
A complete pathway for β‐alanine and β‐amino‐ iso ‐butyrate catabolism in Pseudomonas aeruginosa
Author(s) -
Waters Paul,
Venables W.A.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01420.x
Subject(s) - alanine , transamination , biochemistry , butyrate , decarboxylation , chemistry , catabolism , stereochemistry , biology , metabolism , amino acid , fermentation , catalysis
Pseudomonas aeruginosa PAO1 was found to catabolise β‐alanine and β‐amino‐ iso ‐butyrate (β‐AIB) by the following pathway: (i) transamination by β‐alanine: pyruvate aminotransferase (BAPAT) to yield l ‐alanine and either malonic semialdehyde or its methyl analogue, respectively; (ii) oxidative decarboxylation of the respective semialdehydes to acetyl CoA or propionyl CoA; (iii) regeneration of pyruvate from l ‐alanine by the action of dl ‐alanine racemase (AR) and d ‐alanine dehydrogenase (DAD). Mutants defective in BAPAT or DAD failed to catabolise either β‐alanine or β‐AIB, and β‐alanine was an inducer for the entire pathway.