Abstract
In the presence of the dye 2,6-dichlorophenol indophenol crude extracts of alumina-ground or of sonically disrupted mycelium of Streptomyces scabies catalyzed dehydrogenase reactions with the substrates succinate, citrate, malate, and glutamic acid. These extracts or mycelial homogenates formed glutamic acid in transaminase reactions with α-ketoglutarate and the amino acids aspartic, leucine, and valine. Other amino acids, lysine, threonine, glycine, histidine, and tyrosine, failed to act as amino donors. No evidence could be obtained for direct transamination with α-ketoglutarate and glutamine or asparagine; with the latter, analyses suggested that glutamic acid formation occurred by preliminary deamination and subsequent transamination from the aspartic acid produced.
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