Purification and Cloning of a Broad Substrate Specificity Human Liver Carboxylesterase That Catalyzes the Hydrolysis of Cocaine and Heroin*
- Evgenia V. Pindel, N. Kedishvili, W. Bosron
- Biology, ChemistryJournal of Biological Chemistry
- 6 June 1997
HCE-2 had higher catalytic efficiencies for hydrolysis of 4-methylumbelliferyl acetate, heroin, and 6-monoacetylmorphine and greater inhibition by eserine than hCE-1 and may play an important role in the degradation of cocaine and heroin in human tissues.
Enzymology of retinoic acid biosynthesis and degradation
- N. Kedishvili
- BiologyJournal of Lipid Research
- 1 July 2013
Current knowledge about the roles of various biosynthetic and catabolic enzymes in the regulation of retinoic acid homeostasis is summarized and the remaining questions in the field are outlined.
Medium- and short-chain dehydrogenase/reductase gene and protein families
- X. Parés, J. Farrés, N. Kedishvili, G. Duester
- BiologyCellular and Molecular Life Sciences
- 14 November 2008
Km values for most retinoid-active ADHs and RDHs are close to 1 μM or lower, suggesting that they participate physiologically in retinol/retinaldehyde interconversion.
The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative.
Methylphenidate Is Stereoselectively Hydrolyzed by Human Carboxylesterase CES1A1
- Zejin Sun, D. Murry, W. Bosron
- Chemistry, BiologyJournal of Pharmacology and Experimental…
- 1 August 2004
CES1A1 is the major enzyme responsible for the first-pass, stereoselective metabolism of methylphenidate, and both enantiomers ofethylphenidate can be fit into the three-dimensional model of CES 1A1 to form productive complexes in the active site.
17‐Beta Hydroxysteroid Dehydrogenase 13 Is a Hepatic Retinol Dehydrogenase Associated With Histological Features of Nonalcoholic Fatty Liver Disease
The association of variants in HSD17B13 with specific features of NAFLD histology is demonstrated and the enzyme is identified as a lipid droplet–associated RDH; the data suggest that HSD 17B13 plays a role inNAFLD through its enzymatic activity.
Diversity of the Pyruvate Dehydrogenase Kinase Gene Family in Humans *
- R. Gudi, M. Melissa, N. Kedishvili, Y. Zhao, K. M. Popov
- Biology, Computer ScienceJournal of Biological Chemistry
- 1 December 1995
The deduced amino acid sequences of three isoenzymic forms of PDK found in humans suggest that PDK2 is a major isoenzyme responsible for regulation of pyruvate dehydrogenase in human tissues, and PDK3 appears to have the highest specific activity among the three isenzymes tested as recombinant proteins.
Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and…
- O. Belyaeva, O. Korkina, A. Stetsenko, Tom S Kim, P. Nelson, N. Kedishvili
- Biology, ChemistryBiochemistry
- 10 May 2005
Tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues,RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH 12 might also play a role in detoxification of lipid peroxidation products.
The Retinaldehyde Reductase Activity of DHRS3 Is Reciprocally Activated by Retinol Dehydrogenase 10 to Control Retinoid Homeostasis*
- Mark K. Adams, O. Belyaeva, Lizhi Wu, N. Kedishvili
- Biology, MedicineThe Journal of Biological Chemistry
- 14 April 2014
It is demonstrated that DHRS3 requires the presence of retinol dehydrogenase 10 (RDH10) to display its full catalytic activity and, in turn, activates RDH10, which acts as a robust high affinity all-trans-retinaldehyde-specific reductase that effectively converts retinal dehyde back to retinl, decreasing the rate of retinoic acid biosynthesis.
Expression and Kinetic Characterization of Recombinant Human Stomach Alcohol Dehydrogenase
- N. Kedishvili, W. Bosron, Ting-kai Li
- Chemistry, BiologyThe Journal of Biological Chemistry
- 24 February 1995
There are important amino acid differences in the alcohol-binding site between the human class IV (σ) and human class I (β) alcohol dehydrogenases that appear to explain the high catalytic efficiency for all-trans-retinol, the high kcat for ethanol, and the low catalytic Efficiency for secondary alcohols of σ-ADH relative to β1-ADh.