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Results show that HOGA1 harboring mutations found in primary hyperoxaluria is thermally unstable and targeted for proteolytic degradation leading to an absolute loss of function.
Among the seven patients identified with HOGA1 mutations the median onset of clinical symptoms was 1.8 years. Five patients initially presented with urolithiasis, and two other patients presented with urinary tract infection.
Our results strongly suggest HOGA1 as a major cause of PH, indicate a greater genetic heterogeneity of hyperoxaluria, and point to a favorable outcome of type III in the context of PH despite incomplete or absent biochemical remission
Two crystal forms of DHDPSL were obtained, both of which diffracted X-rays to approximately 2.0 A resolution
hHOGA utilizes a type I aldolase reaction mechanism, but employs novel residue interactions for substrate binding
Detection of HOGA1 variants in idiopathic calcium oxalate urolithiasis also suggests HOGA1 may be a predisposing factor for this condition
DHDPSL is the gene encoding 4-hydroxy-2-oxoglutarate aldolase, catalyzing the final step in the metabolic pathway of hydroxyproline.
Native HOGA (zeige OAT Proteine) was purified from bovine kidney using a novel microtitration protocol to obtain diffraction-quality crystals.
The authors of PMID searching for genes in a region of chromosome 10 linked to primary hyperoxalurea type III. They noted that even though the encoded protein has been described as a mitochondrial dihydrodipicolinate synthase-like enzyme, it shares little homology with E. coli dihydrodipicolinate synthase (Dhdps), particularly in the putative substrate-binding region. Moreover, neither lysine biosynthesis nor sialic acid metabolism, for which Dhdps is responsible, occurs in vertebrate mitochondria. They propose that this gene encodes mitochondrial 4-hydroxyl-2-oxoglutarate aldolase (EC 18.104.22.168), which catalyzes the final step in the metabolic pathway of hydroxyproline, releasing glyoxylate and pyruvate. This gene is predominantly expressed in the liver and kidney, and mutations in this gene are found in patients with primary hyperoxalurea type III. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.
, N-acetylneuraminate pyruvate lyase 2 (putative)
, dihydrodipicolinate synthase-like, mitochondrial
, dihydrodipicolinate synthetase homolog 2
, probable 2-keto-4-hydroxyglutarate aldolase
, probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
, probable KHG-aldolase
, protein 569272