1991
DOI: 10.1128/jb.173.2.757-767.1991
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Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system

Abstract: Dihydrolipoamide dehydrogenase (DHLDH), dihydrolipoamide acetyltransferase (DHLTA), and acetoin: 2,6-dichlorophenolindophenol oxidoreductase (Ao:DCPIP OR) were purified from acetoin-grown cells of Pelobacter carbinolicus. DHLDH had a native Mr of 110,000, consisted of two identical subunits of Mr 54,000, and reacted only with NAD(H) as a coenzyme. The N-terminal amino acid sequence included the flavin adenine dinucleotide-binding site and exhibited a high degree of homology to other DHLDHs. DHLTA had a native … Show more

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Cited by 75 publications
(81 citation statements)
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“…In these bacteria, acetoin (3-hydroxy-2-butanone) is formed from pyruvate in two enzymatic steps (191), providing the substrate for AoDH. Reconstituted AoDH containing the E1, E2, and E3 subunits from the bacterium Pelobacter carbinolicus is specific for acetoin and does not use pyruvate or ␣-ketoglutarate as substrate (162). The E1␣ protein contains a region of divergent sequence compared to other ␣-ketoacid dehydrogenases and appears to be responsible for the substrate specificity of AoDH (115).…”
Section: Lipoylated Complexesmentioning
confidence: 99%
“…In these bacteria, acetoin (3-hydroxy-2-butanone) is formed from pyruvate in two enzymatic steps (191), providing the substrate for AoDH. Reconstituted AoDH containing the E1, E2, and E3 subunits from the bacterium Pelobacter carbinolicus is specific for acetoin and does not use pyruvate or ␣-ketoglutarate as substrate (162). The E1␣ protein contains a region of divergent sequence compared to other ␣-ketoacid dehydrogenases and appears to be responsible for the substrate specificity of AoDH (115).…”
Section: Lipoylated Complexesmentioning
confidence: 99%
“…22) In diaphorase activity, the apparent K m values of rBfmBC for DCPIP and NADH were 0.12 mM and 0.25 mM respectively. No diaphorase activity was detected when NADH was replaced by NADPH, as observed in the DLD of halophilic archaebacteria 20) and the hyperthermophilic archaeon Thermococcus kodakaraensis.…”
Section: Kinetic Parametersmentioning
confidence: 99%
“…Therefore, this bacterium lacks the 2,3-butanedi oil cycle which was described by Juni and Heym (36) in Aci netobacter calcoaceticus. In contrast, A. eutrophus degr&Ldes acetoin directly by cleavage into two C2 compounds , like Bacillus subtilis (35,43,44) or Pelobacter car binolicus (48)(49)(50).…”
mentioning
confidence: 99%