Characterization of the process of 5-aminolevulinic acid formation from glutamate via the C5 pathway in Clostridium thermoaceticum.
1. In vitro formation of 5-aminolevulinic acid (ALA) from glutamate required two enzyme fractions, separable on Blue Sepharose affinity chromatography, and a tRNA fraction, which can be replaced by Escherichia coli tRNA(Glu) in the reconstituted assay. 2. Gabaculine was shown to inhibit ALA formation in the complete assay as well as in a defined system consisting of only glutamate-1-semialdehyde and the enzyme fraction not retained on Blue Sepharose. 3. The results indicate that the enzyme system supporting ALA formation in Clostridium thermoaceticum is very similar to the tRNA(Glu)-dependent C5 pathway in plant plastids.
Oh-hama
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Department of Chemistry, Texas A & M University, College Station 77843-3255.
Stolowich
N J
NJ
Scott
A I
AI
D000622:Aminolevulinic Acid / Q000378:metabolism*; D003013:Clostridium / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D007700:Kinetics; D010944:Plants / Q000378:metabolism; D012343:RNA, Transfer / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives; D013696:Temperature
D005971:Glutamates; C029483:Blue-Sepharose; D000622:Aminolevulinic Acid; D012685:Sepharose; D012343:RNA, Transfer