Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis.
作者： Matthias Wagner , Denise Sonntag , Rudolf Grimm , Andreas Pich , Christoph Eckerskorn
DOI: 10.1046/J.1432-1327.1999.00107.X
关键词:
摘要: The substrate-specific selenoprotein B of glycine reductase (PBglycine) from Eubacterium acidaminophilum was purified and characterized. enzyme consisted three different subunits with molecular masses about 22 (alpha), 25 (beta) 47 kDa (gamma), probably in an alpha 2 beta gamma composition. PBglycine cells grown the presence [75Se]selenite labeled 47-kDa subunit. 22-kDa both reacted fluorescein thiosemicarbazide, indicating a carbonyl compound. This residue prevented N-terminal sequencing (alpha) subunit, but it could be removed for Edman degradation by incubation o-phenylenediamine. A DNA fragment isolated sequenced which encoded (grdE), followed gene encoding (grdA2) subunit (grdB2). cloned represented second GrdB-encoding slightly previously identified partial grdBl-containing fragment. Both grdB genes contained in-frame UGA codon confirmed observed selenium content (gamma) Peptide sequence analyses suggest that grdE encodes proprotein is cleaved into 25-kDa PBglycine. Cleavage most occurred at -Asn-Cys- site concomitantly generation blocking moiety cysteine
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