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3-hydroxyisobutyryl-CoA hydrolase

3-hydroxyisobutyryl-CoA hydrolase, 3-hydroxyisobutyryl-coenzyme A hydrolase
Top mentioned proteins: ACID, HAD, fibrillin-1, CAN, AGE
Papers on 3-hydroxyisobutyryl-CoA hydrolase
Effect of a 5-mo nutritional intervention on nutritional status and quality of life for patient with 3-hydroxyisobutyryl-coenzyme A hydrolase deficiency: A case report.
Wang et al., Beijing, China. In Nutrition, Nov 2015
3-Hydroxy-isobutyryl-coenzyme A (CoA) hydrolase (HBICH) deficiency is a rare cerebral organic aciduria caused by disturbance of valine catabolism that leads to the accumulation of toxic metabolites, methacrylyl-CoA.
Metabolite studies in HIBCH and ECHS1 defects: Implications for screening.
Pitt et al., Melbourne, Australia. In Mol Genet Metab, Aug 2015
3-hydroxyisobutyryl-CoA hydrolase activity in fibroblasts was below the limit of detection of the enzymatic assay and two novel HIBCH mutations were identified (c.[129dupA];[1033G>A]).
Thiamine-Responsive and Non-responsive Patients with PDHC-E1 Deficiency: A Retrospective Assessment.
Boneh et al., Melbourne, Australia. In Jimd Rep, 2014
We retrospectively reviewed all medical records of all PDHC-deficient patients (n = 19; all had PDHA1 gene mutations) and one patient with severe PDHC deficiency secondary to 3-hydroxyisobutyryl-CoA hydrolase deficiency managed at our centre between 1982 and 2012.
HIBCH deficiency in a patient with phenotypic characteristics of mitochondrial disorders.
Reis et al., Erlangen, Germany. In Am J Med Genet A, 2014
HIBCH (3-hydroxyisobutyryl-CoA hydrolase) deficiency (MIM #250620) is a rare autosomal recessive inborn error of metabolism, leading to a block in the catabolic pathway of the amino acid valine and presumably to accumulation of toxic valine metabolites in mitochondria.
ECHS1 mutations in Leigh disease: a new inborn error of metabolism affecting valine metabolism.
Pitt et al., Australia. In Brain, 2014
Two siblings with fatal Leigh disease had increased excretion of S-(2-carboxypropyl)cysteine and several other metabolites that are features of 3-hydroxyisobutyryl-CoA hydrolase (HIBCH) deficiency, a rare defect in the valine catabolic pathway associated with Leigh-like disease.
Sustained complete response to CTLA-4 blockade in a patient with metastatic, castration-resistant prostate cancer.
Beer et al., Portland, United States. In Cancer Immunol Res, 2014
Of the top 5 genes, only 3-hydroxyisobutyryl-CoA hydrolase (HIBCH) could be identified in the amplified tumor biopsy cDNA.
Redox proteomics changes in the fungal pathogen Trichosporon asahii on arsenic exposure: identification of protein responses to metal-induced oxidative stress in an environmentally-sampled isolate.
Sheehan et al., Lahore, Pakistan. In Plos One, 2013
Some proteins showed both increase in abundance coupled with decrease in IAF fluorescence; 3-hydroxyisobutyryl-CoA hydrolase; homoserine dehydrogenase Hom6 and hypothetical proteins A1Q2_03020 and A1Q1_00754.
Identification and computational annotation of genes differentially expressed in pulp development of Cocos nucifera L. by suppression subtractive hybridization.
Li et al., Haikou, China. In Bmc Plant Biol, 2013
KEGG (Kyoto Encyclopedia of Genes and Genomes) analysis showed that 1-acyl-sn-glycerol-3-phosphate acyltransferase (LPAAT), phospholipase D, acetyl-CoA carboxylase carboxyltransferase beta subunit, 3-hydroxyisobutyryl-CoA hydrolase-like and pyruvate dehydrogenase E1 β subunit were associated with fatty acid biosynthesis or metabolism.
Technical note: a gene delivery system in the embryonic cells of avian species using a human adenoviral vector.
Lee et al., Columbus, United States. In J Anim Sci, 2009
Primary cells isolated from the embryonic pectoralis major muscles of the chicken and quail were cultured and incubated with human recombinant Ad serotype 5 (Ad5) containing sequences encoding either the green fluorescence protein (GFP) gene alone, as a tracking marker, or both GFP and murine 3-hydroxyisobutyryl-CoA hydrolase (mHIBCH) as a target gene.
Biosynthesis of enantiopure (S)-3-hydroxybutyric acid in metabolically engineered Escherichia coli.
Hong et al., Taejŏn, South Korea. In Appl Microbiol Biotechnol, 2008
A biosynthetic pathway for the production of (S)-3-hydroxybutyric acid (S3HB) from glucose was established in recombinant Escherichia coli by introducing the beta-ketothiolase gene from Ralstonia eutropha H16, the (S)-3-hydroxybutyryl-CoA dehydrogenase gene from R. eutropha H16, or Clostridium acetobutylicum ATCC824, and the 3-hydroxyisobutyryl-CoA hydrolase gene from Bacillus cereus ATCC14579.
Mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase results in progressive infantile neurodegeneration.
Wanders et al., Amsterdam, Netherlands. In Am J Hum Genet, 2007
Only a single patient with 3-hydroxyisobutyryl-CoA hydrolase deficiency has been described in the literature, and the molecular basis of this inborn error of valine catabolism has remained unknown until now.
Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis.
Schofield et al., Oxford, United Kingdom. In J Biol Chem, 2005
Labeling experiments ruled out the possibility that hydrolysis proceeds via an anhydride in which water attacks a carbonyl derived from Glu(131), as proposed for 3-hydroxyisobutyryl-CoA hydrolase.
Divergent function in the crotonase superfamily: an anhydride intermediate in the reaction catalyzed by 3-hydroxyisobutyryl-CoA hydrolase.
Gerlt et al., Urbana, United States. In J Am Chem Soc, 2003
3-Hydroxyisobutyryl-CoA hydrolase (HICH), a member of the enoyl-CoA (crotonase) superfamily, catalyzes the hydrolysis of 3-hydroxyisobutyryl-CoA to 3-hydroxyisobutyrate. Like other members of the superfamily, the sequence of HICH contains conserved sequences for an oxyanion hole that stabilizes anionic intermediates.
Catabolism of isobutyrate by colonocytes.
Harris et al., Indianapolis, United States. In Arch Biochem Biophys, 1996
Both enterocytes and colonocytes express high levels of 3-hydroxyisobutyryl-CoA hydrolase, an enzyme activity important in maintaining low intracellular concentrations of methacrylyl-CoA, a common, potentially toxic intermediate in the catabolic pathways of these compounds.
Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver.
Harris et al., Nagoya, Japan. In J Biol Chem, 1994
The enzyme responsible for this reaction, 3-hydroxyisobutyryl-CoA hydrolase (EC, was purified 7200-fold from rat liver in this study.
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