Discovery and biochemical characterization of enzymes completing the 4-hydroxyphenylacetate pathway in Acinetobacter baumannii TH.

ABSTRACT: A metabolic pathway for degrading 4-hydroxyphenylacetate (4-HPA) is crucial for environmental and pathogenic microbes to assimilate aromatic compounds. The 4-HPA degradation pathway in Acinetobacter baumannii TH comprises multiple reactions that are not fully understood. Enzymes involved in the first two steps (a two-component 4-HPA-3-hydroxylase, and 3,4-dihydroxyphenylacetate 2,3-dioxygenase) and the last two steps (4-hydroxy-2-keto-heptane-1,7-dioate aldolase and succinic semialdehyde (SSA) dehydrogenase (SSADH)) have been identified and studied, while the enzymes functioning in the middle of the pathway remain uncharacterized. Here, we identified products associated with individual enzymes including 5-carboxymethyl-2-hydroxymuconate-semialdehyde (CHMS) dehydrogenase (CHMSD), 5-carboxym

SUBMITTER: Chinantuya W 

PROVIDER: S-EPMC12718150 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature