2gmv
From Proteopedia
PEPCK complex with a GTP-competitive inhibitor
Structural highlights
Disease[PCKGC_HUMAN] Defects in PCK1 are the cause of cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:261680]. A metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autoposy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait. Function[PCKGC_HUMAN] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNew modifications on the C-8 4-aminobenzyl unit of the previously reported 3-alkyl-1,8-dibenzylxanthine inhibitors of cPEPCK are presented. The most active compound reported here is the 5-chloro-1,3-dimethyl-1H-pyrazole-4-sulfonic acid amide derivative 2 with an IC(50) of 0.29+/-0.08 microM. An X-ray analysis of a heteroaromatic sulfonamide is presented showing a new pi-pi interaction. C-8 Modifications of 3-alkyl-1,8-dibenzylxanthines as inhibitors of human cytosolic phosphoenolpyruvate carboxykinase.,Pietranico SL, Foley LH, Huby N, Yun W, Dunten P, Vermeulen J, Wang P, Toth K, Ramsey G, Gubler ML, Wertheimer SJ Bioorg Med Chem Lett. 2007 Jul 15;17(14):3835-9. Epub 2007 May 22. PMID:17532214[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Human | Large Structures | Dunten, P | Gluconeogenesis | Inhibitor | Lyase | Xanthine
