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Anthranilate synthase enzyme system and complementation in Pseudomonas species.

S F Queener, I C Gunsalus

    Proceedings of the National Academy of Sciences of the United States of America
    |November 1, 1970
    PubMed
    Summary

    Anthranilate synthase in Pseudomonas species is a two-component enzyme system. Different Pseudomonas groups show distinct subunit complementation, impacting enzyme activity and complex stability.

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    Area of Science:

    • Biochemistry
    • Microbiology
    • Enzymology

    Background:

    • Anthranilate synthase (AS) is crucial for tryptophan biosynthesis.
    • Pseudomonas putida possesses a two-component AS system (AS I and AS II).
    • AS I (65 kDa) and AS II (18 kDa) have distinct roles in anthranilate formation.

    Purpose of the Study:

    • To investigate the structure and function of anthranilate synthase in Pseudomonas species.
    • To compare the organization of the tryptophan biosynthesis pathway across different Pseudomonas groups.
    • To analyze subunit interactions and their impact on enzyme activity.

    Main Methods:

    • Enzyme characterization of AS I and AS II.
    • Analysis of subunit complementation in hybrid enzymes.
    • Comparative study across six Pseudomonas species.

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    Main Results:

    • AS I binds chorismate and is feedback-inhibited by tryptophan; AS II binds L-glutamine.
    • Ammonium-dependent amination requires only AS I, while L-glutamine-dependent amide transfer requires both AS I and AS II.
    • Two complementation groups (putida-aeruginosa and acidovorans-testosteroni) were identified, differing in hybrid enzyme activity and subunit dissociation.
    • Pseudomonas organization differs from enteric bacteria, where phosphoribosyl transferase has dual activity.

    Conclusions:

    • Pseudomonas anthranilate synthase exhibits species-specific variations in subunit interaction and organization.
    • The distinct functional roles of AS I and AS II are conserved across Pseudomonas.
    • Subunit complementation patterns provide a basis for classifying Pseudomonas species regarding tryptophan biosynthesis.