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Circular dichroism of biodegradative threonine deaminase

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
29
Issue
2
Identifiers
DOI: 10.1016/0006-291x(67)90584-0
Disciplines
  • Biology

Abstract

Abstract Biodegradative threonine deaminase of Escherichia coli ( Umbarger and Brown, 1957) contains pyridoxal phosphate (PLP) as a cofactor and is activated by AMP ( Wood and Gunsalus, 1949; Phillips and Wood, 1964; Hirata et al. , 1965 ). In addition to the catalytic function through Schiff base formation with substrate, the enzymebound PLP was shown to contribute to the stabilization of the enzyme conformation ( Tokushige, 1967). In this paper is described the circular dichroism (CD) of PLP in the biodegradative threonine deaminase in relation to the catalytic reaction; the results are pertinent to the mode of binding of PLP to the enzyme protein, and their interaction.

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