Transformation of glutamate to. delta. -aminolevulinic acid by soluble extracts of Chlorobium vibrioforme

Journal Article · Sat Jul 01 00:00:00 EDT 1989 · Journal of Bacteriology; (USA)

OSTI ID:5027837

Rieble, S; Ormerod, J G; Beale, S ^[1]

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1. Brown Univ., Providence, RI (USA)

Formation of the tetrapyrrole pigment precursor {delta}-aminolevulinic acid (ALA) from glutamate was detected and partially characterized in extracts of the strictly anaerobic green photosynthetic bacterial species Chlorobium vibrioforme by using assay methods derived from those developed for algae and cyanobacteria. ALA formation in Chlorobium extracts was saturated at 10 mM glutamate and required NADPH and ATP at optimal concentrations of 0.3 and 3 mM, respectively. Preincubation of the enzyme extract with RNase A destroyed the ALA-forming activity completely. Activity in the RNase-treated extract was restored by supplementation with Chlorobium RNA after addition of RNasin to block further RNase action. RNA from the cyanobacterium Synechocystis sp. strain PCC 6803 and Escherichia coli tRNA{sup Glu} also restored activity. Activity was inhibited 50% by 0.2 {mu}M hemin. ALA formation was completely abolished by the addition of 5 {mu}M 3-amino-2,3-dihydrobenzoic acid (gabaculine). These results indicate that Chlorobium extracts share with those of plants, eucaryotic algae, cyanobacteria, prochlorophytes, and methanogens the capacity for RNA-dependent ALA formation from glutamate.

• OSTI ID: 5027837
• Journal Information: Journal of Bacteriology; (USA), Vol. 171:7; ISSN 0021-9193
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
AMINOLEVULINIC ACID
BIOCHEMICAL REACTION KINETICS
GLUTAMIC ACID
PHOTOSYNTHETIC BACTERIA
METABOLISM
BIOLOGICAL PATHWAYS
ENZYME ACTIVITY
RNA-ASE
AMINO ACIDS
CARBOXYLIC ACIDS
ENZYMES
ESTERASES
HYDROLASES
KINETICS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHODIESTERASES
REACTION KINETICS
550200* - Biochemistry