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Mutations affecting lipoamide dehydrogenases of Pseudomonas putida
Journal of Bacteriology
|February 1, 1983
Summary
Pseudomonas putida utilizes two distinct lipoamide dehydrogenases (LPDs) for different metabolic pathways. Mutant studies reveal these LPDs are likely products of separate genes, despite some cross-reactivity.
Area of Science:
- Biochemistry
- Microbial Metabolism
- Enzymology
Background:
- Pseudomonas putida synthesizes two lipoamide dehydrogenases (LPDs): LPD-glu (56 kDa) and LPD-val (49 kDa).
- LPD-val is specific for branched-chain keto acid dehydrogenase, while LPD-glu likely serves pyruvate and 2-ketoglutarate dehydrogenases.
Purpose of the Study:
- To isolate and characterize Pseudomonas putida mutants affecting lipoamide dehydrogenases.
- To elucidate the relationship between LPD-glu and LPD-val.
Main Methods:
- Isolation and characterization of P. putida mutants (JS287, JS94).
- Proteolysis and immunological analysis (antiserum cross-reactivity) to compare LPD-glu and LPD-val.
Main Results:
- Mutant JS287 specifically lacked LPD-val, with normal LPD-glu levels.
- Mutant JS94 exhibited pleiotropic defects in multiple dehydrogenase activities.
- Proteolysis yielded distinct fragments for LPD-glu and LPD-val, indicating separate structural genes.
- Antisera confirmed LPD-glu and LPD-val are distinct, though LPD-val showed cross-reactivity with LPD-glu.
Conclusions:
- LPD-glu and LPD-val are products of separate structural genes in Pseudomonas putida.
- Mutant studies and immunological data support distinct roles and origins for the two lipoamide dehydrogenases.