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Literature summary for 3.5.4.16 extracted from

  • Sun, X.; Fratz, S.; Sharma, S.; Hou, Y.; Rafikov, R.; Kumar, S.; Rehmani, I.; Tian, J.; Smith, A.; Schreiber, C.; Reiser, J.; Naumann, S.; Haag, S.; Hess, J.; Catravas, J.D.; Patterson, C.; Fineman, J.R.; Black, S.M.
    C-terminus of heat shock protein 70-interacting protein-dependent GTP cyclohydrolase I degradation in lambs with increased pulmonary blood flow (2011), Am. J. Respir. Cell Mol. Biol., 45, 163-171.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
additional information asymmetric dimethylarginine, ADMA, decreases GCH1 protein, but not mRNA concentrations, in pulmonary arterial endothelial cells because of the ubiquitination and proteasome-dependent degradation of GCH1. Overexpression of CHIP potentiates, whereas a CHIP U-box domain mutant attenuates, ADMA-induced GCH1 degradation and reductions in cellular BH4 concentrations. L-Arginine acts antagonistic and restores the activities Ovis aries

Organism

Organism UniProt Comment Textmining
Ovis aries
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 lambs
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Posttranslational Modification

Posttranslational Modification Comment Organism
additional information ubiquitination and proteasome-dependent degradation of GCH1. The CHIP-ubiquitin pathway modifies GCH1 in a lamb model of pulmonary hypertension secondary to increased pulmonary blood flow Ovis aries

Source Tissue

Source Tissue Comment Organism Textmining
lung
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 Ovis aries
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pulmonary artery endothelial cell
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 Ovis aries
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Synonyms

Synonyms Comment Organism
GCH1
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 Ovis aries
guanosine-5'-triphosphate cyclohydrolase 1
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 Ovis aries

General Information

General Information Comment Organism
metabolism GCH1 is the rate-limiting enzyme in the generation of BH4 Ovis aries
additional information asymmetric dimethylarginine, ADMA, decreases GCH1 protein, but not mRNA concentrations, in pulmonary arterial endothelial cells because of the ubiquitination and proteasome-dependent degradation of GCH1. Hsp90-GCH1 interactions are reduced, whereas the association of GCH1 with Hsp70 and the C-terminus of Hsp70-interacting protein, i.e. CHIP, increases in the cells. In vivo Hsp90/GCH1 interactions are decreased, whereas GCH1-Hsp70 and GCH1-CHIP interactions and GCH1 ubiquitination are increased. L-Arginine acts antagonistic and restores the activities Ovis aries
physiological function GTP cyclohydrolase I interaction is required for degradation of the C-terminus of heat shock protein 70-interacting protein. GCH1 is a client protein for Hsp90. The U-box domain of CHIP is essential for ADMA-mediated GCH1 degradation in pulmonary arterial endothelial cells Ovis aries