Search results for "gamma-Butyrobetaine Dioxygenase"

showing 4 items of 4 documents

Crystal structure of human gamma-butyrobetaine hydroxylase.

2010

Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domai…

EGF-like domainStereochemistrygamma-Butyrobetaine DioxygenaseBiophysicsDrug designBiochemistryHydroxylationchemistry.chemical_compoundDioxygenaseCatalytic DomainHumansEnzyme InhibitorsMolecular BiologyHistidinechemistry.chemical_classificationCrystallographybiologyActive siteCell BiologyRecombinant ProteinsZincEnzymeBiochemistrychemistryCyclic nucleotide-binding domainDrug Designbiology.proteinProtein MultimerizationMethylhydrazinesBiochemical and biophysical research communications
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Molecular cloning and characterization of the cDNA encoding the rat liver gamma-butyrobetaine hydroxylase

1999

Carnitine biosynthesis from lysine and methionine involves five enzymatic reactions. gamma-butyrobetaine hydroxylase (BBH; EC 1.14. 11.1) is the last enzyme of this pathway. It catalyzes the reaction of hydroxylation of gamma-butyrobetaine to carnitine. The cDNA encoding this enzyme has been isolated and characterized. The cDNA contained an open reading frame of 1161 bp encoding a protein of 387 amino acids with a deduced molecular weight of 44.5 kDa. The sequence of the cDNA showed an important homology with the human cDNA recently isolated. Northern analysis showed gamma-butyrobetaine hydroxylase expression in the liver and in some extend in the testis and the epididymis. During this stud…

MaleDNA Complementarygamma-Butyrobetaine DioxygenaseMolecular Sequence DataBiologyMolecular cloningMixed Function Oxygenaseschemistry.chemical_compoundSequence Homology Nucleic AcidComplementary DNAmedicineAnimalsAmino Acid SequenceCarnitineCloning MolecularRats WistarMolecular Biologychemistry.chemical_classificationMessenger RNAMethionineBase SequenceSequence Homology Amino AcidGene Expression Regulation DevelopmentalCell BiologyMolecular biologyRatsAmino acidOpen reading frameLiverchemistryBiochemistryCarnitine biosynthesisSequence Alignmentmedicine.drugBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Thyroid hormone controls carnitine status through modifications of gamma-butyrobetaine hydroxylase activity and gene expression.

2002

The carnitine system plays a key role in beta-oxidation of long-chain fatty acids by permitting their transport into the mitochondrial matrix. The effects of hypothyroidism and hyperthyroidism were studied on gamma-butyrobetaine hydroxylase (BBH), the enzyme responsible for carnitine biosynthesis in the rat. In rat liver, BBH activity was decreased in the hypothyroid state and increased in hyperthyroid animals. The modifications in BBH activity correlated with changes in the enzyme Vmax values. These changes were shown to be related to hepatic BBH mRNA abundance. Thyroid hormones are known to interact with lipid metabolism, in particular by increasing long-chain fatty acid oxidation through…

Maleendocrine systemmedicine.medical_specialtyThyroid Hormonesendocrine system diseasesgamma-Butyrobetaine DioxygenaseThyroid GlandBiologyGene Expression Regulation EnzymologicMixed Function OxygenasesCellular and Molecular Neurosciencechemistry.chemical_compoundInternal medicineCarnitinemedicineAnimalsCarnitineRNA MessengerMolecular BiologyBeta oxidationPharmacologychemistry.chemical_classificationFatty acid metabolismThyroidFatty acidLipid metabolismCell BiologyRatsKineticsEndocrinologymedicine.anatomical_structurechemistryBiochemistryLiverOrgan SpecificityCarnitine biosynthesisMolecular Medicinemedicine.drugHormoneCellular and molecular life sciences : CMLS
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Enhancement of activities relative to fatty acid oxidation in the liver of rats depleted of l-carnitine by d-carnitine and a γ-butyrobetaine hydroxyl…

1995

Abstract This study was designed to examine whether the depletion of l -carnitine may induce compensatory mechanisms allowing higher fatty acid oxidative activities in liver, particularly with regard to mitochondrial carnitine palmitoyltransferase I activity and peroxisomal fatty acid oxidation. Wistar rats received d -carnitine for 2 days and 3-(2,2,2-trimethylhydrazinium)propionate (mildronate), a non-competitive inhibitor of γ-butyrobetaine hydroxylase, for 10 days. They were starved for 20 hr before being sacrificed. A dramatic reduction in carnitine concentration was observed in heart, skeletal muscles and kidneys, and to a lesser extent, in liver. Triacylglycerol content was found to …

Malemedicine.medical_specialtygamma-Butyrobetaine DioxygenaseOxidative phosphorylationBiologyMitochondrionBiochemistryMixed Function OxygenasesCarnitineInternal medicinemedicineAnimalsCarnitineRats WistarBeta oxidationPharmacologychemistry.chemical_classificationBody WeightFatty AcidsFatty acidOrgan SizePeroxisomeRatsEndocrinologyLiverchemistryKetone bodiesCarnitine palmitoyltransferase IOxidation-ReductionMethylhydrazinesmedicine.drugBiochemical Pharmacology
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