Abstract
The enzymatic defects in a number of Bacillus subtilis mutants of the alpha-ketoglutarate dehydrogenase complex lacking activity have been investigated. Mutants in the citK locus, as well as a series of deletions of unknown length covering the citK locus, are deficient in E1 of the complex, alpha-ketoglutarate dehydrogenase, but have normal activities of E2, dehydrolipoyl transsuccinylase, and E3, lipoamide dehydrogenase. The citK mutants and the citL22 mutant show in vitro complementation of alpha-ketoglutarate dehydrogenase complex activity. The citL22 mutant is severely deficient in lipoamide dehydrogenase activity, and, as a result, lacks activity for both the alpha-ketoglutarate and the pyruvate dehydrogenase complexes. Thus, the E3 components of both complexes are identical. The citL22 mutation maps between ura and metC on the chromosome.
MeSH Terms
Bacillus subtilis/enzymology,genetics
Chromosome Mapping
Dihydrolipoamide Dehydrogenase/metabolism
Genetic Complementation Test
Ketoglutarate Dehydrogenase Complex/genetics
Ketone Oxidoreductases/genetics
Mutation
Transduction, Genetic
Transformation, Genetic
Chemicals
Ketone Oxidoreductases
Ketoglutarate Dehydrogenase Complex
Dihydrolipoamide Dehydrogenase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hoch J A
Coukoulis H J
References (13)
13 references, click to expand
-
Gene-protein relationships of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: Chromosomal location of the lipoamide dehydrogenase gene.
J Gen Microbiol. 1974 Feb;80(2):523-32
PMID: 4596989
-
Citric acid cycle: gene-enzyme relationships in Bacillus subtilis.
J Bacteriol. 1970 Nov;104(2):826-33
PMID: 4992371
-
Transformation and transduction in recombination-defective mutants of Bacillus subtilis.
J Bacteriol. 1967 Jun;93(6):1925-37
PMID: 4960898
-
Studies with alpha-ketoglutarate dehydrogenase mutants of Escherichia coli.
Mol Gen Genet. 1969 Oct 13;105(2):182-90
PMID: 4904515
-
Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: lipoic acid and alpha-ketoglutarate dehydrogenase-less mutants.
J Gen Microbiol. 1968 Oct;53(3):363-81
PMID: 4889470
-
Activities of alpha-ketoisovalerate, pyruvate, and alpha-ketoglutarate dehydrogenases in a mutant of Bacillus subtilis.
Can J Microbiol. 1976 Apr;22(4):592-7
PMID: 816442
-
Uptake of branched-chain alpha-keto acids in Bacillus subtilis.
J Bacteriol. 1976 Jul;127(1):667-70
PMID: 819424
-
REQUIREMENTS FOR TRANSFORMATION IN BACILLUS SUBTILIS.
J Bacteriol. 1961 May;81(5):741-6
PMID: 16561900
-
Bacillus subtilis bacteriophage SPbeta: localization of the prophage attachment site, and specialized transduction.
J Bacteriol. 1977 Jan;129(1):556-8
PMID: 401505
-
Conditional dihydrostreptomycin resistance in Bacillus subtilis.
J Bacteriol. 1972 Apr;110(1):202-7
PMID: 4111768
-
Further studies with lipoamide dehydrogenase mutants of Escherichia coli K12.
J Gen Microbiol. 1974 Mar;81(1):237-45
PMID: 4207059
-
The membrane systems of the mitochondrion. I. The S fraction of the outer membrane of beef heart mitochondria.
Arch Biochem Biophys. 1966 Jul;115(1):153-64
PMID: 4226061
-
Gene-protein relationships of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: isolation and characterization of lipoamide dehydrogenase mutants.
J Gen Microbiol. 1973 Mar;75(1):197-210
PMID: 4578971