scholarly journals Crystal Structure of the E1 Component of the Escherichia coli 2-Oxoglutarate Dehydrogenase Multienzyme Complex

2007 ◽  
Vol 368 (3) ◽  
pp. 639-651 ◽  
Author(s):  
René A.W. Frank ◽  
Amanda J. Price ◽  
Fred D. Northrop ◽  
Richard N. Perham ◽  
Ben F. Luisi
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Multienzyme Complex ◽  
Oxoglutarate Dehydrogenase

Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex

1998 ◽  
Vol 280 (4) ◽  
pp. 655-668 ◽  
Author(s):  
James E Knapp ◽  
David T Mitchell ◽  
Mohammad A Yazdi ◽  
Stephen R Ernst ◽  
Lester J Reed ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Multienzyme Complex ◽  
Core Component ◽  
Oxoglutarate Dehydrogenase

scholarly journals Altering the substrate specificity of the Escherichia coli E1 Component of the 2‐Oxoglutarate Dehydrogenase Multienzyme Complex

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Da Jeong Shim ◽  
Natalia S. Nemeria ◽  
Anand Balakrishnan ◽  
Frank Jordan ◽  
Edgardo T. Farinas
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Multienzyme Complex ◽  
Oxoglutarate Dehydrogenase

scholarly journals Limited proteolysis and proton n.m.r. spectroscopy of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli

1981 ◽  
Vol 199 (3) ◽  
pp. 733-740 ◽  
Author(s):  
R N Perham ◽  
G C K Roberts
Keyword(s):  
Escherichia Coli ◽  
Lipoic Acid ◽  
Polypeptide Chain ◽  
Pyruvate Dehydrogenase Complex ◽  
Proton Nuclear Magnetic Resonance ◽  
Resonance Spectroscopy ◽  
Multienzyme Complex ◽  
Oxoglutarate Dehydrogenase ◽  
Polypeptide Chains ◽  
Dehydrogenase Complex

The 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli was treated with trypsin at pH 7.0 at 0 degrees C. Loss of the overall catalytic activity was accompanied by rapid cleavage of the lipoate succinyltransferase polypeptide chains, this apparent Mr falling from 50 000 to 36 000 as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. A slower shortening of the 2-oxoglutarate decarboxylase chains was also observed, whereas the lipoamide dehydrogenase chains were unaffected. The inactive trypsin-treated enzyme had lost the lipoic acid-containing regions of the lipoate succinyltransferase polypeptide chains, yet remained a highly assembled structure, as judged by gel filtration and electron microscopy. The lipoic acid-containing regions are therefore likely to be physically exposed in the complex, protruding from the structural core formed by the lipoate succinyltransferase component between the subunits of the other component enzymes. Proton nuclear magnetic resonance spectroscopy of the 2-oxoglutarate dehydrogenase complex revealed the existence of substantial regions of polypeptide chain with remarkable intramolecular mobility, most of which were retained after removal of the lipoic acid-containing regions by treatment of the complex with trypsin. By analogy with the comparably mobile regions of the pyruvate dehydrogenase complex of E. coli, it is likely that the highly mobile regions of polypeptide chain in the 2-oxoglutarate complex are in the lipoate succinyltransferase component and encompass the lipoyl-lysine residues. It is clear, however, that the mobility of this polypeptide chain is not restricted to the immediate vicinity of these residues.

scholarly journals Detection of bacterial lipoic acid. A modified gas-chromatographic-mass-spectrometric procedure

1989 ◽  
Vol 258 (3) ◽  
pp. 749-754 ◽  
Author(s):  
K J Pratt ◽  
C Carles ◽  
T J Carne ◽  
M J Danson ◽  
K J Stevenson
Keyword(s):  
Escherichia Coli ◽  
Mass Spectrum ◽  
Lipoic Acid ◽  
Mass Spectrometric ◽  
Halobacterium Halobium ◽  
Multienzyme Complex ◽  
Whole Cells ◽  
Oxoglutarate Dehydrogenase ◽  
Covalent Chromatography ◽  
Chromatographic Mass

The detection of bacterial lipoic acid by a modified g.c.-m.s. procedure is reported. Cells were hydrolysed in HCl to release protein-bound lipoic acid, which, after extraction into benzene, was reduced with NaBH4. The dihydrolipic acid so generated was then isolated by covalent chromatography on dithiolspecific p-aminophenylarsenoxide-agarose and, after elution by 2,3-dimercaptopropane-1-sulphonic acid and extraction into benzene, was allowed to O2-oxidize to the disulphide form. The isolated lipoic acid was allowed to react with diazomethane, and the methyl ester so produced was detected by g.c.-m.s. Analysis of the mass spectrum showed the characteristic molecular ion and seven fragmentation ions, which, along with the identification of those ions retaining the two sulphur atoms, allows the definitive detection of lipoic acid. The methodology has been successfully tested with authentic lipoic acid, the 2-oxoglutarate dehydrogenase multienzyme complex and with whole cells of Escherichia coli. In addition, it has been used to search for and identify lipoic acid in the archaebacterium Halobacterium halobium. The significance of this discovery and the possible roles of the cofactor in H. halobium are discussed.

Crystal Structure of Murein-Tripeptide Amidase MpaA from Escherichia coli O157 at 2.6 Å Resolution

2017 ◽  
Vol 24 (2) ◽  
pp. 181-187 ◽  
Author(s):  
Yinliang Ma ◽  
Guohui Bai ◽  
Yaqi Cui ◽  
Jing Zhao ◽  
Zenglin Yuan ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Escherichia Coli O157
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