1972
DOI: 10.1007/978-3-642-65456-5_3
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Structure, Function and Dynamics of a Regulatory Enzyme — Aspartate Transcarbamylase

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Cited by 13 publications
(4 citation statements)
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“…Instead, one of the two proteins might regulate the activity of the other. The presencelabsence of one would affect the activity of the other, similar to the way in which the regulatory subunit of aspartate transcarbamoylase inhibits the activity of the catalytic subunit (Schachman, 1974). It appears plausible that CheC might regulate CheD in some way, because the phenotypes are exactly opposite: cheD mutants are very tumbly and are not 'excitable' by attractant; cheC mutants are quite smooth swimming and do not adapt to addition of attractant (Rosario, eta/., 1995).…”
Section: Discussionmentioning
confidence: 99%
“…Instead, one of the two proteins might regulate the activity of the other. The presencelabsence of one would affect the activity of the other, similar to the way in which the regulatory subunit of aspartate transcarbamoylase inhibits the activity of the catalytic subunit (Schachman, 1974). It appears plausible that CheC might regulate CheD in some way, because the phenotypes are exactly opposite: cheD mutants are very tumbly and are not 'excitable' by attractant; cheC mutants are quite smooth swimming and do not adapt to addition of attractant (Rosario, eta/., 1995).…”
Section: Discussionmentioning
confidence: 99%
“…The apparent ability of compensating mutations to occur in any phage-host pair of these components would seem puzzling. However, a possibly analogous observation has been made with the multimeric regulatory enzyme aspartate transcarbamylase: mutational changes in the regulatory subunit affect the specificity of the catalytic subunit active site, solely by interaction between the heterologous subunits (26). The recent identification of a host protein defined by a groE mutation (10, 11) should lead to more direct tests for the existence of a functional phage-host protein complex in head assembly.…”
Section: Discussionmentioning
confidence: 85%
“…Properties of its regulatory and catalytic subunits were investigated in detail by enzymology and physical chemistry. 19 The complete structure determined by X-ray diffraction shows that there are six catalytic and six regulatory subunits. 20 In agreement with these findings, Jean-Pierre Changeux in Jacques Monod's laboratory investigated the mechanism of the feedback inhibition of L-threonine deaminase discovered by Edward Adelberg and Umbarger , and from kinetic studies with extracts proposed that this enzyme has inhibitory sites in addition to catalytic ones.…”
Section: Major Mechanisms Of Regulationmentioning
confidence: 99%