Search results for "D-cysteine"

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Biochemical Properties of Human D-Amino Acid Oxidase

2017

D-amino acid oxidase catalyzes the oxidative deamination of D-amino acids. In the brain, the NMDA receptor coagonist D-serine has been proposed as its physiological substrate. In order to shed light on the mechanisms regulating D-serine concentration at the cellular level, we biochemically characterized human DAAO (hDAAO) in greater depth. In addition to clarify the physical-chemical properties of the enzyme, we demonstrated that divalent ions and nucleotides do not affect flavoenzyme function. Moreover, the definition of hDAAO substrate specificity demonstrated that D-cysteine is the best substrate, which made it possible to propose it as a putative physiological substrate in selected tiss…

0301 basic medicinestructure-function relationshipssubstrate specificityD-amino acid oxidaseD-serineGenetics and Molecular Biology (miscellaneous)Flavin groupBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryCofactor03 medical and health sciencesMolecular BiosciencesMolecular Biologylcsh:QH301-705.5D-cysteineOriginal Researchchemistry.chemical_classificationbiologyActive siteSubstrate (chemistry)Oxidative deaminationLigand (biochemistry)Amino acidD-amino acid oxidase; D-cysteine; D-serine; structure-function relationships; substrate specificity030104 developmental biologyBiochemistrychemistrylcsh:Biology (General)biology.proteinD-amino acid oxidase; D-cysteine; D-serine; Structure-function relationships; Substrate specificity; Molecular Biology; Biochemistry; Biochemistry Genetics and Molecular Biology (miscellaneous)D-amino acid oxidaseFrontiers in Molecular Biosciences

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