Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-09

AUTHORS

Dhirendra K. Simanshu, Sagar Chittori, H. S. Savithri, M. R. N. Murthy

ABSTRACT

In Escherichia coli and Salmonella typhimurium, L-threonine is cleaved non-oxidatively to propionate via 2-ketobutyrate by biodegradative threonine deaminase, 2-ketobutyrate formate-lyase (or pyruvate formate-lyase), phosphotransacetylase and propionate kinase. In the anaerobic condition, L-threonine is converted to the energy-rich keto acid and this is subsequently catabolised to produce ATP via substrate-level phosphorylation, providing a source of energy to the cells. Most of the enzymes involved in the degradation of L-threonine to propionate are encoded by the anaerobically regulated tdc operon. In the recent past, extensive structural and biochemical studies have been carried out on these enzymes by various groups. Besides detailed structural and functional insights, these studies have also shown the similarities and differences between the other related enzymes present in the metabolic network. In this paper, we review the structural and biochemical studies carried out on these enzymes. More... »

PAGES

1195-1206

Journal

TITLE

Journal of Biosciences

ISSUE

Suppl 2

VOLUME

32

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s12038-007-0121-1

    DOI

    http://dx.doi.org/10.1007/s12038-007-0121-1

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1010157375

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/17954980


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