 5. Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1.

6. A model for the complex between the hypoxia-inducible factor-1 (HIF-1) and its consensus DNA sequence.

7. Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma.

8. cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase.

9. Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase.

10. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.

Review 1. Regulation of erythropoietin production.

Review 2. Adaptive and maladaptive cardiorespiratory responses to continuous and intermittent hypoxia mediated by hypoxia-inducible factors 1 and 2.

3. Uncoupled O2-activation in the human HIF-asparaginyl hydroxylase, FIH, does not produce reactive oxygen species.

4. Featured Article: Hypoxia-inducible factor-1α dependent nuclear entry of factor inhibiting HIF-1.

Review 5. Therapeutic targeting of the HIF oxygen-sensing pathway: Lessons learned from clinical studies.

6. Interaction of HIF-1α and Notch3 Is Required for the Expression of Carbonic Anhydrase 9 in Breast Carcinoma Cells.

Review 7. Carcinogenic effect of nickel compounds.

8. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia.

9. Inverse solvent isotope effects arising from substrate triggering in the factor inhibiting hypoxia inducible factor.

10. The biology of hypoxia: the role of oxygen sensing in development, normal function, and disease.