Enzymes involved in the metabolism of γ-hydroxybutyrate in SH-SY5Y cells: Identification of an iron-dependent alcohol dehydrogenase ADHFe1

Chemico-Biological Interactions

Volumn 178, Issue 1-3, 2009, Pages 283-287

  Lyon, Robert C ^a,b   Johnston, Stuart M ^a   Panopoulos, Andreas ^a   Alzeer, Samar ^a   McGarvie, Gail ^b   Ellis, Elizabeth M ^a  

^a UNIVERSITY OF STRATHCLYDE   (United Kingdom)

^b UNIVERSITY OF THE WEST OF SCOTLAND   (United Kingdom)

Author keywords

Hydroxybutyrate; Hydroxyacid oxoacid transhydrogenase; SH SY5Y

Indexed keywords

4 AMINOBUTYRATE AMINOTRANSFERASE; 4 HYDROXYBUTYRIC ACID; ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; ALDEHYDE REDUCTASE; IRON; NICOTINAMIDE ADENINE DINUCLEOTIDE; SUCCINATE SEMIALDEHYDE DEHYDROGENASE;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME METABOLISM; ENZYME RELEASE; ENZYME SYNTHESIS; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

ALCOHOL DEHYDROGENASE; AMINO ACID SEQUENCE; BASE SEQUENCE; CELL LINE, TUMOR; DNA PRIMERS; GAS CHROMATOGRAPHY-MASS SPECTROMETRY; HUMANS; IRON; MOLECULAR SEQUENCE DATA; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM OXYBATE;

BACTERIA (MICROORGANISMS);

EID: 59049096225     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.10.025     Document Type: Article

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