Conformational mobility of polypeptide chains in the 2‐oxo acid dehydrogenase complexes from ox heart revealed by proton NMR spectroscopy

Wawrzynczak, Edward J.; Perham, Richard N.; Roberts, Gordon C. K.

doi:10.1016/0014-5793(81)80908-8

Cited by 23 publications

(14 citation statements)

References 24 publications

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“…The structure of E2 is consistent with these two properties, comprising a compact inner core domain containing the catalytic and subunitbinding sites, and one or more extended outer domains containing the lipoic acid moiety. Stretches of flexible polypeptide rich in alanine and proline residues link the different domains and contain trypsin-sensitive sites where E2 can be cleaved into separate functional domains [14,15].…”

Section: Introductionmentioning

confidence: 99%

Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis

et al. 1989

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Autoantibodies in the sera of patients with primary biliary cirrhosis, shown previously to recognise the E2 polypeptide of the mammalian pyruvate dehydrogenase complex (PDC), have been demonstrated to react with the E2 component of PDC from bacteria (E. coli) and yeast (S. cerevisiae). Limited tryptic digestion, which cleaves E2 into well-characterised domains, followed by Western blotting indicates that the main immunodominant region of PDC E2 lies within the lipoic acid-containing domains of the polypeptide.

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Section: Introductionmentioning

confidence: 99%

Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis

et al. 1989

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“…Similarly, since the incorporation of [14C]acetyl groups into partly El-inhibited pyruvate dehydrogenase complexes from E coli and ox heart did not increase significantly when the incubation time was lengthened from lOs to 45s, it is unlikely that intra-core migration of El subunits is contributing much to our measurements of active-site coupling. The most likely explanations remain those of some form of intramolecular transacetylation reaction (Bates et al, 1977;Collins & Reed, 1977) and the effects of the remarkable polypeptide-chain mobility discovered in the E2 cores Wawrzynczak et al, 1981;Berman et al, 1981;Stepp et al, 1981;Duckworth et al, 1982). Raising the temperature has already been demonstrated to increase the mobility of the lipoic acid residues of the E. coli pyruvate dehydrogenase complex, as measured by e.s.r.…”

Section: Discussionmentioning

confidence: 99%

“…spectroscopy of the E. coli complex Packman et al, 1982). Similar regions of polypeptide chain with high conformational mobility appear to exist in 2-oxo acid dehydrogenase complexes from all sources thus far examined (Wawrzynczak et al, 1981;Duckworth et al, 1982). They presumably underlie the mechanism of active-site coupling and obviate the need for exact stoicheiometric arrangement of active sites in the 2-oxo acid dehydrogenase complexes Berman et al, 1981;Stepp et al, 1981;Duckworth et al, 1982).…”

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Temperature-dependence of intramolecular coupling of active sites in pyruvate dehydrogenase multienzyme complexes

Packman¹,

Stanley²,

Perham³

1983

Biochemical Journal

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Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes of Escherichia coli, ox heart and Bacillus stearothermophilus was measured at various temperatures. As the temperature was raised, the extent of active-site coupling was found to increase, approaching a maximum near the physiological growth temperature of the organism. Under these conditions, a single pyruvate dehydrogenase (lipoamide) dimer appeared able to cause a rapid (20s) reductive acetylation of probably all 24 polypeptide chains in the dihydrolipoamide acetyltransferase core of the enzyme complex from E. coli at 37 degrees C, and of most if not all of the 60 polypeptide chains in the dihydrolipoamide acetyltransferase cores of the enzymes from ox heart and B. stearothermophilus at 37 degrees C and 60 degrees C respectively. Experiments designed to measure the inter-core and intra-core migration of enzyme subunits suggested that, in the bacterial enzymes at least, this was not a major contributor to active-site coupling.

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“…72 • Homo sapiens: isoform 1, 148 AA, SWP P62158. 73 • Chlamydomonas reinhardtii: isoform 1, 162 AA, SWP P04352. 74…”

Section: A M I N O a C I D S E Q U E N C E I N F O R M A T I O N Calmunclassified

Calmodulin Interactions withCa_v1 andCa_v2 Voltage‐Gated Calcium ChannelIQDomains

Kim

Findeisen

Minor

2004

Handbook of Metalloproteins

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Conformational mobility of polypeptide chains in the 2‐oxo acid dehydrogenase complexes from ox heart revealed by proton NMR spectroscopy

Cited by 23 publications

References 24 publications

Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis

Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis

Temperature-dependence of intramolecular coupling of active sites in pyruvate dehydrogenase multienzyme complexes

Calmodulin Interactions withCa_v1 andCa_v2 Voltage‐Gated Calcium ChannelIQDomains

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Conformational mobility of polypeptide chains in the 2‐oxo acid dehydrogenase complexes from ox heart revealed by proton NMR spectroscopy

Cited by 23 publications

References 24 publications

Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis

Characterisation of the reactivity of autoantibodies in primary biliary cirrhosis

Temperature-dependence of intramolecular coupling of active sites in pyruvate dehydrogenase multienzyme complexes

Calmodulin Interactions withCav1 andCav2 Voltage‐Gated Calcium ChannelIQDomains

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Product

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Calmodulin Interactions withCa_v1 andCa_v2 Voltage‐Gated Calcium ChannelIQDomains