Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes
A mutant strain of Salmonella typhimurium (SL 1634 dml-51) capable of growth on d-malate as sole carbon source was shown to produce d-malic enzyme. This enzyme was absent in the parent wild-type strain which was unable to grow on d-malate. Growth of the mutant on d-malate also resulted in a greatly...
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ftpubmed:oai:pubmedcentral.nih.gov:249916 2023-05-15T16:02:02+02:00 Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes Stern, Joseph R. O'Brien, R. W. 1969-04 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC249916 http://www.ncbi.nlm.nih.gov/pubmed/4889267 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC249916 http://www.ncbi.nlm.nih.gov/pubmed/4889267 Copyright © 1969 American Society for Microbiology Genetics and Molecular Biology Text 1969 ftpubmed 2013-08-29T16:22:41Z A mutant strain of Salmonella typhimurium (SL 1634 dml-51) capable of growth on d-malate as sole carbon source was shown to produce d-malic enzyme. This enzyme was absent in the parent wild-type strain which was unable to grow on d-malate. Growth of the mutant on d-malate also resulted in a greatly increased level of β-isopropylmalic enzyme compared with its level in the wild-type strain grown on citrate or l-malate. The d-malic and β-isopropylmalic enzymes, both of which catalyze a nicotinamide adenine dinucleotide- and Mg++-dependent oxidative decarboxylation of their respective substrates, were shown to be distinct enzymes by selective inhibition with erythro-dl-β-hydroxyaspartate and by other methods. Cell extracts of the mutant strain also oxidized dl-β-methyl-, dl-β-ethyl-, dl-β-propyl- and dl-ββ-dimethylmalates, in order of decreasing activity. dl-β-Methyl-malate was shown to be oxidized by both the d-malic and the β-isopropylmalic enzymes, whereas the oxidation of the other β-alkylmalates appeared to be effected exclusively by the β-isopropylmalic enzyme. β-Isopropylmalic enzyme activity was induced by d-malate but not by l-malate, showing that it behaved as a d-malictype enzyme. Growth of Aerobacter aerogenes on d-malate, which caused induction of d malic enzyme, resulted in only a small increase in the activity of β-isopropylmalic enzyme. Text DML PubMed Central (PMC) |
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Genetics and Molecular Biology |
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Genetics and Molecular Biology Stern, Joseph R. O'Brien, R. W. Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes |
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Genetics and Molecular Biology |
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A mutant strain of Salmonella typhimurium (SL 1634 dml-51) capable of growth on d-malate as sole carbon source was shown to produce d-malic enzyme. This enzyme was absent in the parent wild-type strain which was unable to grow on d-malate. Growth of the mutant on d-malate also resulted in a greatly increased level of β-isopropylmalic enzyme compared with its level in the wild-type strain grown on citrate or l-malate. The d-malic and β-isopropylmalic enzymes, both of which catalyze a nicotinamide adenine dinucleotide- and Mg++-dependent oxidative decarboxylation of their respective substrates, were shown to be distinct enzymes by selective inhibition with erythro-dl-β-hydroxyaspartate and by other methods. Cell extracts of the mutant strain also oxidized dl-β-methyl-, dl-β-ethyl-, dl-β-propyl- and dl-ββ-dimethylmalates, in order of decreasing activity. dl-β-Methyl-malate was shown to be oxidized by both the d-malic and the β-isopropylmalic enzymes, whereas the oxidation of the other β-alkylmalates appeared to be effected exclusively by the β-isopropylmalic enzyme. β-Isopropylmalic enzyme activity was induced by d-malate but not by l-malate, showing that it behaved as a d-malictype enzyme. Growth of Aerobacter aerogenes on d-malate, which caused induction of d malic enzyme, resulted in only a small increase in the activity of β-isopropylmalic enzyme. |
format |
Text |
author |
Stern, Joseph R. O'Brien, R. W. |
author_facet |
Stern, Joseph R. O'Brien, R. W. |
author_sort |
Stern, Joseph R. |
title |
Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes |
title_short |
Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes |
title_full |
Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes |
title_fullStr |
Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes |
title_full_unstemmed |
Oxidation of d-Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of Salmonella typhimurium and by Aerobacter aerogenes |
title_sort |
oxidation of d-malic and β-alkylmalic acids by wild-type and mutant strains of salmonella typhimurium and by aerobacter aerogenes |
publishDate |
1969 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC249916 http://www.ncbi.nlm.nih.gov/pubmed/4889267 |
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DML |
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DML |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC249916 http://www.ncbi.nlm.nih.gov/pubmed/4889267 |
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Copyright © 1969 American Society for Microbiology |
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